FMO DATABASE

FMODB ID: LJ5J9

Calculation Name: 1FRS-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1FRS

Chain ID: A

ChEMBL ID:

UniProt ID: P03614

Base Structure: X-ray

Registration Date: 2023-06-21

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	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	129
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-899856.179017
FMO2-HF: Nuclear repulsion	851495.957926
FMO2-HF: Total energy	-48360.221092
FMO2-MP2: Total energy	-48500.575859

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.
0.063	1.767	-0.014	-0.874	-0.816	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 : 0.031 / q_NPA : 0.012

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	ASN	0	0.003	-0.001	3.850	-0.408	1.296	-0.014	-0.874	-0.816	0.004
4	A	4	PHE	0	-0.069	-0.018	5.809	0.450	0.450	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.884	-0.944	7.060	-0.693	-0.693	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.819	-0.894	9.465	-0.093	-0.093	0.000	0.000	0.000	0.000
7	A	7	PHE	0	-0.024	-0.004	12.193	0.050	0.050	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.023	0.009	14.715	-0.008	-0.008	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.052	-0.020	18.339	0.005	0.005	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.033	-0.029	20.168	0.009	0.009	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.882	-0.936	21.982	0.011	0.011	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.077	-0.052	23.548	0.003	0.003	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.018	0.008	25.585	0.001	0.001	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.028	-0.007	24.225	0.011	0.011	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.103	-0.053	25.239	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.027	0.011	26.673	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.814	-0.890	22.449	-0.024	-0.024	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.008	0.000	22.563	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.820	0.878	16.661	0.131	0.131	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.074	-0.031	16.992	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.054	0.014	15.261	-0.021	-0.021	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.026	0.004	11.582	0.039	0.039	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.028	-0.048	14.644	0.006	0.006	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.004	-0.011	17.075	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.040	0.016	12.889	-0.053	-0.053	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.031	0.026	16.462	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.046	-0.038	19.748	0.009	0.009	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.026	0.032	16.747	0.027	0.027	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.084	-0.039	17.132	0.006	0.006	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.005	0.025	13.716	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.804	-0.875	15.603	-0.225	-0.225	0.000	0.000	0.000	0.000
32	A	32	TRP	0	0.032	0.002	11.593	-0.051	-0.051	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.039	-0.031	17.706	0.039	0.039	0.000	0.000	0.000	0.000
34	A	34	SER	0	0.046	0.027	19.916	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.000	0.003	22.017	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.003	0.005	23.462	0.011	0.011	0.000	0.000	0.000	0.000
37	A	37	SER	0	0.080	0.034	26.520	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.864	0.891	22.293	0.246	0.246	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.012	-0.018	28.180	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.036	-0.026	29.988	0.011	0.011	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.030	0.010	24.538	0.005	0.005	0.000	0.000	0.000	0.000
42	A	42	TYR	0	0.103	0.035	23.864	0.002	0.002	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.859	0.936	22.050	0.196	0.196	0.000	0.000	0.000	0.000
44	A	44	VAL	0	0.020	0.017	17.485	0.023	0.023	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.028	-0.012	18.574	-0.023	-0.023	0.000	0.000	0.000	0.000
46	A	46	CYS	0	-0.048	-0.020	15.079	0.034	0.034	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.045	0.036	16.766	-0.031	-0.031	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.005	-0.019	14.642	0.035	0.035	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.842	0.918	17.735	0.161	0.161	0.000	0.000	0.000	0.000
50	A	50	GLN	0	0.015	-0.001	20.160	0.001	0.001	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.025	-0.015	21.906	0.007	0.007	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.031	0.018	24.993	0.011	0.011	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.049	0.026	24.957	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.041	0.023	25.094	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.048	-0.027	23.670	0.008	0.008	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.943	0.978	14.582	0.231	0.231	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.879	0.927	21.205	0.135	0.135	0.000	0.000	0.000	0.000
58	A	58	TYR	0	0.060	0.037	13.624	-0.031	-0.031	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.048	-0.038	18.902	0.035	0.035	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.014	0.002	17.477	-0.034	-0.034	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.909	0.942	20.256	0.196	0.196	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.022	0.015	20.997	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.852	-0.905	23.420	-0.152	-0.152	0.000	0.000	0.000	0.000
