FMO DATABASE

FMODB ID: 4J1JN

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	OptAll
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	-1573854.839938
FMO2-HF: Nuclear repulsion	1511949.302446
FMO2-HF: Total energy	-61905.537492
FMO2-MP2: Total energy	-62084.74462

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.
-2.07	2.973	1.16	-2.379	-3.823	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 : 0.096 / q_NPA : 0.024

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	-0.948	-0.965	3.030	-2.227	0.841	-0.001	-1.385	-1.682	0.001
4	A	7	ILE	0	-0.039	-0.005	2.485	-0.430	0.777	1.057	-0.826	-1.438	0.000
5	A	8	ASP	-1	-0.790	-0.873	4.905	-0.457	-0.421	-0.001	-0.004	-0.031	0.000
6	A	9	PRO	0	0.011	-0.003	8.318	0.144	0.144	0.000	0.000	0.000	0.000
7	A	10	SER	0	-0.081	-0.073	9.604	0.097	0.097	0.000	0.000	0.000	0.000
8	A	11	LYS	1	0.836	0.912	11.263	0.148	0.148	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.006	0.013	8.178	0.040	0.040	0.000	0.000	0.000	0.000
10	A	13	PRO	0	-0.006	0.004	12.518	0.027	0.027	0.000	0.000	0.000	0.000
11	A	14	GLY	0	0.027	0.025	16.257	0.011	0.011	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.867	-0.945	19.303	0.012	0.012	0.000	0.000	0.000	0.000
13	A	16	TRP	0	-0.098	-0.051	14.319	0.017	0.017	0.000	0.000	0.000	0.000
14	A	17	ARG	1	0.865	0.922	19.942	-0.051	-0.051	0.000	0.000	0.000	0.000
15	A	18	ILE	0	0.025	0.023	19.326	0.011	0.011	0.000	0.000	0.000	0.000
16	A	19	ILE	0	-0.075	-0.032	20.190	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	20	TYR	0	-0.034	-0.035	19.540	-0.016	-0.016	0.000	0.000	0.000	0.000
18	A	21	ALA	0	0.071	0.052	19.164	0.006	0.006	0.000	0.000	0.000	0.000
19	A	22	ALA	0	0.018	0.013	18.401	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	23	ALA	0	0.048	0.017	18.610	0.011	0.011	0.000	0.000	0.000	0.000
21	A	24	ASP	-1	-0.707	-0.847	19.853	0.115	0.115	0.000	0.000	0.000	0.000
22	A	25	ASN	0	-0.090	-0.030	21.575	-0.018	-0.018	0.000	0.000	0.000	0.000
23	A	26	LYS	1	0.897	0.941	24.136	-0.088	-0.088	0.000	0.000	0.000	0.000
24	A	27	ASP	-1	-0.849	-0.913	25.467	0.065	0.065	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.871	0.920	23.077	-0.071	-0.071	0.000	0.000	0.000	0.000
26	A	29	ILE	0	-0.004	0.010	21.477	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	30	VAL	0	0.004	0.021	24.948	0.001	0.001	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.840	-0.929	28.417	0.049	0.049	0.000	0.000	0.000	0.000
29	A	32	GLY	0	-0.027	-0.009	30.708	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	33	GLY	0	0.001	0.020	27.868	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	34	PRO	0	-0.018	-0.018	26.101	0.001	0.001	0.000	0.000	0.000	0.000
32	A	35	LEU	0	0.027	0.009	20.570	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.735	0.841	22.325	-0.062	-0.062	0.000	0.000	0.000	0.000
34	A	37	ASN	0	0.015	0.007	20.744	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	38	TYR	0	0.014	-0.014	22.293	0.008	0.008	0.000	0.000	0.000	0.000
