FMO DATABASE

FMODB ID: 3Q2QL

Calculation Name: 1FRS-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	129
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-901666.906598
FMO2-HF: Nuclear repulsion	853308.087389
FMO2-HF: Total energy	-48358.819209
FMO2-MP2: Total energy	-48499.383848

3D Structure Molmil

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.
-0.47	1.343	0.012	-0.698	-1.126	0.005

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 : 0.006 / q_NPA : -0.007

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	3	ASN	0	-0.051	-0.020	3.707	-0.786	0.967	0.013	-0.695	-1.070	0.005
4	A	4	PHE	0	-0.048	-0.017	5.049	0.320	0.380	-0.001	-0.003	-0.056	0.000
5	A	5	GLU	-1	-0.891	-0.947	6.615	-0.530	-0.530	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.812	-0.881	8.944	-0.043	-0.043	0.000	0.000	0.000	0.000
7	A	7	PHE	0	-0.013	-0.004	11.754	0.071	0.071	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.068	0.018	14.054	-0.037	-0.037	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.079	-0.030	17.608	0.016	0.016	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.060	-0.060	19.615	0.011	0.011	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.894	-0.949	21.342	0.087	0.087	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.031	-0.002	23.136	0.010	0.010	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.059	0.024	25.471	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.009	0.003	23.980	0.013	0.013	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.125	-0.053	25.060	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.013	-0.009	26.162	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.781	-0.873	21.528	0.041	0.041	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.089	-0.050	22.042	-0.019	-0.019	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.818	0.902	15.989	0.099	0.099	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.077	-0.033	16.125	-0.013	-0.013	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.061	0.018	14.577	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.038	-0.010	11.149	0.042	0.042	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.014	-0.035	14.223	0.005	0.005	0.000	0.000	0.000	0.000
24	A	24	ASN	0	0.008	-0.011	16.648	-0.029	-0.029	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.035	0.004	12.079	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.009	0.013	16.112	-0.010	-0.010	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.004	-0.019	19.314	0.017	0.017	0.000	0.000	0.000	0.000
28	A	28	GLY	0	0.010	0.023	15.862	0.028	0.028	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.085	-0.026	16.818	0.038	0.038	0.000	0.000	0.000	0.000
30	A	30	ALA	0	-0.009	0.011	13.234	-0.040	-0.040	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.805	-0.872	15.110	-0.182	-0.182	0.000	0.000	0.000	0.000
32	A	32	TRP	0	0.049	0.003	10.984	-0.060	-0.060	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.055	-0.044	16.877	0.041	0.041	0.000	0.000	0.000	0.000
34	A	34	SER	0	0.022	0.022	19.143	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.032	0.016	21.461	-0.021	-0.021	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.012	0.023	22.991	0.009	0.009	0.000	0.000	0.000	0.000
37	A	37	SER	0	0.065	0.025	26.051	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.913	0.910	21.650	0.221	0.221	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.054	-0.030	27.664	0.000	0.000	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.027	-0.032	28.986	0.014	0.014	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.073	0.013	23.771	0.007	0.007	0.000	0.000	0.000	0.000
42	A	42	TYR	0	0.150	0.050	22.862	0.006	0.006	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.839	0.909	21.207	0.142	0.142	0.000	0.000	0.000	0.000
44	A	44	VAL	0	0.009	0.006	16.850	0.024	0.024	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.003	-0.014	17.506	-0.033	-0.033	0.000	0.000	0.000	0.000
46	A	46	CYS	0	-0.052	-0.007	14.382	0.048	0.048	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.077	0.044	15.787	-0.043	-0.043	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.008	-0.018	13.698	0.045	0.045	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.871	0.958	16.793	0.076	0.076	0.000	0.000	0.000	0.000
50	A	50	GLN	0	0.020	-0.015	19.178	0.012	0.012	0.000	0.000	0.000	0.000
51	A	51	SER	0	0.012	0.004	20.903	0.002	0.002	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.027	0.030	24.380	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.034	0.022	24.900	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.004	-0.011	24.634	0.002	0.002	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.017	-0.031	22.351	0.008	0.008	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.918	0.982	13.583	0.076	0.076	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.852	0.906	19.687	0.072	0.072	0.000	0.000	0.000	0.000
58	A	58	TYR	0	0.050	0.040	12.891	-0.034	-0.034	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.085	-0.059	18.211	0.015	0.015	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.037	0.011	16.751	-0.028	-0.028	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.900	0.945	19.605	0.121	0.121	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.058	0.036	20.591	-0.017	-0.017	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.860	-0.901	22.839	-0.109	-0.109	0.000	0.000	0.000	0.000
