FMO DATABASE

FMODB ID: 5JGYZ

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	OptHSide
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	-1351151.892925
FMO2-HF: Nuclear repulsion	1294992.42148
FMO2-HF: Total energy	-56159.471445
FMO2-MP2: Total energy	-56322.20041

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.
50.843	57.424	2.462	-3.879	-5.165	0.023

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 : -0.915 / q_NPA : -0.965

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	0.919	0.957	3.144	-42.066	-38.886	0.250	-1.543	-1.888	0.010
4	A	5	GLU	-1	-0.957	-0.958	2.301	33.804	36.337	2.206	-1.995	-2.743	0.012
5	A	6	PHE	0	-0.007	-0.010	3.664	-9.238	-8.370	0.006	-0.341	-0.534	0.001
6	A	7	ALA	0	0.011	-0.002	5.640	-5.766	-5.766	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.858	0.896	6.802	-31.590	-31.590	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.022	-0.001	7.774	-3.622	-3.622	0.000	0.000	0.000	0.000
9	A	10	GLN	0	-0.040	-0.026	9.535	-2.122	-2.122	0.000	0.000	0.000	0.000
10	A	11	MET	0	0.003	0.008	11.540	-1.546	-1.546	0.000	0.000	0.000	0.000
11	A	12	GLN	0	0.033	0.008	12.524	-1.314	-1.314	0.000	0.000	0.000	0.000
12	A	13	ALA	0	-0.007	-0.007	13.784	-1.575	-1.575	0.000	0.000	0.000	0.000
13	A	14	ALA	0	-0.017	-0.005	15.696	-1.294	-1.294	0.000	0.000	0.000	0.000
14	A	15	CYS	0	-0.011	-0.003	16.894	-1.149	-1.149	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.045	-0.026	18.357	-0.764	-0.764	0.000	0.000	0.000	0.000
16	A	17	TYR	0	0.013	-0.002	19.883	-0.951	-0.951	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.011	-0.009	21.131	-0.800	-0.800	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.897	0.953	22.933	-11.914	-11.914	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.901	-0.927	22.840	12.777	12.777	0.000	0.000	0.000	0.000
20	A	21	LYS	1	0.770	0.882	24.918	-12.850	-12.850	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.048	-0.021	26.762	-0.764	-0.764	0.000	0.000	0.000	0.000
22	A	23	PRO	0	0.013	0.006	29.003	0.136	0.136	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.790	0.879	31.219	-9.419	-9.419	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.035	-0.020	25.914	0.033	0.033	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.805	-0.886	28.192	9.893	9.893	0.000	0.000	0.000	0.000
26	A	27	TRP	0	-0.017	-0.023	21.392	0.414	0.414	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.010	-0.001	21.040	-0.201	-0.201	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.023	0.012	19.406	0.556	0.556	0.000	0.000	0.000	0.000
29	A	30	PHE	0	-0.003	-0.009	15.874	-0.268	-0.268	0.000	0.000	0.000	0.000
30	A	31	TYR	0	0.007	-0.007	16.641	0.796	0.796	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.014	-0.020	13.418	-0.167	-0.167	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.033	-0.019	16.477	-0.389	-0.389	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.817	-0.907	12.034	21.521	21.521	0.000	0.000	0.000	0.000
34	A	35	HIS	0	-0.045	-0.041	14.934	-0.639	-0.639	0.000	0.000	0.000	0.000
35	A	36	GLY	0	-0.030	-0.022	18.984	-0.594	-0.594	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.873	0.938	20.090	-13.289	-13.289	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.007	0.023	19.329	0.787	0.787	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.851	0.925	15.059	-17.530	-17.530	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.032	0.003	16.504	0.552	0.552	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.805	-0.888	10.692	24.990	24.990	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.034	-0.020	12.369	1.532	1.532	0.000	0.000	0.000	0.000
42	A	43	PHE	0	-0.003	0.002	14.882	-0.850	-0.850	0.000	0.000	0.000	0.000
43	A	44	VAL	0	-0.031	-0.005	18.155	0.453	0.453	0.000	0.000	0.000	0.000