36	A	39	TYR	0	-0.054	-0.059	16.297	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	40	ARG	1	0.646	0.782	21.922	-0.042	-0.042	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.780	0.868	20.805	0.014	0.014	0.000	0.000	0.000	0.000
39	A	42	ILE	0	0.020	0.027	14.661	0.004	0.004	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.810	-0.898	17.906	-0.046	-0.046	0.000	0.000	0.000	0.000
41	A	44	CYS	0	-0.039	-0.009	10.912	-0.045	-0.045	0.000	0.000	0.000	0.000
42	A	45	ILE	0	0.001	0.005	15.882	0.002	0.002	0.000	0.000	0.000	0.000
43	A	46	ASN	0	-0.039	-0.039	16.013	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.858	-0.920	14.109	-0.195	-0.195	0.000	0.000	0.000	0.000
45	A	49	GLU	-1	-0.770	-0.851	11.650	-0.198	-0.198	0.000	0.000	0.000	0.000
46	A	50	SER	0	-0.053	-0.046	13.662	0.024	0.024	0.000	0.000	0.000	0.000
47	A	51	LEU	0	-0.012	0.011	10.964	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	52	SER	0	0.022	0.018	15.320	0.012	0.012	0.000	0.000	0.000	0.000
49	A	53	ILE	0	0.003	-0.003	15.047	0.000	0.000	0.000	0.000	0.000	0.000
50	A	54	THR	0	-0.015	-0.009	19.360	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	55	PHE	0	-0.008	-0.013	22.101	0.007	0.007	0.000	0.000	0.000	0.000
52	A	56	TYR	0	0.032	0.004	24.282	-0.007	-0.007	0.000	0.000	0.000	0.000
53	A	57	LEU	0	0.041	0.025	26.374	0.006	0.006	0.000	0.000	0.000	0.000
54	A	58	LYS	1	0.771	0.872	28.455	-0.051	-0.051	0.000	0.000	0.000	0.000
55	A	59	ASP	-1	-0.829	-0.903	31.763	0.027	0.027	0.000	0.000	0.000	0.000
56	A	60	GLN	0	-0.069	-0.057	34.258	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	61	GLY	0	-0.005	0.007	35.548	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	62	THR	0	-0.057	-0.028	35.839	0.000	0.000	0.000	0.000	0.000	0.000
59	A	63	CYS	0	-0.040	-0.003	29.685	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	64	LEU	0	0.021	0.014	31.046	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	65	LEU	0	-0.037	-0.014	27.740	0.003	0.003	0.000	0.000	0.000	0.000
62	A	66	LEU	0	-0.014	0.001	25.915	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	67	THR	0	-0.018	-0.026	22.867	0.001	0.001	0.000	0.000	0.000	0.000
64	A	68	GLU	-1	-0.887	-0.925	20.544	0.006	0.006	0.000	0.000	0.000	0.000
65	A	69	VAL	0	-0.036	-0.031	18.926	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	70	ALA	0	0.017	0.030	14.626	0.001	0.001	0.000	0.000	0.000	0.000
67	A	71	LYS	1	0.878	0.941	14.799	0.102	0.102	0.000	0.000	0.000	0.000
68	A	72	ARG	1	0.833	0.906	8.695	0.317	0.317	0.000	0.000	0.000	0.000
69	A	73	GLN	0	-0.080	-0.043	10.636	0.026	0.026	0.000	0.000	0.000	0.000
70	A	74	GLU	-1	-0.886	-0.969	7.770	-0.254	-0.254	0.000	0.000	0.000	0.000
71	A	75	GLY	0	-0.019	0.001	4.907	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	76	TYR	0	-0.040	-0.019	2.835	-0.412	0.207	0.106	-0.160	-0.565	0.000
73	A	77	VAL	0	0.030	0.019	5.498	0.168	0.168	0.000	0.000	0.000	0.000
