FMO DATABASE

FMODB ID: 5J6MZ

Calculation Name: 4GA2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4GA2

Chain ID: A

ChEMBL ID:

UniProt ID: H2QII6

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:

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	144
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1327721.262805
FMO2-HF: Nuclear repulsion	1269306.144195
FMO2-HF: Total energy	-58415.11861
FMO2-MP2: Total energy	-58586.634666

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:ARG)

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

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.
15.609	17.591	-0.02	-1.004	-0.958	0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.980 / q_NPA : 0.988

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	SER	0	-0.002	-0.024	3.875	0.214	2.147	-0.019	-1.002	-0.912	0.004
4	A	5	LYS	1	0.887	0.919	6.630	20.883	20.883	0.000	0.000	0.000	0.000
5	A	6	ALA	0	0.099	0.053	10.292	1.073	1.073	0.000	0.000	0.000	0.000
6	A	7	ASP	-1	-0.821	-0.879	6.889	-29.005	-29.005	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.044	-0.013	9.631	1.097	1.097	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.898	-0.962	11.860	-16.435	-16.435	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.885	0.934	9.552	23.559	23.559	0.000	0.000	0.000	0.000
10	A	11	TYR	0	0.012	0.018	13.641	1.169	1.169	0.000	0.000	0.000	0.000
11	A	12	ILE	0	0.025	0.017	15.455	1.013	1.013	0.000	0.000	0.000	0.000
12	A	13	ALA	0	0.016	0.011	17.893	0.835	0.835	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.040	-0.029	18.141	0.637	0.637	0.000	0.000	0.000	0.000
14	A	15	VAL	0	-0.015	-0.002	18.928	0.612	0.612	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.012	0.003	21.496	0.580	0.580	0.000	0.000	0.000	0.000
16	A	17	GLY	0	0.018	0.015	23.234	0.490	0.490	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.023	-0.008	23.299	0.345	0.345	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.098	-0.053	24.333	0.262	0.262	0.000	0.000	0.000	0.000
19	A	20	PRO	0	0.077	0.043	25.942	-0.206	-0.206	0.000	0.000	0.000	0.000
20	A	21	SER	0	-0.002	-0.027	27.805	0.057	0.057	0.000	0.000	0.000	0.000
21	A	22	PRO	0	0.046	-0.005	27.588	-0.342	-0.342	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.954	0.959	26.892	9.016	9.016	0.000	0.000	0.000	0.000
23	A	24	GLN	0	0.055	0.046	25.914	-0.178	-0.178	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.882	0.943	22.754	10.105	10.105	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.006	0.006	22.074	-0.407	-0.407	0.000	0.000	0.000	0.000
26	A	27	ILE	0	-0.050	-0.020	22.785	-0.299	-0.299	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.929	0.963	18.879	12.803	12.803	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.056	0.041	18.185	-0.735	-0.735	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.037	0.006	17.244	-0.779	-0.779	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.040	-0.013	14.948	-0.424	-0.424	0.000	0.000	0.000	0.000
31	A	32	PHE	0	0.029	0.003	13.373	-1.051	-1.051	0.000	0.000	0.000	0.000
32	A	33	ALA	0	0.036	0.021	13.030	-1.019	-1.019	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.853	0.942	11.361	14.441	14.441	0.000	0.000	0.000	0.000
34	A	35	LEU	0	0.012	0.008	8.705	-1.310	-1.310	0.000	0.000	0.000	0.000
35	A	36	TYR	0	0.047	-0.004	8.316	-1.589	-1.589	0.000	0.000	0.000	0.000
36	A	37	TYR	0	0.004	0.019	9.537	-1.170	-1.170	0.000	0.000	0.000	0.000
37	A	38	GLU	-1	-0.856	-0.907	4.745	-29.598	-29.549	-0.001	-0.002	-0.046	0.000
38	A	39	ALA	0	-0.065	-0.026	5.268	-2.982	-2.982	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.890	0.954	5.708	30.108	30.108	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.799	-0.879	9.141	-19.473	-19.473	0.000	0.000	0.000	0.000
41	A	42	TYR	0	0.050	-0.005	11.145	0.585	0.585	0.000	0.000	0.000	0.000
42	A	43	ASP	-1	-0.841	-0.913	14.409	-12.779	-12.779	0.000	0.000	0.000	0.000
43	A	44	LEU	0	0.000	0.002	14.155	0.745	0.745	0.000	0.000	0.000	0.000
