FMO DATABASE

FMODB ID: KG4G3

Calculation Name: 4WFV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4WFV

Chain ID: A

ChEMBL ID:

UniProt ID: Q28133

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	151
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1571164.2151
FMO2-HF: Nuclear repulsion	1509258.7224
FMO2-HF: Total energy	-61905.4927
FMO2-MP2: Total energy	-62084.652769

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:4:PRO)

Summations of interaction energy for fragment #1(A:4: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.
-2.464	3.16	1.118	-2.458	-4.281	0.001

Interaction energy analysis for fragmet #1(A:4:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.085 / q_NPA : 0.016

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	6	GLU	-1	-0.950	-0.971	2.572	-1.977	1.316	0.072	-1.425	-1.939	0.002
4	A	7	ILE	0	-0.048	-0.004	2.386	-0.431	0.880	0.932	-0.767	-1.474	0.000
5	A	8	ASP	-1	-0.782	-0.861	4.702	-0.431	-0.428	-0.001	-0.007	0.005	0.000
6	A	9	PRO	0	0.011	-0.010	7.141	0.141	0.141	0.000	0.000	0.000	0.000
7	A	10	SER	0	-0.069	-0.062	8.944	0.058	0.058	0.000	0.000	0.000	0.000
8	A	11	LYS	1	0.825	0.903	10.825	-0.009	-0.009	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.013	0.001	7.865	0.036	0.036	0.000	0.000	0.000	0.000
10	A	13	PRO	0	-0.006	0.010	12.186	0.011	0.011	0.000	0.000	0.000	0.000
11	A	14	GLY	0	-0.015	-0.013	15.788	0.006	0.006	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.890	-0.950	18.673	0.048	0.048	0.000	0.000	0.000	0.000
13	A	16	TRP	0	-0.088	-0.026	14.035	0.011	0.011	0.000	0.000	0.000	0.000
14	A	17	ARG	1	0.898	0.936	19.691	-0.090	-0.090	0.000	0.000	0.000	0.000
15	A	18	ILE	0	0.021	0.021	19.423	0.016	0.016	0.000	0.000	0.000	0.000
16	A	19	ILE	0	-0.080	-0.040	20.172	-0.017	-0.017	0.000	0.000	0.000	0.000
17	A	20	TYR	0	-0.018	-0.026	19.822	-0.023	-0.023	0.000	0.000	0.000	0.000
18	A	21	ALA	0	0.063	0.048	19.174	0.013	0.013	0.000	0.000	0.000	0.000
19	A	22	ALA	0	0.020	0.017	18.305	-0.012	-0.012	0.000	0.000	0.000	0.000
20	A	23	ALA	0	0.056	0.020	18.569	0.010	0.010	0.000	0.000	0.000	0.000
21	A	24	ASP	-1	-0.733	-0.864	19.873	0.092	0.092	0.000	0.000	0.000	0.000
22	A	25	ASN	0	-0.076	-0.024	21.571	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	26	LYS	1	0.917	0.942	24.172	-0.077	-0.077	0.000	0.000	0.000	0.000
24	A	27	ASP	-1	-0.843	-0.908	25.645	0.060	0.060	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.852	0.906	23.385	-0.061	-0.061	0.000	0.000	0.000	0.000
26	A	29	ILE	0	0.008	0.015	21.253	0.000	0.000	0.000	0.000	0.000	0.000
27	A	30	VAL	0	-0.013	0.018	24.686	0.002	0.002	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.870	-0.958	28.175	0.057	0.057	0.000	0.000	0.000	0.000
29	A	32	GLY	0	-0.042	-0.021	30.324	-0.003	-0.003	0.000	0.000	0.000	0.000
30	A	33	GLY	0	-0.001	0.019	27.694	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	34	PRO	0	-0.009	-0.008	25.662	0.002	0.002	0.000	0.000	0.000	0.000