44	A	45	GLY	0	0.039	0.013	20.766	-0.486	-0.486	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.947	-0.964	23.366	10.565	10.565	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.928	0.951	20.969	-12.751	-12.751	0.000	0.000	0.000	0.000
47	A	48	THR	0	0.091	0.058	21.945	-0.569	-0.569	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.911	-0.957	23.279	10.895	10.895	0.000	0.000	0.000	0.000
49	A	50	HIS	0	-0.045	-0.021	24.290	0.221	0.221	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.012	0.015	17.881	0.321	0.321	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.875	-0.942	19.215	14.485	14.485	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.021	0.017	21.178	-0.560	-0.560	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.088	-0.049	23.645	0.540	0.540	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.010	0.001	24.530	-0.296	-0.296	0.000	0.000	0.000	0.000
55	A	56	GLY	0	-0.042	-0.037	26.702	-0.325	-0.325	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.895	-0.937	28.550	9.516	9.516	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.064	0.028	28.462	0.397	0.397	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.045	-0.031	29.979	-0.050	-0.050	0.000	0.000	0.000	0.000
59	A	60	CYS	0	0.069	0.041	24.509	-0.009	-0.009	0.000	0.000	0.000	0.000
60	A	61	SER	0	0.027	0.003	25.762	0.362	0.362	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.092	-0.040	27.391	-0.082	-0.082	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.054	0.033	26.547	-0.158	-0.158	0.000	0.000	0.000	0.000
63	A	64	VAL	0	0.004	0.003	22.555	0.003	0.003	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.048	-0.012	25.925	-0.134	-0.134	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.787	0.875	28.825	-9.643	-9.643	0.000	0.000	0.000	0.000
66	A	67	ASN	0	0.019	0.026	25.911	-0.312	-0.312	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.852	-0.915	28.721	9.650	9.650	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.025	-0.008	28.726	0.198	0.198	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.036	-0.007	29.707	-0.407	-0.407	0.000	0.000	0.000	0.000
70	A	71	ASN	0	-0.055	-0.059	30.899	0.298	0.298	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.798	-0.863	33.322	7.898	7.898	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.006	-0.009	35.136	0.081	0.081	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.796	-0.929	37.696	7.329	7.329	0.000	0.000	0.000	0.000
74	A	75	VAL	0	0.017	0.025	33.732	-0.161	-0.161	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.898	0.962	36.857	-8.215	-8.215	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.077	-0.037	39.847	-0.109	-0.109	0.000	0.000	0.000	0.000
77	A	78	ASN	0	-0.015	-0.022	36.242	-0.055	-0.055	0.000	0.000	0.000	0.000
78	A	79	PRO	0	-0.018	-0.019	37.345	0.154	0.154	0.000	0.000	0.000	0.000
79	A	80	LYS	1	0.923	0.964	33.759	-8.429	-8.429	0.000	0.000	0.000	0.000
80	A	81	TYR	0	-0.019	-0.004	31.967	0.132	0.132	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.024	-0.002	28.495	-0.191	-0.191	0.000	0.000	0.000	0.000
82	A	83	ALA	0	-0.014	-0.001	30.504	0.199	0.199	0.000	0.000	0.000	0.000
83	A	84	CYS	0	0.003	0.008	26.849	0.022	0.022	0.000	0.000	0.000	0.000
84	A	85	PHE	0	0.047	0.010	25.101	0.108	0.108	0.000	0.000	0.000	0.000
85	A	86	PRO	0	-0.050	-0.014	31.070	-0.206	-0.206	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.060	-0.047	33.562	-0.270	-0.270	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.023	0.001	30.468	-0.250	-0.250	0.000	0.000	0.000	0.000
88	A	89	GLN	0	-0.114	-0.099	33.834	-0.457	-0.457	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.044	-0.031	34.020	-0.263	-0.263	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.841	-0.926	28.688	10.364	10.364	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.064	-0.036	28.030	-0.282	-0.282	0.000	0.000	0.000	0.000
92	A	93	VAL	0	0.015	0.020	25.030	0.381	0.381	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.006	-0.013	24.693	-0.401	-0.401	0.000	0.000	0.000	0.000
