FMO DATABASE

FMODB ID: 9GRJ2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1107996.021737
FMO2-HF: Nuclear repulsion	1054141.048416
FMO2-HF: Total energy	-53854.97332
FMO2-MP2: Total energy	-54011.490001

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.
-1.382	0.131	-0.023	-0.709	-0.78	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 : -0.028 / q_NPA : -0.030

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	-0.040	-0.015	3.815	-0.827	0.686	-0.023	-0.709	-0.780	0.001
4	A	4	PHE	0	-0.024	-0.013	6.316	0.136	0.136	0.000	0.000	0.000	0.000
5	A	5	ASP	-1	-0.863	-0.950	10.076	-0.479	-0.479	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.019	-0.028	13.105	0.051	0.051	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.053	0.004	16.291	0.044	0.044	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.069	-0.049	17.549	0.021	0.021	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.035	0.011	16.406	0.026	0.026	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.909	-0.957	20.129	-0.053	-0.053	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.047	-0.014	22.014	0.000	0.000	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.010	-0.027	24.593	0.001	0.001	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.079	-0.053	28.081	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.004	0.011	27.166	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.867	-0.909	24.726	-0.050	-0.050	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.043	-0.037	22.087	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.021	0.020	18.015	0.010	0.010	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.852	-0.903	16.019	-0.173	-0.173	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.013	-0.008	11.970	0.025	0.025	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.060	-0.039	11.649	-0.022	-0.022	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.013	-0.003	11.156	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.045	0.020	11.092	0.051	0.051	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.016	0.015	7.312	0.025	0.025	0.000	0.000	0.000	0.000
24	A	24	GLN	0	0.012	0.023	6.438	-0.031	-0.031	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.084	-0.024	8.517	0.167	0.167	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.084	-0.042	9.012	0.033	0.033	0.000	0.000	0.000	0.000
27	A	27	GLN	0	0.000	-0.015	12.691	-0.050	-0.050	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.028	0.018	15.552	-0.015	-0.015	0.000	0.000	0.000	0.000
29	A	29	PRO	0	-0.003	0.017	18.564	0.017	0.017	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.050	0.032	21.619	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	31	ASN	0	-0.021	-0.009	24.651	0.013	0.013	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.026	-0.038	20.234	0.008	0.008	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.005	-0.004	25.628	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.015	0.011	24.874	0.012	0.012	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.043	-0.033	27.378	-0.020	-0.020	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.018	0.017	28.049	0.012	0.012	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.031	-0.025	28.628	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.067	0.034	30.513	0.003	0.003	0.000	0.000	0.000	0.000
39	A	39	ASN	0	0.001	-0.019	32.067	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	GLY	0	0.003	0.010	30.609	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.902	0.960	31.636	-0.082	-0.082	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.911	0.953	31.713	-0.101	-0.101	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.080	-0.057	33.529	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.837	-0.929	33.538	0.066	0.066	0.000	0.000	0.000	0.000
45	A	45	SER	0	-0.045	-0.011	31.761	0.009	0.009	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.003	0.012	31.202	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.045	-0.018	29.830	0.009	0.009	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.021	0.002	27.895	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.881	-0.939	27.455	0.051	0.051	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.001	-0.008	22.987	0.009	0.009	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.923	0.939	23.539	-0.054	-0.054	0.000	0.000	0.000	0.000
52	A	52	LEU	0	-0.007	-0.008	17.365	0.014	0.014	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.773	-0.856	21.142	0.054	0.054	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.903	0.943	17.564	-0.025	-0.025	0.000	0.000	0.000	0.000
55	A	55	HIS	1	0.833	0.895	20.275	-0.107	-0.107	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.015	-0.014	20.157	0.013	0.013	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.054	0.038	18.451	0.010	0.010	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.930	0.963	14.391	-0.318	-0.318	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.840	-0.906	15.714	0.044	0.044	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.031	-0.010	16.140	0.043	0.043	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.017	0.009	18.365	-0.021	-0.021	0.000	0.000	0.000	0.000
62	A	62	TRP	0	0.011	-0.008	20.604	0.019	0.019	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.007	0.009	24.180	-0.009	-0.009	0.000	0.000	0.000	0.000
64	A	64	CYS	0	-0.021	0.001	27.194	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.017	-0.014	30.277	0.001	0.001	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.097	0.040	33.034	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	67	SER	0	0.079	0.025	36.826	0.003	0.003	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.004	-0.001	39.404	0.002	0.002	0.000	0.000	0.000	0.000