32	A	35	LEU	0	-0.011	-0.014	20.268	0.000	0.000	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.774	0.873	22.033	-0.068	-0.068	0.000	0.000	0.000	0.000
34	A	37	ASN	0	0.027	0.017	21.222	-0.015	-0.015	0.000	0.000	0.000	0.000
35	A	38	TYR	0	-0.030	-0.037	22.451	0.011	0.011	0.000	0.000	0.000	0.000
36	A	39	TYR	0	-0.031	-0.050	16.475	-0.014	-0.014	0.000	0.000	0.000	0.000
37	A	40	ARG	1	0.659	0.794	21.771	-0.068	-0.068	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.775	0.867	20.642	-0.030	-0.030	0.000	0.000	0.000	0.000
39	A	42	ILE	0	0.003	0.022	14.490	0.001	0.001	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.801	-0.881	17.764	0.015	0.015	0.000	0.000	0.000	0.000
41	A	44	CYS	0	-0.054	-0.025	10.867	-0.018	-0.018	0.000	0.000	0.000	0.000
42	A	45	ILE	0	0.004	0.003	15.882	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	46	ASN	0	-0.047	-0.039	15.917	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.873	-0.932	14.135	-0.114	-0.114	0.000	0.000	0.000	0.000
45	A	49	GLU	-1	-0.756	-0.826	11.301	-0.127	-0.127	0.000	0.000	0.000	0.000
46	A	50	SER	0	-0.046	-0.045	13.226	0.010	0.010	0.000	0.000	0.000	0.000
47	A	51	LEU	0	-0.006	0.014	11.225	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	52	SER	0	0.017	0.012	15.382	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	53	ILE	0	0.009	0.000	15.247	0.006	0.006	0.000	0.000	0.000	0.000
50	A	54	THR	0	-0.012	-0.011	19.521	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	55	PHE	0	0.002	-0.013	22.072	0.010	0.010	0.000	0.000	0.000	0.000
52	A	56	TYR	0	0.021	0.001	24.144	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	57	LEU	0	0.064	0.046	26.385	0.006	0.006	0.000	0.000	0.000	0.000
54	A	58	LYS	1	0.804	0.885	28.473	-0.059	-0.059	0.000	0.000	0.000	0.000
55	A	59	ASP	-1	-0.841	-0.920	31.700	0.033	0.033	0.000	0.000	0.000	0.000
56	A	60	GLN	0	-0.053	-0.036	34.237	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	61	GLY	0	-0.026	-0.009	35.549	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	62	THR	0	-0.040	-0.012	36.332	0.000	0.000	0.000	0.000	0.000	0.000
59	A	63	CYS	0	-0.056	-0.007	29.769	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	64	LEU	0	0.014	0.002	31.198	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	65	LEU	0	-0.039	-0.016	27.323	0.003	0.003	0.000	0.000	0.000	0.000
62	A	66	LEU	0	-0.009	0.004	26.002	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	67	THR	0	0.006	-0.011	22.828	0.006	0.006	0.000	0.000	0.000	0.000
64	A	68	GLU	-1	-0.889	-0.925	20.764	0.026	0.026	0.000	0.000	0.000	0.000
65	A	69	VAL	0	-0.045	-0.029	18.661	0.002	0.002	0.000	0.000	0.000	0.000
66	A	70	ALA	0	-0.001	0.015	14.701	0.000	0.000	0.000	0.000	0.000	0.000
67	A	71	LYS	1	0.844	0.911	14.599	0.066	0.066	0.000	0.000	0.000	0.000
68	A	72	ARG	1	0.860	0.925	8.040	0.189	0.189	0.000	0.000	0.000	0.000
69	A	73	GLN	0	-0.076	-0.038	10.468	0.015	0.015	0.000	0.000	0.000	0.000
70	A	74	GLU	-1	-0.888	-0.962	7.687	-0.217	-0.217	0.000	0.000	0.000	0.000
71	A	75	GLY	0	-0.012	0.005	4.174	-0.080	0.006	-0.001	-0.015	-0.070	0.000
