FMO DATABASE

FMODB ID: V5G61

Calculation Name: 3A7P-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3A7P

Chain ID: A

ChEMBL ID:

UniProt ID: Q03818

Base Structure: X-ray

Registration Date: 2023-09-19

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	88
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-409146.743038
FMO2-HF: Nuclear repulsion	374405.38485
FMO2-HF: Total energy	-34741.358188
FMO2-MP2: Total energy	-34844.414921

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:55:GLY)

Summations of interaction energy for fragment #1(A:55:GLY)

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.
-3.354	-0.781	2.256	-1.743	-3.085	-0.002

Interaction energy analysis for fragmet #1(A:55:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.033 / q_NPA : 0.006

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	57	ILE	0	0.068	0.028	3.820	-1.910	-0.604	-0.004	-0.591	-0.711	0.001
4	A	58	VAL	0	0.033	0.021	2.163	-2.487	-1.831	2.248	-0.990	-1.915	-0.003
5	A	59	SER	0	0.007	0.020	3.590	0.551	1.070	0.013	-0.153	-0.378	0.000
6	A	60	HIS	0	-0.031	-0.016	4.855	0.608	0.700	-0.001	-0.009	-0.081	0.000
7	A	61	ASP	-1	-0.843	-0.941	7.130	-0.192	-0.192	0.000	0.000	0.000	0.000
8	A	62	ASP	-1	-0.888	-0.937	7.176	-1.122	-1.122	0.000	0.000	0.000	0.000
9	A	63	ALA	0	-0.017	0.004	9.181	0.196	0.196	0.000	0.000	0.000	0.000
10	A	64	LEU	0	-0.020	0.002	11.190	0.150	0.150	0.000	0.000	0.000	0.000
11	A	65	LEU	0	-0.004	-0.012	10.751	0.100	0.100	0.000	0.000	0.000	0.000
12	A	66	ASN	0	-0.043	-0.025	11.849	0.128	0.128	0.000	0.000	0.000	0.000
13	A	67	THR	0	-0.018	-0.013	14.974	0.069	0.069	0.000	0.000	0.000	0.000
14	A	68	LEU	0	-0.026	-0.008	16.825	0.044	0.044	0.000	0.000	0.000	0.000
15	A	69	ALA	0	0.001	-0.002	17.680	0.035	0.035	0.000	0.000	0.000	0.000
16	A	70	ILE	0	-0.025	-0.016	18.228	0.030	0.030	0.000	0.000	0.000	0.000
17	A	71	LEU	0	0.045	0.016	20.934	0.027	0.027	0.000	0.000	0.000	0.000
18	A	72	GLN	0	-0.038	-0.007	22.542	0.019	0.019	0.000	0.000	0.000	0.000
19	A	73	LYS	1	0.941	0.963	23.771	0.172	0.172	0.000	0.000	0.000	0.000
20	A	74	GLU	-1	-0.894	-0.950	24.585	-0.143	-0.143	0.000	0.000	0.000	0.000
21	A	75	LEU	0	0.006	0.006	26.064	0.014	0.014	0.000	0.000	0.000	0.000
22	A	76	LYS	1	0.976	0.979	28.623	0.109	0.109	0.000	0.000	0.000	0.000
23	A	77	SER	0	-0.031	-0.005	29.828	0.011	0.011	0.000	0.000	0.000	0.000
24	A	78	LYS	1	0.987	0.984	30.674	0.101	0.101	0.000	0.000	0.000	0.000
25	A	79	GLU	-1	-0.804	-0.868	32.498	-0.074	-0.074	0.000	0.000	0.000	0.000
26	A	80	GLN	0	-0.039	-0.025	33.455	0.004	0.004	0.000	0.000	0.000	0.000
27	A	81	GLU	-1	-0.839	-0.910	35.817	-0.073	-0.073	0.000	0.000	0.000	0.000
28	A	82	ILE	0	-0.007	-0.013	35.653	0.005	0.005	0.000	0.000	0.000	0.000
29	A	83	ARG	1	0.792	0.874	35.192	0.074	0.074	0.000	0.000	0.000	0.000
30	A	84	ARG	1	0.864	0.924	36.777	0.075	0.075	0.000	0.000	0.000	0.000
31	A	85	LEU	0	0.021	-0.001	40.234	0.003	0.003	0.000	0.000	0.000	0.000
32	A	86	LYS	1	0.940	0.976	40.957	0.053	0.053	0.000	0.000	0.000	0.000
33	A	87	GLU	-1	-0.852	-0.918	45.007	-0.039	-0.039	0.000	0.000	0.000	0.000
34	A	88	VAL	0	-0.034	-0.016	46.189	0.003	0.003	0.000	0.000	0.000	0.000
35	A	89	ILE	0	-0.014	-0.014	45.954	0.002	0.002	0.000	0.000	0.000	0.000
36	A	90	ALA	0	0.047	0.033	49.126	0.002	0.002	0.000	0.000	0.000	0.000
37	A	91	LEU	0	-0.013	0.000	50.942	0.003	0.003	0.000	0.000	0.000	0.000
38	A	92	LYS	1	0.952	0.968	51.422	0.039	0.039	0.000	0.000	0.000	0.000
39	A	93	ASN	0	0.030	0.022	52.606	0.001	0.001	0.000	0.000	0.000	0.000
40	A	94	LYS	1	1.003	1.021	55.193	0.033	0.033	0.000	0.000	0.000	0.000