69	A	69	GLN	0	-0.009	-0.011	34.036	0.000	0.000	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.048	0.025	34.358	0.003	0.003	0.000	0.000	0.000	0.000
71	A	71	THR	0	0.031	0.030	37.500	0.002	0.002	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.899	0.955	37.722	-0.058	-0.058	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.046	-0.019	32.763	0.002	0.002	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.018	-0.018	37.368	0.005	0.005	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.021	-0.009	34.938	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.844	-0.930	39.521	0.045	0.045	0.000	0.000	0.000	0.000
77	A	77	ILE	0	-0.034	-0.038	39.505	0.000	0.000	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.878	-0.920	41.699	0.039	0.039	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.833	0.928	42.013	-0.053	-0.053	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.010	-0.017	38.946	0.001	0.001	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.078	0.037	40.674	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.915	-0.968	38.430	0.037	0.037	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.042	-0.008	35.809	0.000	0.000	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.009	0.017	37.434	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.821	0.887	35.983	-0.042	-0.042	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.054	-0.036	39.659	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.065	0.027	40.608	0.002	0.002	0.000	0.000	0.000	0.000
88	A	88	THR	0	-0.083	-0.041	39.568	0.000	0.000	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.886	-0.931	33.903	0.028	0.028	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.081	-0.045	36.597	0.002	0.002	0.000	0.000	0.000	0.000
91	A	92	VAL	0	-0.016	-0.011	33.748	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.821	-0.890	32.456	0.057	0.057	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.002	-0.029	28.918	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.051	-0.016	27.572	0.005	0.005	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.008	0.009	31.651	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.046	-0.009	33.902	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	98	PRO	0	0.012	0.032	33.522	0.005	0.005	0.000	0.000	0.000	0.000
98	A	99	HIS	0	-0.057	-0.051	32.770	0.003	0.003	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.047	-0.036	31.089	0.004	0.004	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.882	-0.930	24.865	0.171	0.171	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.009	-0.003	25.455	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	103	GLN	0	-0.074	-0.042	20.512	0.028	0.028	0.000	0.000	0.000	0.000
103	A	104	PHE	0	0.021	0.020	20.623	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	105	TYR	0	-0.010	-0.022	18.945	0.017	0.017	0.000	0.000	0.000	0.000
105	A	106	PHE	0	0.060	0.025	16.619	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	107	ASN	0	0.023	0.010	14.249	-0.046	-0.046	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.022	-0.022	18.336	0.005	0.005	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.007	0.004	20.669	-0.041	-0.041	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.892	0.972	22.817	-0.224	-0.224	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.038	0.022	23.577	0.016	0.016	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.051	-0.039	25.076	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.004	0.006	26.585	0.003	0.003	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.016	-0.020	27.064	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	115	VAL	0	0.046	0.033	30.533	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	116	PRO	0	0.068	0.065	33.764	0.002	0.002	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.029	0.016	36.516	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	118	GLN	0	0.052	0.001	39.075	0.001	0.001	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.047	-0.014	37.908	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.067	-0.034	36.736	0.000	0.000	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.006	0.008	40.450	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	122	PRO	0	-0.016	-0.006	43.002	0.003	0.003	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.831	0.889	41.912	-0.068	-0.068	0.000	0.000	0.000	0.000
123	A	124	PHE	0	0.045	0.033	45.473	0.003	0.003	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.836	-0.872	47.637	0.054	0.054	0.000	0.000	0.000	0.000
125	A	126	GLY	0	0.004	-0.059	45.645	0.001	0.001	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.060	-0.014	39.974	0.000	0.000	0.000	0.000	0.000	0.000
127	A	128	MET	0	-0.031	-0.016	37.673	0.003	0.003	0.000	0.000	0.000	0.000
128	A	129	PRO	0	-0.013	-0.005	42.078	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	130	MET	0	0.004	0.008	45.281	0.000	0.000	0.000	0.000	0.000	0.000
130	A	131	GLN	0	0.017	0.013	46.547	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.035	-0.029	40.782	0.003	0.003	0.000	0.000	0.000	0.000
132	A	133	TRP	0	-0.005	0.004	40.807	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	134	ASP	-1	-0.978	-0.991	40.504	0.062	0.062	0.000	0.000	0.000	0.000
134	A	135	ASP	-1	-0.881	-0.934	36.068	0.071	0.071	0.000	0.000	0.000	0.000

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