FMO DATABASE

FMODB ID: M3LGZ

Calculation Name: 4B0M-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4B0M

Chain ID: A

ChEMBL ID:

UniProt ID: P26949

Base Structure: X-ray

Registration Date: 2023-03-14

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	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1109447.855472
FMO2-HF: Nuclear repulsion	1055591.933435
FMO2-HF: Total energy	-53855.922037
FMO2-MP2: Total energy	-54012.390468

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.
-1.999	0.117	-0.025	-1.095	-0.996	0.004

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 : 0.000 / q_NPA : -0.001

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

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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	THR	0	-0.034	-0.016	3.815	-0.792	1.324	-0.025	-1.095	-0.996	0.004
4	A	4	PHE	0	-0.021	-0.008	6.422	-0.024	-0.024	0.000	0.000	0.000	0.000
5	A	5	ASP	-1	-0.824	-0.900	10.189	-0.628	-0.628	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.019	-0.034	13.209	0.009	0.009	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.081	-0.044	16.397	0.063	0.063	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.082	-0.051	17.705	0.017	0.017	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.034	0.007	16.186	0.017	0.017	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.904	-0.950	20.150	-0.207	-0.207	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.046	-0.016	22.162	0.007	0.007	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.076	-0.076	24.708	0.007	0.007	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.052	-0.041	28.196	0.005	0.005	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.015	0.002	27.267	0.009	0.009	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.808	-0.866	24.825	-0.141	-0.141	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.050	-0.039	21.982	0.002	0.002	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.018	0.019	18.065	0.013	0.013	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.834	-0.878	15.969	-0.230	-0.230	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.004	-0.011	12.240	0.010	0.010	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.049	-0.047	11.753	-0.040	-0.040	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.002	-0.008	11.251	0.025	0.025	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.045	0.018	11.167	0.061	0.061	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.013	0.014	7.575	-0.201	-0.201	0.000	0.000	0.000	0.000
24	A	24	GLN	0	0.010	0.022	6.535	0.056	0.056	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.077	-0.020	8.522	0.127	0.127	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.086	-0.042	9.019	0.066	0.066	0.000	0.000	0.000	0.000
27	A	27	GLN	0	0.003	-0.012	12.699	-0.094	-0.094	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.032	0.019	15.563	0.018	0.018	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.004	0.008	18.576	0.014	0.014	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.046	0.031	21.630	-0.017	-0.017	0.000	0.000	0.000	0.000
31	A	31	ASN	0	-0.019	-0.017	24.662	0.018	0.018	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.038	-0.038	20.188	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.014	-0.004	25.638	0.008	0.008	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.022	0.013	24.861	0.001	0.001	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.027	-0.025	27.387	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.033	0.020	28.053	0.009	0.009	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.024	-0.022	28.618	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.062	0.037	30.513	0.007	0.007	0.000	0.000	0.000	0.000
39	A	39	ASN	0	0.004	-0.025	32.073	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.002	0.011	30.606	0.001	0.001	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.877	0.939	31.633	-0.061	-0.061	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.833	0.915	31.641	-0.032	-0.032	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.064	-0.046	33.531	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.756	-0.871	33.429	0.022	0.022	0.000	0.000	0.000	0.000
45	A	45	SER	0	-0.017	-0.005	31.778	0.005	0.005	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.008	0.021	31.208	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.022	0.000	29.846	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.015	0.002	28.168	0.003	0.003	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.867	-0.931	27.464	0.006	0.006	0.000	0.000	0.000	0.000
50	A	50	PHE	0	-0.005	-0.014	23.083	0.014	0.014	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.923	0.941	23.576	-0.071	-0.071	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.008	-0.005	17.497	0.016	0.016	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.760	-0.838	21.148	0.086	0.086	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.878	0.915	17.636	-0.168	-0.168	0.000	0.000	0.000	0.000
55	A	55	HIS	1	0.814	0.879	20.266	-0.162	-0.162	0.000	0.000	0.000	0.000
56	A	56	ASN	0	0.006	-0.004	20.151	0.027	0.027	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.030	0.026	18.526	0.028	0.028	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.926	0.962	14.418	-0.350	-0.350	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.802	-0.875	15.936	0.130	0.130	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.046	-0.021	16.140	0.037	0.037	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.020	0.015	18.475	-0.019	-0.019	0.000	0.000	0.000	0.000
