FMO DATABASE

FMODB ID: 4JY5N

Calculation Name: 3CPK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CPK

Chain ID: A

ChEMBL ID:

UniProt ID: Q7W7N7

Base Structure: X-ray

Registration Date: 2023-09-23

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	118
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-896184.220729
FMO2-HF: Nuclear repulsion	852778.400505
FMO2-HF: Total energy	-43405.820224
FMO2-MP2: Total energy	-43533.267416

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:7:PRO)

Summations of interaction energy for fragment #1(A:7:PRO)

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.
-1.701	1.308	-0.024	-1.39	-1.594	0.004

Interaction energy analysis for fragmet #1(A:7:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.016 / q_NPA : -0.015

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	9	THR	0	-0.026	-0.010	3.830	-1.530	1.392	-0.023	-1.381	-1.518	0.004
4	A	10	ALA	0	0.015	0.016	5.222	-0.503	-0.416	-0.001	-0.009	-0.076	0.000
5	A	11	LEU	0	0.020	0.003	8.445	0.059	0.059	0.000	0.000	0.000	0.000
6	A	12	ASN	0	-0.054	-0.025	11.582	-0.048	-0.048	0.000	0.000	0.000	0.000
7	A	13	THR	0	0.023	0.013	14.788	-0.026	-0.026	0.000	0.000	0.000	0.000
8	A	14	VAL	0	-0.008	0.004	17.432	-0.002	-0.002	0.000	0.000	0.000	0.000
9	A	15	THR	0	-0.043	-0.026	19.809	-0.003	-0.003	0.000	0.000	0.000	0.000
10	A	16	ALA	0	0.013	0.015	21.851	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	17	TYR	0	0.002	-0.007	25.626	0.004	0.004	0.000	0.000	0.000	0.000
12	A	18	GLY	0	0.006	-0.002	28.395	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	19	ASP	-1	-0.946	-0.968	31.503	0.030	0.030	0.000	0.000	0.000	0.000
14	A	20	GLY	0	0.042	0.007	33.812	0.000	0.000	0.000	0.000	0.000	0.000
15	A	21	TYR	0	-0.090	-0.048	27.843	0.000	0.000	0.000	0.000	0.000	0.000
16	A	22	ILE	0	0.012	0.020	24.223	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	23	GLU	-1	-0.871	-0.939	23.027	0.063	0.063	0.000	0.000	0.000	0.000
18	A	24	VAL	0	0.001	0.002	18.220	0.000	0.000	0.000	0.000	0.000	0.000
19	A	25	ASN	0	0.007	-0.012	15.264	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	26	GLN	0	-0.035	-0.023	17.754	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	27	VAL	0	0.021	0.025	19.655	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	28	ARG	1	0.850	0.925	22.184	-0.048	-0.048	0.000	0.000	0.000	0.000
23	A	29	PHE	0	0.008	0.013	20.631	0.000	0.000	0.000	0.000	0.000	0.000
24	A	30	SER	0	0.024	0.000	26.461	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	31	HIS	0	-0.041	-0.016	26.216	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	32	ALA	0	0.027	-0.001	27.965	0.003	0.003	0.000	0.000	0.000	0.000
27	A	33	ILE	0	-0.034	-0.001	22.489	0.002	0.002	0.000	0.000	0.000	0.000
28	A	34	ALA	0	0.006	-0.008	22.668	-0.007	-0.007	0.000	0.000	0.000	0.000
29	A	35	PHE	0	-0.022	-0.010	17.570	0.005	0.005	0.000	0.000	0.000	0.000
30	A	36	ALA	0	0.074	0.049	15.331	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	37	PRO	0	0.060	0.029	12.858	0.020	0.020	0.000	0.000	0.000	0.000
32	A	38	GLU	-1	-0.827	-0.881	8.249	0.484	0.484	0.000	0.000	0.000	0.000
33	A	39	GLY	0	0.002	0.003	10.840	-0.066	-0.066	0.000	0.000	0.000	0.000