74	A	78	TYR	0	-0.076	-0.050	7.710	-0.067	-0.067	0.000	0.000	0.000	0.000
75	A	79	VAL	0	0.013	0.000	11.284	0.027	0.027	0.000	0.000	0.000	0.000
76	A	80	LEU	0	-0.019	-0.016	14.863	-0.012	-0.012	0.000	0.000	0.000	0.000
77	A	81	GLU	-1	-0.844	-0.894	18.120	0.021	0.021	0.000	0.000	0.000	0.000
78	A	82	PHE	0	-0.020	-0.013	21.370	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	83	TYR	0	-0.008	-0.006	22.673	0.005	0.005	0.000	0.000	0.000	0.000
80	A	84	GLY	0	0.053	0.035	23.716	0.005	0.005	0.000	0.000	0.000	0.000
81	A	85	THR	0	-0.018	-0.023	18.536	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	86	ASN	0	-0.059	-0.033	17.072	0.019	0.019	0.000	0.000	0.000	0.000
83	A	87	THR	0	0.023	0.013	11.983	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	88	LEU	0	0.011	-0.006	10.744	0.017	0.017	0.000	0.000	0.000	0.000
85	A	89	GLU	-1	-0.894	-0.953	4.783	0.321	0.434	-0.001	-0.004	-0.107	0.000
86	A	90	VAL	0	0.000	-0.011	7.005	0.052	0.052	0.000	0.000	0.000	0.000
87	A	91	ILE	0	-0.037	-0.016	5.513	0.153	0.153	0.000	0.000	0.000	0.000
88	A	92	HIS	0	0.002	-0.003	6.393	0.517	0.517	0.000	0.000	0.000	0.000
89	A	93	VAL	0	-0.008	0.001	7.607	-0.169	-0.169	0.000	0.000	0.000	0.000
90	A	94	SER	0	-0.051	-0.030	9.637	-0.015	-0.015	0.000	0.000	0.000	0.000
91	A	95	GLU	-1	-0.822	-0.918	12.468	-0.042	-0.042	0.000	0.000	0.000	0.000
92	A	96	ASN	0	-0.017	-0.011	16.042	-0.017	-0.017	0.000	0.000	0.000	0.000
93	A	97	MET	0	-0.042	-0.001	14.450	0.005	0.005	0.000	0.000	0.000	0.000
94	A	98	LEU	0	0.027	0.026	10.902	0.008	0.008	0.000	0.000	0.000	0.000
95	A	99	VAL	0	-0.038	-0.016	10.724	-0.036	-0.036	0.000	0.000	0.000	0.000
96	A	100	THR	0	-0.020	-0.028	9.916	0.088	0.088	0.000	0.000	0.000	0.000
97	A	101	TYR	0	-0.051	-0.076	9.447	0.035	0.035	0.000	0.000	0.000	0.000
98	A	102	VAL	0	0.026	0.009	11.450	-0.034	-0.034	0.000	0.000	0.000	0.000
99	A	103	GLU	-1	-0.817	-0.867	13.146	0.164	0.164	0.000	0.000	0.000	0.000
100	A	104	ASN	0	0.000	-0.007	15.543	-0.017	-0.017	0.000	0.000	0.000	0.000
101	A	105	TYR	0	-0.052	-0.046	19.008	0.003	0.003	0.000	0.000	0.000	0.000
102	A	106	ASP	-1	-0.766	-0.863	21.705	0.044	0.044	0.000	0.000	0.000	0.000
103	A	107	GLY	0	-0.011	0.002	25.240	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	108	GLU	-1	-0.986	-0.976	27.121	0.041	0.041	0.000	0.000	0.000	0.000
105	A	109	ARG	1	0.747	0.821	24.855	-0.057	-0.057	0.000	0.000	0.000	0.000
106	A	110	ILE	0	-0.002	0.001	18.581	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	111	THR	0	-0.071	-0.047	19.787	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	112	LYS	1	0.854	0.954	14.054	-0.193	-0.193	0.000	0.000	0.000	0.000
109	A	113	MET	0	-0.018	-0.016	15.743	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	114	THR	0	0.010	-0.008	12.880	0.011	0.011	0.000	0.000	0.000	0.000
111	A	115	GLU	-1	-0.808	-0.864	14.793	0.090	0.090	0.000	0.000	0.000	0.000
112	A	116	GLY	0	0.026	0.005	14.640	0.041	0.041	0.000	0.000	0.000	0.000