41	A	95	ASN	0	-0.111	-0.073	56.989	0.001	0.001	0.000	0.000	0.000	0.000
42	A	96	THR	0	-0.025	-0.020	57.067	0.001	0.001	0.000	0.000	0.000	0.000
43	A	97	GLU	-1	-0.875	-0.935	57.387	-0.027	-0.027	0.000	0.000	0.000	0.000
44	A	98	ARG	1	0.935	0.966	60.539	0.028	0.028	0.000	0.000	0.000	0.000
45	A	99	LEU	0	-0.015	0.003	61.224	0.001	0.001	0.000	0.000	0.000	0.000
46	A	100	ASN	0	-0.010	-0.016	61.841	0.000	0.000	0.000	0.000	0.000	0.000
47	A	101	ALA	0	0.004	0.011	65.054	0.001	0.001	0.000	0.000	0.000	0.000
48	A	102	ALA	0	0.024	0.010	67.426	0.001	0.001	0.000	0.000	0.000	0.000
49	A	103	LEU	0	0.013	0.004	66.901	0.001	0.001	0.000	0.000	0.000	0.000
50	A	104	ILE	0	0.020	0.026	67.258	0.001	0.001	0.000	0.000	0.000	0.000
51	A	105	SER	0	-0.015	-0.006	70.882	0.001	0.001	0.000	0.000	0.000	0.000
52	A	106	GLY	0	0.037	0.008	72.792	0.001	0.001	0.000	0.000	0.000	0.000
53	A	107	THR	0	-0.031	-0.027	72.325	0.000	0.000	0.000	0.000	0.000	0.000
54	A	108	ILE	0	-0.024	-0.012	74.230	0.001	0.001	0.000	0.000	0.000	0.000
55	A	109	GLU	-1	-0.814	-0.920	77.142	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	110	ASN	0	-0.035	-0.010	77.726	0.001	0.001	0.000	0.000	0.000	0.000
57	A	111	ASN	0	0.025	0.007	79.176	0.000	0.000	0.000	0.000	0.000	0.000
58	A	112	VAL	0	-0.008	-0.004	80.986	0.001	0.001	0.000	0.000	0.000	0.000
59	A	113	LEU	0	-0.048	-0.026	81.438	0.000	0.000	0.000	0.000	0.000	0.000
60	A	114	GLN	0	-0.045	-0.022	80.503	0.001	0.001	0.000	0.000	0.000	0.000
61	A	115	GLN	0	-0.037	-0.019	84.929	0.000	0.000	0.000	0.000	0.000	0.000
62	A	116	LYS	1	0.928	0.982	84.787	0.013	0.013	0.000	0.000	0.000	0.000
63	A	117	LEU	0	-0.013	-0.010	87.376	0.000	0.000	0.000	0.000	0.000	0.000
64	A	118	SER	0	-0.016	-0.009	88.926	0.000	0.000	0.000	0.000	0.000	0.000
65	A	119	ASP	-1	-0.859	-0.939	90.737	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	120	LEU	0	-0.003	0.002	92.722	0.000	0.000	0.000	0.000	0.000	0.000
67	A	121	LYS	1	0.958	0.983	89.596	0.012	0.012	0.000	0.000	0.000	0.000
68	A	122	LYS	1	0.968	1.000	95.159	0.009	0.009	0.000	0.000	0.000	0.000
69	A	123	GLU	-1	-0.948	-0.968	97.089	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	124	HIS	0	0.016	-0.012	98.092	0.000	0.000	0.000	0.000	0.000	0.000
71	A	125	SER	0	-0.017	-0.011	98.429	0.000	0.000	0.000	0.000	0.000	0.000
72	A	126	GLN	0	-0.025	-0.022	100.988	0.000	0.000	0.000	0.000	0.000	0.000
73	A	127	LEU	0	0.003	0.015	103.025	0.000	0.000	0.000	0.000	0.000	0.000
74	A	128	VAL	0	0.057	0.025	102.412	0.000	0.000	0.000	0.000	0.000	0.000
75	A	129	ALA	0	-0.022	-0.008	105.022	0.000	0.000	0.000	0.000	0.000	0.000
76	A	130	ARG	1	0.932	0.960	106.724	0.008	0.008	0.000	0.000	0.000	0.000
77	A	131	TRP	0	0.028	0.016	108.293	0.000	0.000	0.000	0.000	0.000	0.000
78	A	132	LEU	0	0.080	0.053	107.817	0.000	0.000	0.000	0.000	0.000	0.000
79	A	133	LYS	1	0.926	0.968	109.481	0.008	0.008	0.000	0.000	0.000	0.000
80	A	134	LYS	1	0.740	0.856	112.756	0.008	0.008	0.000	0.000	0.000	0.000
81	A	135	THR	0	-0.013	-0.030	112.790	0.000	0.000	0.000	0.000	0.000	0.000
82	A	136	GLU	-1	-0.913	-0.964	114.046	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	137	LYS	1	0.934	0.962	116.541	0.007	0.007	0.000	0.000	0.000	0.000
84	A	138	GLU	-1	-0.838	-0.896	117.237	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	139	THR	0	0.005	-0.003	118.261	0.000	0.000	0.000	0.000	0.000	0.000
86	A	140	GLU	-1	-0.980	-0.972	120.630	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	141	ALA	0	-0.076	-0.043	122.459	0.000	0.000	0.000	0.000	0.000	0.000
88	A	142	MET	0	-0.080	-0.017	122.319	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:55:GLY)