94	A	95	PRO	0	-0.012	0.007	23.517	0.664	0.664	0.000	0.000	0.000	0.000
95	A	96	VAL	0	0.006	0.004	17.730	0.063	0.063	0.000	0.000	0.000	0.000
96	A	97	ARG	1	0.840	0.901	20.609	-11.208	-11.208	0.000	0.000	0.000	0.000
97	A	98	TYR	0	0.022	0.007	15.659	0.295	0.295	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.020	-0.020	19.982	-0.239	-0.239	0.000	0.000	0.000	0.000
99	A	100	GLY	0	0.005	0.018	22.552	-0.302	-0.302	0.000	0.000	0.000	0.000
100	A	101	GLU	-1	-0.788	-0.876	21.281	13.085	13.085	0.000	0.000	0.000	0.000
101	A	102	PRO	0	-0.019	-0.010	21.895	0.546	0.546	0.000	0.000	0.000	0.000
102	A	103	ILE	0	-0.041	-0.024	15.793	0.137	0.137	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.047	0.017	17.544	0.842	0.842	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.866	-0.938	19.088	12.004	12.004	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.050	-0.030	19.917	0.678	0.678	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.822	-0.922	21.717	11.354	11.354	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.012	-0.014	23.585	0.407	0.407	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.780	-0.869	26.189	10.079	10.079	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.052	-0.059	28.989	0.007	0.007	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.754	-0.867	31.992	8.998	8.998	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.813	0.926	34.851	-8.506	-8.506	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.864	0.959	36.337	-7.238	-7.238	0.000	0.000	0.000	0.000
113	A	114	ALA	0	-0.001	-0.015	38.166	-0.051	-0.051	0.000	0.000	0.000	0.000
114	A	115	ALA	0	-0.083	-0.036	34.000	-0.087	-0.087	0.000	0.000	0.000	0.000
115	A	116	PHE	0	0.012	0.003	29.996	0.028	0.028	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.015	-0.031	34.376	-0.156	-0.156	0.000	0.000	0.000	0.000
117	A	118	LYS	1	0.859	0.899	34.429	-8.375	-8.375	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.841	-0.889	34.297	8.740	8.740	0.000	0.000	0.000	0.000
119	A	120	ASP	-1	-0.728	-0.822	30.903	10.078	10.078	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.742	-0.856	29.907	9.341	9.341	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.021	0.005	30.017	0.321	0.321	0.000	0.000	0.000	0.000
122	A	123	MET	0	-0.008	-0.007	26.909	0.376	0.376	0.000	0.000	0.000	0.000
123	A	124	LEU	0	0.027	0.009	25.013	0.562	0.562	0.000	0.000	0.000	0.000
124	A	125	SER	0	0.028	0.003	24.688	0.570	0.570	0.000	0.000	0.000	0.000
125	A	126	SER	0	-0.045	-0.018	25.117	0.281	0.281	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.022	-0.021	20.933	0.592	0.592	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.031	0.011	20.696	0.904	0.904	0.000	0.000	0.000	0.000
128	A	129	ASP	-1	-0.917	-0.961	20.168	13.722	13.722	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.108	-0.050	19.991	0.773	0.773	0.000	0.000	0.000	0.000
130	A	131	MET	0	-0.027	-0.007	14.421	1.174	1.174	0.000	0.000	0.000	0.000
131	A	132	ALA	0	0.048	0.037	15.479	1.488	1.488	0.000	0.000	0.000	0.000
132	A	133	PRO	0	-0.063	-0.050	14.453	0.766	0.766	0.000	0.000	0.000	0.000
133	A	134	LEU	0	0.006	0.006	10.525	1.640	1.640	0.000	0.000	0.000	0.000
134	A	135	VAL	0	0.060	0.024	10.923	1.732	1.732	0.000	0.000	0.000	0.000
135	A	136	HIS	1	0.900	0.962	12.307	-20.568	-20.568	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.911	-0.946	7.479	33.111	33.111	0.000	0.000	0.000	0.000
137	A	138	PHE	0	-0.059	-0.053	7.094	2.840	2.840	0.000	0.000	0.000	0.000
138	A	139	PHE	0	-0.026	0.014	10.606	-1.599	-1.599	0.000	0.000	0.000	0.000
139	A	140	VAL	0	-0.045	-0.016	12.511	0.818	0.818	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.801	0.891	15.046	-14.456	-14.456	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.008	-0.008	18.674	-0.009	-0.009	0.000	0.000	0.000	0.000

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