64	A	64	VAL	0	0.029	0.004	25.763	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	65	PRO	0	-0.005	0.006	27.759	0.008	0.008	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.944	0.982	30.809	0.058	0.058	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.032	-0.026	30.815	0.000	0.000	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.005	0.003	33.949	0.007	0.007	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.019	-0.013	36.722	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.027	-0.024	39.329	0.005	0.005	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.020	0.016	41.883	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	72	GLN	0	0.000	-0.006	41.423	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.009	0.000	45.417	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.003	0.005	48.213	0.001	0.001	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.003	-0.001	42.660	0.002	0.002	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.885	-0.926	41.326	-0.056	-0.056	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.020	-0.008	38.511	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	78	PRO	0	0.019	0.019	33.887	0.002	0.002	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.010	0.000	34.635	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.015	0.003	32.364	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.005	0.002	34.480	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	TRP	0	0.023	0.007	33.363	0.002	0.002	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.792	0.878	27.451	0.132	0.132	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.003	0.018	30.974	0.002	0.002	0.000	0.000	0.000	0.000
85	A	85	TYR	0	0.016	-0.003	28.210	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	86	MET	0	0.007	0.018	23.012	0.004	0.004	0.000	0.000	0.000	0.000
87	A	87	ASN	0	0.023	-0.001	25.178	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	88	MET	0	-0.003	0.003	22.331	0.008	0.008	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.764	-0.856	22.893	-0.161	-0.161	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.035	0.031	18.598	0.013	0.013	0.000	0.000	0.000	0.000
91	A	91	THR	0	-0.019	-0.022	21.210	-0.018	-0.018	0.000	0.000	0.000	0.000
92	A	92	ILE	0	0.004	0.003	17.765	0.013	0.013	0.000	0.000	0.000	0.000
93	A	93	PRO	0	-0.001	-0.008	21.832	-0.014	-0.014	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.018	-0.019	20.615	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	95	PHE	0	-0.019	-0.016	20.611	0.002	0.002	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.044	0.008	19.919	0.014	0.014	0.000	0.000	0.000	0.000
97	A	97	THR	0	0.045	-0.007	18.526	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	98	ASN	0	0.023	-0.005	13.407	-0.047	-0.047	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.875	-0.931	15.597	0.147	0.147	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.811	-0.873	18.255	0.024	0.024	0.000	0.000	0.000	0.000
101	A	101	CYS	0	-0.061	-0.038	15.735	-0.024	-0.024	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.004	0.000	15.698	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.019	-0.008	17.065	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.014	0.002	19.613	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	105	VAL	0	-0.014	-0.006	15.247	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.965	0.983	18.416	-0.118	-0.118	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.016	0.019	20.989	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.011	0.003	19.648	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.005	-0.014	17.539	0.006	0.006	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.003	0.000	22.287	0.001	0.001	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.069	-0.033	25.574	0.000	0.000	0.000	0.000	0.000	0.000
112	A	112	PHE	0	-0.023	-0.027	24.064	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.900	0.973	25.580	-0.025	-0.025	0.000	0.000	0.000	0.000
114	A	114	THR	0	0.056	0.004	26.738	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.019	0.014	29.539	0.007	0.007	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.017	0.004	29.050	0.005	0.005	0.000	0.000	0.000	0.000
117	A	117	PRO	0	0.037	0.016	32.165	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	118	ILE	0	0.018	0.016	30.410	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	119	ALA	0	0.032	0.015	29.175	-0.004	-0.004	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.036	-0.031	31.132	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	121	ALA	0	-0.005	-0.002	34.482	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	122	ILE	0	0.004	-0.001	31.033	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.017	-0.009	32.930	-0.002	-0.002	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.032	-0.006	34.678	0.001	0.001	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.073	-0.031	37.505	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.005	-0.008	38.578	0.001	0.001	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.019	0.016	38.464	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.012	-0.014	35.356	0.002	0.002	0.000	0.000	0.000	0.000
129	A	129	TYR	0	-0.018	0.007	39.498	0.001	0.001	0.000	0.000	0.000	0.000

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