FMO DATABASE

FMODB ID: 4JG6N

Calculation Name: 4MMN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4MMN

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HJW5

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1351800.122482
FMO2-HF: Nuclear repulsion	1295641.707589
FMO2-HF: Total energy	-56158.414893
FMO2-MP2: Total energy	-56321.188528

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:ASP)

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

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.
57.539	64.45	2.576	-4.058	-5.429	0.011

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.925 / q_NPA : -0.963

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	LYS	1	0.943	0.983	3.137	-45.085	-41.957	0.291	-1.565	-1.855	0.012
4	A	5	GLU	-1	-0.949	-0.958	2.261	40.533	43.375	2.278	-2.158	-2.962	-0.002
5	A	6	PHE	0	0.005	-0.004	3.649	-8.740	-7.799	0.007	-0.335	-0.612	0.001
6	A	7	ALA	0	0.017	-0.004	5.642	-5.899	-5.899	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.882	0.920	6.375	-30.781	-30.781	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.038	-0.005	7.780	-3.635	-3.635	0.000	0.000	0.000	0.000
9	A	10	GLN	0	-0.030	-0.022	9.540	-1.685	-1.685	0.000	0.000	0.000	0.000
10	A	11	MET	0	0.000	0.008	11.549	-1.545	-1.545	0.000	0.000	0.000	0.000
11	A	12	GLN	0	0.006	0.001	12.532	-0.935	-0.935	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.002	-0.002	13.787	-1.556	-1.556	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.020	-0.006	15.700	-1.286	-1.286	0.000	0.000	0.000	0.000
14	A	15	CYS	0	-0.010	0.005	16.937	-1.172	-1.172	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.041	-0.009	18.363	-0.562	-0.562	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.026	0.004	19.888	-0.989	-0.989	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.026	-0.013	21.468	-0.807	-0.807	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.856	0.918	22.939	-12.041	-12.041	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.972	-0.982	22.840	12.861	12.861	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.857	0.935	25.768	-12.112	-12.112	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.051	-0.025	26.902	-0.777	-0.777	0.000	0.000	0.000	0.000
22	A	23	PRO	0	0.019	0.017	29.010	0.134	0.134	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.794	0.872	31.226	-9.390	-9.390	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.017	-0.002	25.936	0.011	0.011	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.786	-0.860	28.117	9.838	9.838	0.000	0.000	0.000	0.000
26	A	27	TRP	0	-0.035	-0.025	20.946	0.420	0.420	0.000	0.000	0.000	0.000
27	A	28	VAL	0	0.005	0.000	20.712	-0.202	-0.202	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.020	0.011	19.027	0.571	0.571	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.008	-0.011	15.635	-0.270	-0.270	0.000	0.000	0.000	0.000
30	A	31	TYR	0	0.008	0.002	16.365	0.778	0.778	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.011	-0.015	13.428	-0.241	-0.241	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.034	-0.019	16.434	-0.411	-0.411	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.847	-0.948	12.902	20.620	20.620	0.000	0.000	0.000	0.000
34	A	35	HIS	0	-0.067	-0.048	15.459	-0.599	-0.599	0.000	0.000	0.000	0.000
35	A	36	GLY	0	-0.047	-0.032	19.216	-0.592	-0.592	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.929	0.974	20.038	-12.912	-12.912	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.025	0.032	19.228	0.734	0.734	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.938	0.985	15.391	-16.945	-16.945	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.018	0.009	16.224	0.511	0.511	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.850	-0.907	10.668	23.108	23.108	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.041	-0.032	11.889	1.563	1.563	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.020	-0.011	14.417	-0.831	-0.831	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.002	-0.001	17.857	0.514	0.514	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.034	0.006	20.546	-0.497	-0.497	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.954	-0.968	22.936	10.574	10.574	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.918	0.944	20.462	-12.714	-12.714	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.100	0.062	21.443	-0.566	-0.566	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.907	-0.958	22.789	10.910	10.910	0.000	0.000	0.000	0.000
49	A	50	HIS	0	-0.049	-0.025	23.819	0.226	0.226	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.004	0.004	17.379	0.291	0.291	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.917	-0.971	18.763	14.376	14.376	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.018	0.016	20.768	-0.567	-0.567	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.060	-0.035	23.391	0.547	0.547	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.002	0.004	24.273	-0.292	-0.292	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.055	-0.040	26.569	-0.319	-0.319	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.905	-0.945	28.405	9.318	9.318	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.054	0.056	28.222	0.403	0.403	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.017	-0.023	29.706	-0.049	-0.049	0.000	0.000	0.000	0.000
59	A	60	CYS	0	0.040	0.036	24.361	0.147	0.147	0.000	0.000	0.000	0.000
60	A	61	SER	0	-0.005	-0.048	25.660	0.348	0.348	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.093	-0.042	27.281	-0.095	-0.095	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.059	0.035	26.457	-0.159	-0.159	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.002	0.000	22.685	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.083	-0.032	25.925	-0.135	-0.135	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.858	0.915	28.825	-9.198	-9.198	0.000	0.000	0.000	0.000