34	A	40	PRO	0	-0.007	-0.011	12.495	0.004	0.004	0.000	0.000	0.000	0.000
35	A	41	VAL	0	0.004	0.015	15.204	-0.008	-0.008	0.000	0.000	0.000	0.000
36	A	42	ALA	0	-0.003	0.004	18.453	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	43	SER	0	0.020	0.012	20.823	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	44	TRP	0	-0.018	-0.030	24.560	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	45	PRO	0	-0.025	-0.019	26.807	-0.003	-0.003	0.000	0.000	0.000	0.000
40	A	46	VAL	0	-0.030	-0.006	30.271	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	47	GLN	0	0.012	-0.003	32.261	0.001	0.001	0.000	0.000	0.000	0.000
42	A	48	ARG	1	0.823	0.895	34.905	-0.029	-0.029	0.000	0.000	0.000	0.000
43	A	49	PRO	0	0.021	0.019	35.570	0.000	0.000	0.000	0.000	0.000	0.000
44	A	50	ALA	0	0.008	0.000	36.592	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	51	ASP	-1	-0.825	-0.907	36.421	0.029	0.029	0.000	0.000	0.000	0.000
46	A	52	ILE	0	0.022	0.036	32.475	0.002	0.002	0.000	0.000	0.000	0.000
47	A	53	THR	0	0.020	-0.013	33.628	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	54	ALA	0	0.086	0.048	32.298	0.003	0.003	0.000	0.000	0.000	0.000
49	A	55	SER	0	-0.050	-0.020	30.737	0.003	0.003	0.000	0.000	0.000	0.000
50	A	56	LEU	0	0.002	0.006	29.636	0.003	0.003	0.000	0.000	0.000	0.000
51	A	57	LEU	0	0.015	-0.002	27.986	0.005	0.005	0.000	0.000	0.000	0.000
52	A	58	GLN	0	0.012	-0.007	26.463	0.002	0.002	0.000	0.000	0.000	0.000
53	A	59	GLN	0	-0.031	0.007	24.879	0.005	0.005	0.000	0.000	0.000	0.000
54	A	60	ALA	0	-0.018	-0.006	23.325	0.007	0.007	0.000	0.000	0.000	0.000
55	A	61	ALA	0	0.026	0.000	21.846	0.009	0.009	0.000	0.000	0.000	0.000
56	A	62	GLY	0	-0.040	-0.021	20.777	0.004	0.004	0.000	0.000	0.000	0.000
57	A	63	LEU	0	-0.057	-0.002	15.637	0.001	0.001	0.000	0.000	0.000	0.000
58	A	64	ALA	0	0.024	0.000	14.632	0.005	0.005	0.000	0.000	0.000	0.000
59	A	88	ALA	0	0.009	-0.010	18.107	0.001	0.001	0.000	0.000	0.000	0.000
60	A	89	PRO	0	-0.086	-0.024	18.642	0.001	0.001	0.000	0.000	0.000	0.000
61	A	90	GLU	-1	-0.855	-0.944	20.029	0.017	0.017	0.000	0.000	0.000	0.000
62	A	91	VAL	0	0.000	-0.007	21.931	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	92	LEU	0	-0.024	-0.003	22.593	0.008	0.008	0.000	0.000	0.000	0.000
64	A	93	LEU	0	-0.002	-0.001	23.734	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	94	VAL	0	-0.009	-0.024	26.096	0.004	0.004	0.000	0.000	0.000	0.000
66	A	95	GLY	0	0.031	0.004	28.654	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	96	THR	0	-0.046	-0.048	30.198	0.001	0.001	0.000	0.000	0.000	0.000
68	A	97	GLY	0	0.034	0.029	32.717	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	98	ARG	1	0.912	0.954	34.377	-0.028	-0.028	0.000	0.000	0.000	0.000
70	A	99	ARG	1	0.938	0.963	36.801	-0.023	-0.023	0.000	0.000	0.000	0.000
71	A	100	GLN	0	0.029	0.028	36.150	0.001	0.001	0.000	0.000	0.000	0.000
72	A	101	HIS	0	0.007	-0.003	36.542	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	102	LEU	0	-0.015	-0.005	36.654	0.001	0.001	0.000	0.000	0.000	0.000
74	A	103	LEU	0	0.029	0.017	32.413	0.000	0.000	0.000	0.000	0.000	0.000
75	A	104	GLY	0	0.035	0.028	36.752	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	105	PRO	0	0.012	-0.007	37.075	0.001	0.001	0.000	0.000	0.000	0.000
