FMO DATABASE

FMODB ID: 52NVZ

Calculation Name: 4G9M-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4G9M

Chain ID: A

ChEMBL ID:

UniProt ID: L8WGI4

Base Structure: X-ray

Registration Date: 2023-06-22

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	142
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1283828.951395
FMO2-HF: Nuclear repulsion	1231013.529185
FMO2-HF: Total energy	-52815.422209
FMO2-MP2: Total energy	-52973.782299

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:ALA)

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

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.
-0.319	1.061	0.015	-0.579	-0.816	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.005 / q_NPA : -0.015

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	3	ILE	0	0.020	0.010	3.586	-0.832	0.548	0.015	-0.579	-0.816	0.001
4	A	4	SER	0	-0.042	-0.022	5.673	0.726	0.726	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.010	0.010	8.683	-0.017	-0.017	0.000	0.000	0.000	0.000
6	A	6	PRO	0	0.023	0.028	10.484	0.092	0.092	0.000	0.000	0.000	0.000
7	A	7	ALA	0	0.012	0.008	13.314	0.022	0.022	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.040	0.016	16.305	-0.002	-0.002	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.041	-0.019	17.948	0.018	0.018	0.000	0.000	0.000	0.000
10	A	10	TYR	0	0.032	0.001	13.819	-0.049	-0.049	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.029	0.018	18.675	0.044	0.044	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.044	-0.016	18.709	-0.038	-0.038	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.930	0.964	19.472	0.303	0.303	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.052	0.056	20.442	-0.023	-0.023	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.040	-0.027	18.965	0.001	0.001	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.055	-0.040	21.639	0.013	0.013	0.000	0.000	0.000	0.000
17	A	17	THR	0	0.043	0.050	25.213	0.007	0.007	0.000	0.000	0.000	0.000
18	A	18	GLY	0	-0.041	-0.012	23.023	0.007	0.007	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.095	-0.059	24.090	0.002	0.002	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.035	-0.040	22.916	-0.021	-0.021	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.021	0.017	24.287	0.017	0.017	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.827	-0.898	26.131	-0.144	-0.144	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.036	0.035	29.146	0.004	0.004	0.000	0.000	0.000	0.000
24	A	24	TRP	0	0.081	0.040	31.784	0.003	0.003	0.000	0.000	0.000	0.000
25	A	25	ARG	1	0.914	0.960	34.824	0.104	0.104	0.000	0.000	0.000	0.000
26	A	26	GLY	0	-0.017	-0.037	33.180	0.002	0.002	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-0.972	-0.981	34.010	-0.085	-0.085	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.006	-0.010	36.091	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.002	0.020	37.081	0.002	0.002	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.741	-0.839	38.446	-0.103	-0.103	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.010	0.006	38.024	0.004	0.004	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.067	-0.039	35.851	0.001	0.001	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.033	0.012	35.506	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	34	ILE	0	0.005	0.003	29.220	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	35	GLN	0	-0.067	-0.049	31.119	0.008	0.008	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.025	0.015	28.795	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	37	TYR	0	-0.008	-0.019	28.655	0.015	0.015	0.000	0.000	0.000	0.000
38	A	38	LYS	1	0.979	0.986	28.044	0.109	0.109	0.000	0.000	0.000	0.000
39	A	39	SER	0	0.001	0.000	24.311	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	40	HIS	0	-0.036	-0.015	26.450	0.005	0.005	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.019	0.022	25.328	0.007	0.007	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.012	0.007	26.384	0.002	0.002	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.816	-0.927	27.013	-0.161	-0.161	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.083	-0.052	27.767	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.046	-0.029	25.785	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.878	0.958	22.266	0.168	0.168	0.000	0.000	0.000	0.000
47	A	47	TRP	0	-0.026	-0.028	22.458	0.022	0.022	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.890	0.946	21.381	0.137	0.137	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.003	0.019	16.643	0.018	0.018	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.945	0.963	20.011	0.168	0.168	0.000	0.000	0.000	0.000
51	A	51	TRP	0	0.049	0.026	15.888	0.018	0.018	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.049	-0.042	22.213	0.017	0.017	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.027	0.024	24.843	0.014	0.014	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.942	0.983	26.129	0.134	0.134	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.000	-0.004	25.495	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.006	-0.012	20.476	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	57	GLN	0	0.023	0.016	21.747	-0.017	-0.017	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.013	-0.001	20.094	0.002	0.002	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.039	-0.014	23.513	0.020	0.020	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.046	0.015	21.289	-0.018	-0.018	0.000	0.000	0.000	0.000
61	A	61	GLN	0	-0.010	-0.012	24.927	0.008	0.008	0.000	0.000	0.000	0.000