44	A	45	ALA	0	-0.033	-0.014	13.432	0.468	0.468	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.879	0.929	15.438	13.942	13.942	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.952	0.988	19.051	13.392	13.392	0.000	0.000	0.000	0.000
47	A	48	TYR	0	0.015	-0.002	16.668	0.834	0.834	0.000	0.000	0.000	0.000
48	A	49	ILE	0	0.022	0.024	18.333	0.398	0.398	0.000	0.000	0.000	0.000
49	A	50	CYS	0	0.007	0.012	20.040	0.598	0.598	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.056	-0.035	21.775	0.285	0.285	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.051	-0.057	21.542	0.350	0.350	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.016	0.005	23.295	0.406	0.406	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.054	-0.033	25.776	0.194	0.194	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.035	-0.013	26.381	0.310	0.310	0.000	0.000	0.000	0.000
55	A	56	GLN	0	-0.023	0.002	25.426	0.472	0.472	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.792	-0.880	27.457	-8.603	-8.603	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.942	0.962	29.609	8.166	8.166	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.773	-0.862	23.433	-11.179	-11.179	0.000	0.000	0.000	0.000
59	A	60	PRO	0	0.044	0.024	25.548	-0.219	-0.219	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.965	0.988	20.792	11.249	11.249	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.010	0.001	20.739	-0.483	-0.483	0.000	0.000	0.000	0.000
62	A	63	HIS	0	0.006	-0.010	21.426	-0.476	-0.476	0.000	0.000	0.000	0.000
63	A	64	ARG	1	0.841	0.900	20.865	11.478	11.478	0.000	0.000	0.000	0.000
64	A	65	PHE	0	-0.026	-0.018	13.005	-0.353	-0.353	0.000	0.000	0.000	0.000
65	A	66	LEU	0	0.016	-0.001	18.341	-0.472	-0.472	0.000	0.000	0.000	0.000
66	A	67	GLY	0	0.033	0.014	20.602	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	68	LEU	0	0.002	0.011	14.822	-0.094	-0.094	0.000	0.000	0.000	0.000
68	A	69	LEU	0	-0.060	-0.045	14.623	-0.545	-0.545	0.000	0.000	0.000	0.000
69	A	70	TYR	0	0.001	-0.002	17.917	-0.155	-0.155	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.794	-0.880	20.442	-12.221	-12.221	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.057	-0.037	14.390	-0.244	-0.244	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.853	-0.910	18.458	-13.577	-13.577	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.801	-0.873	20.739	-11.476	-11.476	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.033	-0.001	23.386	0.906	0.906	0.000	0.000	0.000	0.000
75	A	76	THR	0	0.020	-0.023	25.257	-0.063	-0.063	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.794	-0.879	27.651	-9.011	-9.011	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.825	0.896	25.714	9.691	9.691	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.041	0.019	24.066	-0.074	-0.074	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.013	0.007	25.283	0.059	0.059	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.842	-0.894	28.714	-9.055	-9.055	0.000	0.000	0.000	0.000
81	A	82	CYS	0	-0.070	-0.021	24.550	0.101	0.101	0.000	0.000	0.000	0.000
82	A	83	TYR	0	-0.028	-0.056	21.572	0.006	0.006	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.928	0.958	26.870	8.267	8.267	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.855	0.922	28.625	8.701	8.701	0.000	0.000	0.000	0.000
85	A	86	SER	0	0.009	-0.027	25.346	0.136	0.136	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.053	-0.024	27.885	0.141	0.141	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.875	-0.931	30.763	-8.058	-8.058	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.089	-0.020	29.010	0.194	0.194	0.000	0.000	0.000	0.000
89	A	90	ASN	0	-0.012	0.009	27.719	0.293	0.293	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.049	0.024	30.479	-0.210	-0.210	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.060	-0.043	30.572	-0.054	-0.054	0.000	0.000	0.000	0.000
92	A	93	GLN	0	-0.020	0.005	25.389	-0.486	-0.486	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.912	0.934	29.240	8.149	8.149	0.000	0.000	0.000	0.000
