FMO DATABASE

FMODB ID: J3839

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

Total energy (hartree)

FMO2-HF: Electronic energy	-902067.845964
FMO2-HF: Nuclear repulsion	853711.099597
FMO2-HF: Total energy	-48356.746366
FMO2-MP2: Total energy	-48497.67967

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.
2.085	3.329	0.022	-0.362	-0.904	0.002

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 : -0.017 / 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	ASN	0	-0.026	-0.008	3.694	0.301	1.478	0.023	-0.357	-0.843	0.002
4	A	4	PHE	0	-0.050	-0.022	4.893	0.298	0.365	-0.001	-0.005	-0.061	0.000
5	A	5	GLU	-1	-0.863	-0.940	6.289	1.018	1.018	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.939	-0.969	8.934	0.164	0.164	0.000	0.000	0.000	0.000
7	A	7	PHE	0	-0.045	-0.015	11.747	0.060	0.060	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.034	0.007	14.044	-0.035	-0.035	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.057	-0.022	17.598	-0.003	-0.003	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.066	-0.061	19.603	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.886	-0.944	21.452	0.142	0.142	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.002	0.018	23.127	-0.007	-0.007	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.052	0.023	25.445	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.002	0.005	23.977	0.015	0.015	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.144	-0.064	25.057	0.001	0.001	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.029	-0.015	26.143	-0.009	-0.009	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.798	-0.889	21.583	0.123	0.123	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.079	-0.051	22.255	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.958	0.992	16.902	-0.173	-0.173	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.053	-0.032	16.113	-0.018	-0.018	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.094	0.038	14.585	0.021	0.021	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.070	-0.037	11.060	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.002	0.007	14.214	0.020	0.020	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.030	-0.001	16.625	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.022	-0.003	11.690	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.015	0.008	15.930	-0.027	-0.027	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.006	-0.014	19.134	0.007	0.007	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.005	0.019	15.681	0.011	0.011	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.085	-0.029	16.636	0.015	0.015	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.005	0.009	13.131	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.835	-0.914	14.925	-0.064	-0.064	0.000	0.000	0.000	0.000
32	A	32	TRP	0	0.053	0.011	11.118	-0.047	-0.047	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.055	-0.033	16.864	0.003	0.003	0.000	0.000	0.000	0.000
34	A	34	SER	0	0.005	0.021	19.134	0.009	0.009	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.032	0.014	21.452	-0.012	-0.012	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.017	0.028	22.985	0.005	0.005	0.000	0.000	0.000	0.000
37	A	37	SER	0	0.053	0.014	26.044	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.936	0.931	21.799	0.069	0.069	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.024	-0.005	27.654	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.019	-0.034	28.988	0.001	0.001	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.074	0.008	23.756	0.004	0.004	0.000	0.000	0.000	0.000
42	A	42	TYR	0	0.127	0.031	22.780	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.889	0.940	21.214	0.065	0.065	0.000	0.000	0.000	0.000
44	A	44	VAL	0	0.030	0.016	16.447	0.005	0.005	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.029	-0.023	17.362	-0.016	-0.016	0.000	0.000	0.000	0.000
46	A	46	CYS	0	-0.004	0.011	13.630	0.016	0.016	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.044	0.038	15.634	-0.023	-0.023	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.061	0.024	13.728	0.027	0.027	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.916	0.967	16.635	0.104	0.104	0.000	0.000	0.000	0.000
50	A	50	GLN	0	0.008	-0.016	19.090	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.028	-0.011	20.772	0.006	0.006	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.058	0.050	24.248	0.001	0.001	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.031	0.015	24.788	-0.011	-0.011	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.012	-0.019	24.547	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	55	ASN	0	0.026	-0.016	22.260	0.005	0.005	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.887	0.966	13.471	0.240	0.240	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.906	0.945	19.556	0.112	0.112	0.000	0.000	0.000	0.000
58	A	58	TYR	0	0.021	0.036	12.783	-0.035	-0.035	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.045	-0.042	18.064	0.024	0.024	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.013	0.001	16.859	-0.018	-0.018	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.907	0.954	19.445	0.096	0.096	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.054	0.030	20.622	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.917	-0.953	22.684	-0.042	-0.042	0.000	0.000	0.000	0.000