62	A	62	ASN	0	0.019	0.005	25.868	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.035	-0.024	24.319	0.010	0.010	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.908	0.976	27.523	0.117	0.117	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.028	0.029	30.930	0.006	0.006	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.010	0.010	30.680	0.007	0.007	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.042	-0.011	31.665	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	68	TYR	0	-0.012	-0.031	27.998	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.014	0.009	26.593	0.007	0.007	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.069	0.031	29.666	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.044	-0.047	32.863	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.015	0.021	35.411	0.005	0.005	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.008	-0.002	38.404	0.006	0.006	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.001	0.021	38.404	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	75	ILE	0	0.014	0.020	32.321	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	GLN	0	-0.018	-0.007	36.213	0.007	0.007	0.000	0.000	0.000	0.000
77	A	77	ASN	0	0.063	0.009	35.133	-0.012	-0.012	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.059	-0.032	35.615	0.006	0.006	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.043	0.012	36.307	0.004	0.004	0.000	0.000	0.000	0.000
80	A	80	ASN	0	0.014	-0.003	35.132	-0.011	-0.011	0.000	0.000	0.000	0.000
81	A	81	VAL	0	0.002	0.010	29.648	0.001	0.001	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.043	-0.019	33.083	0.002	0.002	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.024	0.014	32.992	-0.006	-0.006	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.018	-0.016	33.654	0.008	0.008	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.024	-0.050	34.007	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	86	THR	0	-0.071	-0.034	34.858	0.000	0.000	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.046	-0.015	29.658	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	88	VAL	0	-0.002	0.003	29.510	0.008	0.008	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.024	0.000	27.916	-0.012	-0.012	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.026	-0.027	24.215	0.002	0.002	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.811	-0.910	22.360	-0.227	-0.227	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.051	-0.023	17.025	0.007	0.007	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.015	0.013	18.187	-0.036	-0.036	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.020	-0.013	14.109	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.010	0.002	16.025	0.059	0.059	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.864	-0.918	15.672	-0.372	-0.372	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.883	0.944	16.125	0.245	0.245	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.028	-0.014	15.100	0.036	0.036	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.027	0.009	11.892	-0.041	-0.041	0.000	0.000	0.000	0.000
100	A	100	ALA	0	0.055	0.034	17.530	0.036	0.036	0.000	0.000	0.000	0.000
101	A	101	ILE	0	-0.024	-0.013	20.631	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.890	-0.955	22.856	-0.202	-0.202	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.025	0.007	25.489	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.011	-0.007	26.866	0.005	0.005	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.922	-0.967	28.069	-0.123	-0.123	0.000	0.000	0.000	0.000
106	A	106	HIS	0	-0.110	-0.065	30.942	0.012	0.012	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.973	0.988	26.368	0.169	0.169	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.006	0.014	28.434	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	109	PHE	0	-0.058	-0.030	30.339	0.000	0.000	0.000	0.000	0.000	0.000
110	A	110	VAL	0	0.027	0.018	25.596	-0.009	-0.009	0.000	0.000	0.000	0.000
111	A	111	LEU	0	-0.011	-0.009	25.181	0.013	0.013	0.000	0.000	0.000	0.000
112	A	112	ASP	-1	-0.843	-0.919	26.498	-0.173	-0.173	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.028	-0.004	27.617	0.008	0.008	0.000	0.000	0.000	0.000
114	A	114	LYS	1	1.029	1.006	29.567	0.109	0.109	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.937	-0.981	33.150	-0.105	-0.105	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.016	-0.005	29.680	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	117	ASN	0	-0.004	0.006	30.718	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	118	PRO	0	0.011	-0.012	29.855	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.043	-0.003	31.130	0.000	0.000	0.000	0.000	0.000	0.000
120	A	120	ASN	0	0.009	-0.009	32.573	-0.013	-0.013	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.934	-0.974	33.499	-0.094	-0.094	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.029	0.008	32.440	0.007	0.007	0.000	0.000	0.000	0.000
123	A	123	PRO	0	0.028	0.012	32.789	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	124	VAL	0	0.007	0.007	28.614	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	125	ILE	0	-0.034	-0.021	31.444	0.009	0.009	0.000	0.000	0.000	0.000
126	A	126	TYR	0	0.010	-0.012	29.983	-0.015	-0.015	0.000	0.000	0.000	0.000
127	A	127	TYR	0	0.001	-0.023	31.091	0.015	0.015	0.000	0.000	0.000	0.000
128	A	128	ASN	0	-0.019	0.006	30.762	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	129	ASN	0	0.033	0.011	24.387	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	130	ASN	0	-0.022	-0.015	28.629	0.010	0.010	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.008	0.012	23.442	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	132	THR	0	0.016	-0.005	24.961	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	133	ASP	-1	-0.774	-0.910	22.900	-0.263	-0.263	0.000	0.000	0.000	0.000
134	A	134	ASN	0	-0.035	-0.001	23.885	-0.020	-0.020	0.000	0.000	0.000	0.000
135	A	135	GLN	0	-0.068	-0.031	25.349	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	136	LYS	1	0.771	0.895	19.904	0.261	0.261	0.000	0.000	0.000	0.000
137	A	137	TRP	0	-0.010	-0.017	19.788	0.016	0.016	0.000	0.000	0.000	0.000
138	A	138	LYS	1	0.914	0.943	15.320	0.370	0.370	0.000	0.000	0.000	0.000
139	A	139	PHE	0	0.034	0.013	14.351	0.048	0.048	0.000	0.000	0.000	0.000
140	A	140	ILE	0	-0.060	-0.037	13.729	-0.073	-0.073	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.892	-0.936	12.854	-0.432	-0.432	0.000	0.000	0.000	0.000
142	A	142	GLU	-1	-0.914	-0.950	14.846	-0.271	-0.271	0.000	0.000	0.000	0.000

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