94	A	95	ASP	-1	-0.781	-0.880	24.973	-10.671	-10.671	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.001	0.006	23.965	-0.129	-0.129	0.000	0.000	0.000	0.000
96	A	97	VAL	0	-0.043	-0.019	27.713	0.094	0.094	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.006	0.008	29.128	0.166	0.166	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.841	0.929	23.205	11.785	11.785	0.000	0.000	0.000	0.000
99	A	100	ILE	0	0.000	-0.009	27.670	-0.073	-0.073	0.000	0.000	0.000	0.000
100	A	101	ALA	0	-0.001	0.003	29.940	0.109	0.109	0.000	0.000	0.000	0.000
101	A	102	GLU	-1	-0.879	-0.941	26.630	-10.687	-10.687	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.038	-0.026	24.585	-0.015	-0.015	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.010	-0.002	28.693	0.049	0.049	0.000	0.000	0.000	0.000
104	A	105	CYS	0	-0.018	-0.006	32.313	0.155	0.155	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.772	0.875	25.452	11.263	11.263	0.000	0.000	0.000	0.000
106	A	107	ASN	0	-0.042	-0.002	30.209	-0.344	-0.344	0.000	0.000	0.000	0.000
107	A	108	ASP	-1	-0.816	-0.900	31.783	-7.960	-7.960	0.000	0.000	0.000	0.000
108	A	109	VAL	0	-0.025	-0.017	35.547	-0.048	-0.048	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.049	-0.032	38.560	0.254	0.254	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.783	-0.870	36.792	-7.908	-7.908	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.026	0.018	40.349	0.098	0.098	0.000	0.000	0.000	0.000
112	A	113	ARG	1	0.684	0.800	33.648	8.457	8.457	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.046	0.016	36.117	-0.041	-0.041	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.944	0.951	37.147	6.675	6.675	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.012	-0.002	37.362	-0.033	-0.033	0.000	0.000	0.000	0.000
116	A	117	TRP	0	0.021	-0.009	33.103	-0.025	-0.025	0.000	0.000	0.000	0.000
117	A	118	VAL	0	0.047	0.037	35.973	-0.105	-0.105	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.823	-0.892	37.212	-6.833	-6.833	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.869	0.954	34.660	8.185	8.185	0.000	0.000	0.000	0.000
120	A	121	ALA	0	0.025	0.002	34.219	0.011	0.011	0.000	0.000	0.000	0.000
121	A	122	ALA	0	0.005	0.005	35.842	-0.033	-0.033	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.901	0.938	38.811	7.078	7.078	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.058	-0.017	34.446	0.036	0.036	0.000	0.000	0.000	0.000
124	A	125	PHE	0	-0.017	-0.011	30.460	-0.128	-0.128	0.000	0.000	0.000	0.000
125	A	126	PRO	0	0.045	0.016	36.400	-0.023	-0.023	0.000	0.000	0.000	0.000
126	A	127	GLY	0	0.034	0.025	39.287	-0.057	-0.057	0.000	0.000	0.000	0.000
127	A	128	SER	0	-0.009	0.000	33.634	-0.116	-0.116	0.000	0.000	0.000	0.000
128	A	129	PRO	0	0.060	0.022	34.464	0.046	0.046	0.000	0.000	0.000	0.000
129	A	130	ALA	0	-0.003	0.003	31.406	-0.022	-0.022	0.000	0.000	0.000	0.000
130	A	131	VAL	0	-0.009	-0.012	33.377	-0.054	-0.054	0.000	0.000	0.000	0.000
131	A	132	TYR	0	-0.013	-0.007	35.774	0.111	0.111	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.993	1.008	31.916	9.404	9.404	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.059	-0.032	32.402	-0.010	-0.010	0.000	0.000	0.000	0.000
134	A	135	LYS	1	0.796	0.877	36.504	6.969	6.969	0.000	0.000	0.000	0.000
135	A	136	GLU	-1	-0.904	-0.956	39.453	-7.579	-7.579	0.000	0.000	0.000	0.000
136	A	137	GLN	0	0.051	0.024	34.158	-0.133	-0.133	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.074	-0.029	38.892	0.051	0.051	0.000	0.000	0.000	0.000
138	A	139	LEU	0	0.003	-0.009	41.409	0.127	0.127	0.000	0.000	0.000	0.000
139	A	140	ASP	-1	-0.922	-0.950	41.357	-7.310	-7.310	0.000	0.000	0.000	0.000
140	A	141	CYS	0	-0.141	-0.071	41.591	-0.015	-0.015	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.841	-0.905	44.220	-6.711	-6.711	0.000	0.000	0.000	0.000
142	A	143	GLY	0	-0.019	0.000	46.752	0.030	0.030	0.000	0.000	0.000	0.000
143	A	144	GLU	-1	-0.960	-0.979	49.879	-5.841	-5.841	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-1.019	-1.004	53.407	-5.545	-5.545	0.000	0.000	0.000	0.000

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