64	A	64	VAL	0	-0.001	-0.002	25.378	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	65	PRO	0	0.008	0.002	26.767	0.004	0.004	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.947	0.992	29.958	0.029	0.029	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.019	-0.021	30.687	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.009	-0.002	33.626	0.006	0.006	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.036	0.014	36.293	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	70	GLN	0	-0.048	-0.014	38.931	0.007	0.007	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.060	0.032	41.312	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.016	0.001	40.767	0.001	0.001	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.002	-0.013	44.790	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.010	-0.013	47.708	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.019	0.025	42.199	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.959	-0.979	41.228	-0.044	-0.044	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.017	-0.011	37.786	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.009	0.009	33.222	0.004	0.004	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.002	-0.010	34.100	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.005	0.002	32.027	0.004	0.004	0.000	0.000	0.000	0.000
81	A	81	ALA	0	-0.027	-0.008	34.136	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	TRP	0	0.027	0.004	33.346	0.002	0.002	0.000	0.000	0.000	0.000
83	A	83	ARG	1	0.834	0.903	26.765	0.095	0.095	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.011	0.007	30.154	0.004	0.004	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.001	-0.013	27.858	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	86	MET	0	0.000	0.022	22.712	0.003	0.003	0.000	0.000	0.000	0.000
87	A	87	ASN	0	0.035	-0.004	24.608	-0.024	-0.024	0.000	0.000	0.000	0.000
88	A	88	MET	0	-0.015	-0.004	21.263	0.008	0.008	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.742	-0.867	22.228	-0.082	-0.082	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.010	0.018	18.048	0.011	0.011	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.009	-0.005	20.897	-0.019	-0.019	0.000	0.000	0.000	0.000
92	A	92	ILE	0	-0.024	0.007	17.043	0.011	0.011	0.000	0.000	0.000	0.000
93	A	93	PRO	0	0.011	-0.011	21.060	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	94	VAL	0	0.006	-0.003	20.175	0.005	0.005	0.000	0.000	0.000	0.000
95	A	95	PHE	0	-0.018	-0.021	19.850	0.007	0.007	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.063	0.001	19.128	0.012	0.012	0.000	0.000	0.000	0.000
97	A	97	THR	0	0.054	-0.001	17.924	0.012	0.012	0.000	0.000	0.000	0.000
98	A	98	ASN	0	0.053	0.006	12.722	-0.025	-0.025	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.913	-0.945	15.438	0.311	0.311	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.811	-0.877	17.962	0.133	0.133	0.000	0.000	0.000	0.000
101	A	101	CYS	0	-0.060	-0.043	15.231	-0.025	-0.025	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.011	0.007	15.753	-0.013	-0.013	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.004	0.007	16.863	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	104	ILE	0	0.017	0.010	18.775	-0.014	-0.014	0.000	0.000	0.000	0.000
105	A	105	VAL	0	0.009	0.015	14.762	-0.017	-0.017	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.978	0.980	18.190	-0.275	-0.275	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.004	0.005	20.473	-0.013	-0.013	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.020	-0.003	19.466	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.012	-0.013	17.645	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.005	0.004	22.176	-0.007	-0.007	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.094	-0.057	25.476	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	112	PHE	0	0.019	-0.008	23.452	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.881	0.977	25.775	-0.099	-0.099	0.000	0.000	0.000	0.000
114	A	114	THR	0	0.095	0.029	26.799	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.003	0.007	29.416	0.006	0.006	0.000	0.000	0.000	0.000
116	A	116	ASN	0	-0.028	-0.010	28.504	0.000	0.000	0.000	0.000	0.000	0.000
117	A	117	PRO	0	0.040	0.006	31.835	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	118	ILE	0	-0.042	-0.018	30.138	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	119	ALA	0	0.045	0.022	29.191	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.036	-0.014	30.805	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	121	ALA	0	0.027	0.014	34.198	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	122	ILE	0	-0.010	-0.011	30.338	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.012	-0.001	32.502	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.029	-0.008	34.381	0.000	0.000	0.000	0.000	0.000	0.000
125	A	125	ASN	0	-0.090	-0.038	37.295	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	126	SER	0	0.006	0.007	38.337	0.000	0.000	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.023	0.036	38.311	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.038	-0.042	35.176	0.003	0.003	0.000	0.000	0.000	0.000
129	A	129	TYR	0	0.003	0.012	39.357	-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)