72	A	76	TYR	0	-0.021	-0.022	2.886	-0.563	0.203	0.117	-0.227	-0.656	-0.001
73	A	77	VAL	0	0.051	0.034	5.532	0.145	0.145	0.000	0.000	0.000	0.000
74	A	78	TYR	0	-0.076	-0.053	7.962	-0.051	-0.051	0.000	0.000	0.000	0.000
75	A	79	VAL	0	0.026	0.013	11.422	0.016	0.016	0.000	0.000	0.000	0.000
76	A	80	LEU	0	-0.003	-0.011	14.913	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	81	GLU	-1	-0.850	-0.893	18.123	0.023	0.023	0.000	0.000	0.000	0.000
78	A	82	PHE	0	-0.012	-0.013	21.455	0.001	0.001	0.000	0.000	0.000	0.000
79	A	83	TYR	0	-0.025	-0.009	22.573	0.003	0.003	0.000	0.000	0.000	0.000
80	A	84	GLY	0	0.040	0.035	23.529	0.004	0.004	0.000	0.000	0.000	0.000
81	A	85	THR	0	-0.038	-0.037	18.667	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	86	ASN	0	-0.060	-0.042	16.790	0.013	0.013	0.000	0.000	0.000	0.000
83	A	87	THR	0	0.015	0.014	11.748	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	88	LEU	0	0.005	-0.004	11.203	0.020	0.020	0.000	0.000	0.000	0.000
85	A	89	GLU	-1	-0.912	-0.967	4.411	-0.053	0.112	-0.001	-0.017	-0.147	0.000
86	A	90	VAL	0	-0.021	-0.010	6.895	0.039	0.039	0.000	0.000	0.000	0.000
87	A	91	ILE	0	-0.019	-0.009	5.453	0.281	0.281	0.000	0.000	0.000	0.000
88	A	92	HIS	0	0.007	-0.006	6.482	0.588	0.588	0.000	0.000	0.000	0.000
89	A	93	VAL	0	-0.025	-0.006	7.253	-0.222	-0.222	0.000	0.000	0.000	0.000
90	A	94	SER	0	-0.038	-0.008	9.466	-0.029	-0.029	0.000	0.000	0.000	0.000
91	A	95	GLU	-1	-0.827	-0.927	12.260	0.045	0.045	0.000	0.000	0.000	0.000
92	A	96	ASN	0	-0.027	-0.029	15.632	-0.026	-0.026	0.000	0.000	0.000	0.000
93	A	97	MET	0	-0.033	-0.003	14.211	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	98	LEU	0	0.032	0.018	10.798	0.032	0.032	0.000	0.000	0.000	0.000
95	A	99	VAL	0	-0.026	-0.011	10.683	-0.064	-0.064	0.000	0.000	0.000	0.000
96	A	100	THR	0	-0.025	-0.027	9.943	0.122	0.122	0.000	0.000	0.000	0.000
97	A	101	TYR	0	-0.054	-0.070	9.224	0.001	0.001	0.000	0.000	0.000	0.000
98	A	102	VAL	0	0.031	-0.002	11.097	-0.023	-0.023	0.000	0.000	0.000	0.000
99	A	103	GLU	-1	-0.850	-0.871	12.900	0.090	0.090	0.000	0.000	0.000	0.000
100	A	104	ASN	0	-0.002	-0.015	15.360	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	105	TYR	0	-0.032	-0.009	18.835	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	106	ASP	-1	-0.753	-0.859	21.451	0.040	0.040	0.000	0.000	0.000	0.000
103	A	107	GLY	0	-0.011	-0.006	24.910	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	108	GLU	-1	-1.006	-1.002	26.783	0.031	0.031	0.000	0.000	0.000	0.000
105	A	109	ARG	1	0.763	0.843	24.685	-0.050	-0.050	0.000	0.000	0.000	0.000
106	A	110	ILE	0	-0.001	-0.003	18.362	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	111	THR	0	-0.062	-0.027	19.682	0.001	0.001	0.000	0.000	0.000	0.000
108	A	112	LYS	1	0.847	0.925	14.581	-0.132	-0.132	0.000	0.000	0.000	0.000
109	A	113	MET	0	-0.014	-0.018	15.652	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	114	THR	0	0.002	-0.010	12.744	0.012	0.012	0.000	0.000	0.000	0.000
111	A	115	GLU	-1	-0.804	-0.862	14.572	0.126	0.126	0.000	0.000	0.000	0.000