62	A	62	TRP	0	0.018	-0.004	20.608	0.019	0.019	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.010	0.009	24.183	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	64	CYS	0	-0.028	0.005	27.198	0.003	0.003	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.031	-0.017	30.446	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.081	0.019	33.038	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	SER	0	0.067	0.022	36.830	0.002	0.002	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.017	0.009	39.406	0.001	0.001	0.000	0.000	0.000	0.000
69	A	69	GLN	0	0.022	0.015	33.385	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.031	0.017	34.209	0.002	0.002	0.000	0.000	0.000	0.000
71	A	71	THR	0	0.021	0.018	37.502	0.002	0.002	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.814	0.902	36.846	-0.025	-0.025	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.050	-0.027	33.212	0.000	0.000	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.010	-0.003	37.368	0.004	0.004	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.010	-0.003	34.844	0.003	0.003	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.796	-0.888	39.521	0.044	0.044	0.000	0.000	0.000	0.000
77	A	77	ILE	0	-0.022	-0.029	39.523	0.003	0.003	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.869	-0.920	41.699	0.039	0.039	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.733	0.866	42.158	-0.056	-0.056	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.010	-0.018	38.939	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.070	0.032	40.673	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.854	-0.930	38.215	0.060	0.060	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.027	0.002	35.823	0.001	0.001	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.006	0.015	37.435	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.778	0.862	36.287	-0.064	-0.064	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.051	-0.032	39.607	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.060	0.021	40.986	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	THR	0	-0.090	-0.042	39.448	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.891	-0.942	33.746	0.022	0.022	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.073	-0.038	36.587	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	VAL	0	-0.014	-0.013	33.791	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.840	-0.902	32.557	0.084	0.084	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.001	-0.030	29.000	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.050	-0.015	27.557	0.007	0.007	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.003	0.012	31.648	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.048	-0.012	33.874	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	98	PRO	0	0.009	0.034	33.517	0.008	0.008	0.000	0.000	0.000	0.000
98	A	99	HIS	0	-0.055	-0.056	32.720	0.003	0.003	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.041	-0.033	31.083	0.000	0.000	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.876	-0.931	24.728	0.198	0.198	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.006	-0.003	25.629	-0.015	-0.015	0.000	0.000	0.000	0.000
102	A	103	GLN	0	-0.072	-0.043	20.353	0.029	0.029	0.000	0.000	0.000	0.000
103	A	104	PHE	0	0.012	0.014	20.596	-0.017	-0.017	0.000	0.000	0.000	0.000
104	A	105	TYR	0	0.000	-0.014	19.152	0.022	0.022	0.000	0.000	0.000	0.000
105	A	106	PHE	0	0.074	0.032	16.612	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	107	ASN	0	0.013	0.013	14.285	-0.027	-0.027	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.002	-0.014	18.342	-0.015	-0.015	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.012	-0.004	20.613	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.864	0.956	22.822	-0.130	-0.130	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.034	0.023	23.579	0.016	0.016	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.051	-0.041	25.179	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	113	LEU	0	0.013	0.015	26.584	0.009	0.009	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.034	-0.027	27.241	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	115	VAL	0	0.045	0.031	30.528	0.003	0.003	0.000	0.000	0.000	0.000
115	A	116	PRO	0	0.068	0.063	33.760	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.035	0.021	36.510	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	118	GLN	0	0.039	0.000	39.069	-0.003	-0.003	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.043	-0.023	37.804	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.073	-0.031	36.453	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.009	0.003	40.447	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	122	PRO	0	-0.012	-0.007	43.000	0.001	0.001	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.833	0.891	41.876	-0.047	-0.047	0.000	0.000	0.000	0.000
123	A	124	PHE	0	0.036	0.032	45.471	0.001	0.001	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.834	-0.907	47.602	0.039	0.039	0.000	0.000	0.000	0.000
125	A	126	GLY	0	0.019	-0.023	45.617	0.000	0.000	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.070	-0.013	39.962	0.000	0.000	0.000	0.000	0.000	0.000
127	A	128	MET	0	-0.032	-0.014	37.795	0.002	0.002	0.000	0.000	0.000	0.000
128	A	129	PRO	0	-0.008	-0.005	42.159	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	130	MET	0	0.021	0.013	45.275	0.000	0.000	0.000	0.000	0.000	0.000
130	A	131	GLN	0	-0.010	0.001	46.546	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.032	-0.024	40.544	0.002	0.002	0.000	0.000	0.000	0.000
132	A	133	TRP	0	-0.004	0.004	40.821	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	134	ASP	-1	-0.891	-0.953	40.630	0.074	0.074	0.000	0.000	0.000	0.000
134	A	135	ASP	-1	-0.923	-0.949	36.059	0.100	0.100	0.000	0.000	0.000	0.000

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