66	A	67	ASN	0	0.017	0.027	25.874	-0.250	-0.250	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.878	-0.928	28.721	9.444	9.444	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.004	0.005	28.562	0.212	0.212	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.041	-0.006	29.699	-0.398	-0.398	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.058	-0.056	30.807	0.309	0.309	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.813	-0.877	33.150	7.824	7.824	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.019	-0.014	34.894	0.038	0.038	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.877	-0.969	37.465	7.309	7.309	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.041	0.032	33.517	-0.147	-0.147	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.921	0.963	36.565	-7.898	-7.898	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.080	-0.036	39.477	-0.098	-0.098	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.010	-0.008	35.797	-0.076	-0.076	0.000	0.000	0.000	0.000
78	A	79	PRO	0	-0.025	-0.024	37.059	0.149	0.149	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.920	0.958	33.607	-8.326	-8.326	0.000	0.000	0.000	0.000
80	A	81	TYR	0	-0.023	-0.007	31.249	0.122	0.122	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.011	0.004	27.901	-0.194	-0.194	0.000	0.000	0.000	0.000
82	A	83	ALA	0	-0.028	-0.012	30.084	0.198	0.198	0.000	0.000	0.000	0.000
83	A	84	CYS	0	0.000	0.014	26.566	0.099	0.099	0.000	0.000	0.000	0.000
84	A	85	PHE	0	0.054	0.015	24.522	0.073	0.073	0.000	0.000	0.000	0.000
85	A	86	PRO	0	-0.058	-0.017	30.512	-0.223	-0.223	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.077	-0.077	33.161	-0.266	-0.266	0.000	0.000	0.000	0.000
87	A	88	THR	0	0.028	0.049	30.125	-0.070	-0.070	0.000	0.000	0.000	0.000
88	A	89	GLN	0	-0.128	-0.113	33.355	-0.447	-0.447	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.042	-0.013	34.001	-0.258	-0.258	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.848	-0.921	27.619	10.462	10.462	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.076	-0.037	27.737	-0.291	-0.291	0.000	0.000	0.000	0.000
92	A	93	VAL	0	0.030	0.023	25.019	0.359	0.359	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.017	-0.017	24.768	-0.389	-0.389	0.000	0.000	0.000	0.000
94	A	95	PRO	0	-0.004	0.009	23.517	0.643	0.643	0.000	0.000	0.000	0.000
95	A	96	VAL	0	0.015	0.005	17.719	0.059	0.059	0.000	0.000	0.000	0.000
96	A	97	ARG	1	0.815	0.881	20.609	-11.058	-11.058	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.025	0.009	16.279	0.787	0.787	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.023	-0.021	19.834	-0.359	-0.359	0.000	0.000	0.000	0.000
99	A	100	GLY	0	-0.002	0.013	22.794	-0.296	-0.296	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.900	-0.956	21.501	13.158	13.158	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.019	-0.008	22.022	0.519	0.519	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.039	-0.024	15.889	0.135	0.135	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.064	0.021	17.544	0.821	0.821	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.870	-0.941	19.088	11.872	11.872	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.042	-0.026	19.826	0.669	0.669	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.779	-0.902	21.619	11.206	11.206	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.018	-0.016	23.288	0.411	0.411	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.824	-0.898	25.893	10.332	10.332	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.046	-0.050	28.605	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.750	-0.855	31.588	9.013	9.013	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.839	0.943	34.400	-8.493	-8.493	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.960	0.985	35.975	-7.087	-7.087	0.000	0.000	0.000	0.000
113	A	114	ALA	0	-0.024	-0.033	37.940	-0.051	-0.051	0.000	0.000	0.000	0.000
114	A	115	ALA	0	-0.086	-0.027	33.740	-0.067	-0.067	0.000	0.000	0.000	0.000
115	A	116	PHE	0	-0.008	0.001	29.829	0.030	0.030	0.000	0.000	0.000	0.000
116	A	117	SER	0	0.006	0.011	34.210	-0.246	-0.246	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.975	0.969	34.394	-8.127	-8.127	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.861	-0.926	34.240	8.677	8.677	0.000	0.000	0.000	0.000
119	A	120	ASP	-1	-0.771	-0.861	30.953	9.957	9.957	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.824	-0.917	29.907	9.372	9.372	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.021	0.018	30.017	0.319	0.319	0.000	0.000	0.000	0.000
122	A	123	MET	0	-0.008	-0.009	26.806	0.344	0.344	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.017	0.008	25.156	0.548	0.548	0.000	0.000	0.000	0.000
124	A	125	SER	0	0.030	-0.016	24.688	0.551	0.551	0.000	0.000	0.000	0.000
125	A	126	SER	0	-0.047	-0.014	25.117	0.266	0.266	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.013	-0.017	20.886	0.576	0.576	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.029	0.011	20.693	0.884	0.884	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.915	-0.959	20.168	13.522	13.522	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.124	-0.058	20.034	0.746	0.746	0.000	0.000	0.000	0.000
130	A	131	MET	0	-0.025	-0.012	14.582	1.113	1.113	0.000	0.000	0.000	0.000
131	A	132	ALA	0	0.055	0.041	15.479	1.429	1.429	0.000	0.000	0.000	0.000
132	A	133	PRO	0	-0.055	-0.047	14.450	0.702	0.702	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.004	0.004	10.283	1.517	1.517	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.048	0.024	10.923	1.687	1.687	0.000	0.000	0.000	0.000
135	A	136	HIS	1	0.902	0.960	12.331	-19.488	-19.488	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.936	-0.960	7.561	32.743	32.743	0.000	0.000	0.000	0.000
137	A	138	PHE	0	-0.043	-0.045	6.942	2.987	2.987	0.000	0.000	0.000	0.000
138	A	139	PHE	0	-0.023	0.007	10.611	-1.594	-1.594	0.000	0.000	0.000	0.000
139	A	140	VAL	0	-0.032	-0.006	13.000	0.758	0.758	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.897	0.967	15.385	-13.910	-13.910	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.026	-0.020	19.072	-0.038	-0.038	0.000	0.000	0.000	0.000

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