112	A	116	GLY	0	0.018	0.003	14.744	0.052	0.052	0.000	0.000	0.000	0.000
113	A	117	LEU	0	-0.010	-0.003	15.182	-0.043	-0.043	0.000	0.000	0.000	0.000
114	A	118	ALA	0	0.022	-0.007	16.541	0.024	0.024	0.000	0.000	0.000	0.000
115	A	119	LYS	1	0.952	1.005	16.351	-0.125	-0.125	0.000	0.000	0.000	0.000
116	A	120	GLY	0	-0.025	0.009	20.567	-0.016	-0.016	0.000	0.000	0.000	0.000
117	A	121	THR	0	0.001	-0.023	23.518	0.002	0.002	0.000	0.000	0.000	0.000
118	A	122	SER	0	0.015	-0.004	23.654	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	123	PHE	0	-0.002	0.019	16.658	0.005	0.005	0.000	0.000	0.000	0.000
120	A	124	THR	0	-0.051	-0.054	20.923	-0.012	-0.012	0.000	0.000	0.000	0.000
121	A	125	PRO	0	0.025	-0.010	21.620	0.013	0.013	0.000	0.000	0.000	0.000
122	A	126	GLU	-1	-0.849	-0.903	17.817	0.189	0.189	0.000	0.000	0.000	0.000
123	A	127	GLU	-1	-0.808	-0.884	17.082	0.202	0.202	0.000	0.000	0.000	0.000
124	A	128	LEU	0	-0.036	-0.018	17.222	0.032	0.032	0.000	0.000	0.000	0.000
125	A	129	GLU	-1	-0.959	-0.978	17.085	0.267	0.267	0.000	0.000	0.000	0.000
126	A	130	LYS	1	0.951	0.960	13.564	-0.263	-0.263	0.000	0.000	0.000	0.000
127	A	131	TYR	0	-0.042	-0.029	13.966	0.039	0.039	0.000	0.000	0.000	0.000
128	A	132	GLN	0	0.004	-0.005	15.299	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	133	GLN	0	-0.025	-0.006	12.418	-0.057	-0.057	0.000	0.000	0.000	0.000
130	A	134	LEU	0	-0.007	-0.008	8.975	0.011	0.011	0.000	0.000	0.000	0.000
131	A	135	ASN	0	0.015	0.018	12.084	0.013	0.013	0.000	0.000	0.000	0.000
132	A	136	SER	0	-0.018	-0.016	14.826	-0.034	-0.034	0.000	0.000	0.000	0.000
133	A	137	GLU	-1	-0.875	-0.914	9.297	0.593	0.593	0.000	0.000	0.000	0.000
134	A	138	ARG	1	0.844	0.921	6.192	-0.787	-0.787	0.000	0.000	0.000	0.000
135	A	139	GLY	0	-0.021	0.003	12.812	-0.031	-0.031	0.000	0.000	0.000	0.000
136	A	140	VAL	0	-0.036	-0.007	14.926	-0.022	-0.022	0.000	0.000	0.000	0.000
137	A	141	PRO	0	-0.001	0.012	17.430	0.011	0.011	0.000	0.000	0.000	0.000
138	A	142	ASN	0	0.091	0.020	18.560	0.013	0.013	0.000	0.000	0.000	0.000
139	A	143	GLU	-1	-0.942	-0.976	21.570	0.110	0.110	0.000	0.000	0.000	0.000
140	A	144	ASN	0	-0.095	-0.059	22.817	-0.015	-0.015	0.000	0.000	0.000	0.000
141	A	145	ILE	0	-0.037	-0.001	20.471	0.002	0.002	0.000	0.000	0.000	0.000
142	A	146	GLU	-1	-0.816	-0.877	23.115	0.069	0.069	0.000	0.000	0.000	0.000
143	A	147	ASN	0	-0.027	-0.037	23.758	0.004	0.004	0.000	0.000	0.000	0.000
144	A	148	LEU	0	0.040	0.018	22.376	-0.010	-0.010	0.000	0.000	0.000	0.000
145	A	149	ILE	0	0.025	0.027	24.900	-0.010	-0.010	0.000	0.000	0.000	0.000
146	A	150	LYS	1	0.899	0.947	26.581	-0.084	-0.084	0.000	0.000	0.000	0.000
147	A	151	THR	0	-0.026	0.015	28.801	-0.005	-0.005	0.000	0.000	0.000	0.000
148	A	152	ASP	-1	-0.789	-0.858	26.599	0.067	0.067	0.000	0.000	0.000	0.000
149	A	153	ASN	0	-0.037	-0.021	29.531	0.001	0.001	0.000	0.000	0.000	0.000
150	A	155	PRO	0	0.013	0.010	31.402	0.001	0.001	0.000	0.000	0.000	0.000
151	A	156	PRO	0	0.032	0.024	28.396	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:4:PRO)