113	A	117	LEU	0	-0.022	-0.008	15.133	-0.034	-0.034	0.000	0.000	0.000	0.000
114	A	118	ALA	0	0.030	-0.003	16.433	0.018	0.018	0.000	0.000	0.000	0.000
115	A	119	LYS	1	0.902	0.970	16.871	-0.039	-0.039	0.000	0.000	0.000	0.000
116	A	120	GLY	0	-0.021	0.009	20.578	-0.011	-0.011	0.000	0.000	0.000	0.000
117	A	121	THR	0	-0.013	-0.027	23.324	0.001	0.001	0.000	0.000	0.000	0.000
118	A	122	SER	0	0.014	-0.004	23.511	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	123	PHE	0	0.008	0.019	16.640	0.004	0.004	0.000	0.000	0.000	0.000
120	A	124	THR	0	-0.042	-0.051	20.401	-0.008	-0.008	0.000	0.000	0.000	0.000
121	A	125	PRO	0	0.005	-0.023	21.169	0.014	0.014	0.000	0.000	0.000	0.000
122	A	126	GLU	-1	-0.829	-0.892	17.971	0.169	0.169	0.000	0.000	0.000	0.000
123	A	127	GLU	-1	-0.813	-0.883	16.568	0.168	0.168	0.000	0.000	0.000	0.000
124	A	128	LEU	0	-0.034	-0.020	16.704	0.032	0.032	0.000	0.000	0.000	0.000
125	A	129	GLU	-1	-0.943	-0.974	16.497	0.310	0.310	0.000	0.000	0.000	0.000
126	A	130	LYS	1	0.920	0.951	13.111	-0.233	-0.233	0.000	0.000	0.000	0.000
127	A	131	TYR	0	-0.030	-0.023	13.821	0.052	0.052	0.000	0.000	0.000	0.000
128	A	132	GLN	0	0.017	0.002	15.309	0.004	0.004	0.000	0.000	0.000	0.000
129	A	133	GLN	0	-0.046	-0.012	12.026	-0.075	-0.075	0.000	0.000	0.000	0.000
130	A	134	LEU	0	-0.010	-0.011	8.946	0.014	0.014	0.000	0.000	0.000	0.000
131	A	135	ASN	0	0.004	0.018	11.763	0.034	0.034	0.000	0.000	0.000	0.000
132	A	136	SER	0	-0.023	-0.025	14.460	-0.031	-0.031	0.000	0.000	0.000	0.000
133	A	137	GLU	-1	-0.876	-0.921	9.237	0.886	0.886	0.000	0.000	0.000	0.000
134	A	138	ARG	1	0.826	0.919	5.773	-1.102	-1.102	0.000	0.000	0.000	0.000
135	A	139	GLY	0	-0.025	-0.008	12.323	-0.048	-0.048	0.000	0.000	0.000	0.000
136	A	140	VAL	0	-0.044	-0.008	14.703	-0.032	-0.032	0.000	0.000	0.000	0.000
137	A	141	PRO	0	-0.009	0.007	17.263	0.011	0.011	0.000	0.000	0.000	0.000
138	A	142	ASN	0	0.077	0.016	18.880	0.010	0.010	0.000	0.000	0.000	0.000
139	A	143	GLU	-1	-0.929	-0.976	21.425	0.136	0.136	0.000	0.000	0.000	0.000
140	A	144	ASN	0	-0.093	-0.054	22.837	-0.019	-0.019	0.000	0.000	0.000	0.000
141	A	145	ILE	0	-0.016	-0.002	20.566	0.001	0.001	0.000	0.000	0.000	0.000
142	A	146	GLU	-1	-0.809	-0.871	23.124	0.069	0.069	0.000	0.000	0.000	0.000
143	A	147	ASN	0	-0.034	-0.039	23.612	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	148	LEU	0	0.054	0.042	22.425	-0.010	-0.010	0.000	0.000	0.000	0.000
145	A	149	ILE	0	0.028	0.041	24.734	-0.011	-0.011	0.000	0.000	0.000	0.000
146	A	150	LYS	1	0.887	0.944	26.478	-0.076	-0.076	0.000	0.000	0.000	0.000
147	A	151	THR	0	-0.028	-0.001	28.548	-0.003	-0.003	0.000	0.000	0.000	0.000
148	A	152	ASP	-1	-0.768	-0.841	26.481	0.048	0.048	0.000	0.000	0.000	0.000
149	A	153	ASN	0	-0.051	-0.029	29.434	0.000	0.000	0.000	0.000	0.000	0.000
150	A	155	PRO	0	0.028	0.017	31.110	0.001	0.001	0.000	0.000	0.000	0.000
151	A	156	PRO	0	0.022	0.024	28.127	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)