77	A	106	GLU	-1	-0.885	-0.955	37.094	0.018	0.018	0.000	0.000	0.000	0.000
78	A	107	GLN	0	-0.051	-0.031	34.667	0.001	0.001	0.000	0.000	0.000	0.000
79	A	108	VAL	0	0.087	0.017	32.362	0.002	0.002	0.000	0.000	0.000	0.000
80	A	109	ARG	1	0.933	0.981	32.460	-0.014	-0.014	0.000	0.000	0.000	0.000
81	A	110	PRO	0	0.021	0.014	31.480	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	111	LEU	0	0.042	0.013	26.354	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	112	LEU	0	0.037	0.042	28.480	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	113	ALA	0	-0.076	-0.018	30.606	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	114	MET	0	-0.083	-0.047	25.907	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	115	GLY	0	-0.026	-0.019	26.062	0.000	0.000	0.000	0.000	0.000	0.000
87	A	116	VAL	0	-0.024	-0.002	23.839	0.001	0.001	0.000	0.000	0.000	0.000
88	A	117	GLY	0	0.020	0.014	26.220	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	118	VAL	0	-0.036	-0.029	26.838	0.004	0.004	0.000	0.000	0.000	0.000
90	A	119	GLU	-1	-0.913	-0.951	28.365	0.026	0.026	0.000	0.000	0.000	0.000
91	A	120	ALA	0	-0.022	0.001	29.677	0.004	0.004	0.000	0.000	0.000	0.000
92	A	121	MET	0	-0.043	-0.016	29.470	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	122	ASP	-1	-0.876	-0.927	32.852	0.034	0.034	0.000	0.000	0.000	0.000
94	A	123	THR	0	0.029	-0.058	29.048	0.002	0.002	0.000	0.000	0.000	0.000
95	A	124	GLN	0	-0.004	0.003	29.137	0.005	0.005	0.000	0.000	0.000	0.000
96	A	125	ALA	0	-0.021	-0.011	29.110	0.002	0.002	0.000	0.000	0.000	0.000
97	A	126	ALA	0	0.039	0.035	27.423	0.001	0.001	0.000	0.000	0.000	0.000
98	A	127	ALA	0	0.033	0.004	24.735	0.004	0.004	0.000	0.000	0.000	0.000
99	A	128	ARG	1	0.937	0.980	23.961	-0.031	-0.031	0.000	0.000	0.000	0.000
100	A	129	THR	0	0.007	-0.022	24.957	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	130	TYR	0	-0.021	-0.030	16.643	0.000	0.000	0.000	0.000	0.000	0.000
102	A	131	ASN	0	-0.009	-0.016	20.013	0.014	0.014	0.000	0.000	0.000	0.000
103	A	132	ILE	0	-0.017	0.005	19.875	0.001	0.001	0.000	0.000	0.000	0.000
104	A	133	LEU	0	0.036	0.016	20.777	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	134	MET	0	-0.043	-0.007	15.413	0.002	0.002	0.000	0.000	0.000	0.000
106	A	135	ALA	0	-0.010	-0.011	16.106	0.001	0.001	0.000	0.000	0.000	0.000
107	A	136	GLU	-1	-0.968	-0.968	17.151	0.013	0.013	0.000	0.000	0.000	0.000
108	A	137	GLY	0	-0.025	-0.014	15.218	-0.010	-0.010	0.000	0.000	0.000	0.000
109	A	138	ARG	1	0.811	0.918	15.945	-0.031	-0.031	0.000	0.000	0.000	0.000
110	A	139	ARG	1	0.797	0.881	11.114	-0.141	-0.141	0.000	0.000	0.000	0.000
111	A	140	VAL	0	0.020	0.015	17.302	-0.008	-0.008	0.000	0.000	0.000	0.000
112	A	141	VAL	0	0.004	0.000	18.098	0.018	0.018	0.000	0.000	0.000	0.000
113	A	142	VAL	0	-0.024	-0.004	20.329	-0.013	-0.013	0.000	0.000	0.000	0.000
114	A	143	ALA	0	0.031	0.022	22.882	0.007	0.007	0.000	0.000	0.000	0.000
115	A	144	LEU	0	-0.027	-0.006	24.625	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	145	LEU	0	0.025	0.020	27.817	0.002	0.002	0.000	0.000	0.000	0.000
117	A	146	PRO	0	-0.016	0.020	29.664	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	147	ASP	-1	-0.882	-0.928	31.445	0.029	0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:PRO)