64	A	64	VAL	0	0.000	0.003	25.247	0.005	0.005	0.000	0.000	0.000	0.000
65	A	65	PRO	0	0.017	-0.002	26.684	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.940	0.999	29.944	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.003	-0.016	31.102	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.026	-0.007	33.616	0.002	0.002	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.030	0.013	36.284	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.049	-0.010	38.922	0.001	0.001	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.055	0.026	41.302	0.000	0.000	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.021	-0.005	40.720	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.006	-0.008	44.781	0.000	0.000	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.010	-0.012	47.718	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.013	0.023	42.279	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.939	-0.979	41.128	0.009	0.009	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.032	-0.009	37.716	0.000	0.000	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.026	0.001	33.268	0.001	0.001	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.001	-0.017	34.106	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.018	0.011	32.085	0.004	0.004	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.020	-0.005	34.124	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	82	TRP	0	0.028	0.005	33.060	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.843	0.917	27.023	0.024	0.024	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.000	0.008	29.880	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.008	-0.015	27.705	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	86	MET	0	0.003	0.028	22.495	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.050	-0.057	24.468	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	88	MET	0	0.034	0.028	21.016	0.004	0.004	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.842	-0.936	22.077	-0.090	-0.090	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.003	0.017	18.035	0.008	0.008	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.020	-0.006	20.769	-0.018	-0.018	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.037	0.007	17.455	0.010	0.010	0.000	0.000	0.000	0.000
93	A	93	PRO	0	0.007	-0.013	20.969	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	94	VAL	0	0.008	-0.006	20.103	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	95	PHE	0	-0.007	-0.019	19.802	-0.007	-0.007	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.062	0.011	18.959	0.008	0.008	0.000	0.000	0.000	0.000
97	A	97	THR	0	0.058	0.031	17.932	-0.013	-0.013	0.000	0.000	0.000	0.000
98	A	98	ASN	0	0.090	0.015	12.148	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.924	-0.942	15.442	0.030	0.030	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.843	-0.921	17.978	-0.024	-0.024	0.000	0.000	0.000	0.000
101	A	101	CYS	0	-0.056	-0.043	15.185	-0.004	-0.004	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.020	0.010	16.019	0.007	0.007	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.004	-0.008	16.847	0.010	0.010	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.010	0.017	18.667	0.004	0.004	0.000	0.000	0.000	0.000
105	A	105	VAL	0	0.017	0.016	15.015	0.003	0.003	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.964	0.976	18.133	-0.085	-0.085	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.008	0.002	20.439	0.002	0.002	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.009	0.001	18.950	0.000	0.000	0.000	0.000	0.000	0.000
109	A	109	GLN	0	-0.009	-0.014	17.789	0.004	0.004	0.000	0.000	0.000	0.000
110	A	110	GLY	0	-0.027	-0.007	22.115	0.002	0.002	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.063	-0.058	25.426	0.000	0.000	0.000	0.000	0.000	0.000
112	A	112	PHE	0	0.013	-0.009	23.338	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.924	1.011	25.916	-0.061	-0.061	0.000	0.000	0.000	0.000
114	A	114	THR	0	0.079	0.018	26.743	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.005	0.009	29.358	0.003	0.003	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.029	-0.008	28.296	-0.003	-0.003	0.000	0.000	0.000	0.000
117	A	117	PRO	0	0.018	0.003	31.779	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.022	-0.014	29.780	-0.001	-0.001	0.000	0.000	0.000	0.000
119	A	119	ALA	0	0.028	0.008	29.310	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.032	-0.014	30.720	0.001	0.001	0.000	0.000	0.000	0.000
121	A	121	ALA	0	0.026	0.009	34.117	0.000	0.000	0.000	0.000	0.000	0.000
122	A	122	ILE	0	-0.006	-0.003	30.095	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.022	-0.009	32.529	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.038	-0.012	34.281	0.001	0.001	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.068	-0.020	37.187	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	126	SER	0	-0.007	-0.013	38.232	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.014	0.041	38.203	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.014	-0.028	35.296	0.002	0.002	0.000	0.000	0.000	0.000
129	A	129	TYR	0	-0.017	0.000	39.264	-0.002	-0.002	0.000	0.000	0.000	0.000

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