FMO DATABASE

FMODB ID: QV2VY

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	OptH
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	-1570213.736957
FMO2-HF: Nuclear repulsion	1508308.762198
FMO2-HF: Total energy	-61904.974759
FMO2-MP2: Total energy	-62084.113039

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.
-2.901	2.582	0.546	-2.082	-3.947	0

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 : 0.081 / q_NPA : 0.013

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].
3	A	6	GLU	-1	-0.953	-0.971	2.612	-2.051	1.109	0.066	-1.335	-1.891
4	A	7	ILE	0	-0.038	-0.001	2.684	-0.460	0.823	0.391	-0.488	-1.186
5	A	8	ASP	-1	-0.823	-0.880	4.767	-0.396	-0.395	-0.001	-0.006	0.006
6	A	9	PRO	0	0.014	-0.013	7.054	0.121	0.121	0.000	0.000	0.000
7	A	10	SER	0	-0.065	-0.058	8.943	0.042	0.042	0.000	0.000	0.000
8	A	11	LYS	1	0.840	0.915	10.844	-0.057	-0.057	0.000	0.000	0.000
9	A	12	ILE	0	-0.004	0.010	7.938	0.028	0.028	0.000	0.000	0.000
10	A	13	PRO	0	-0.013	0.008	12.187	0.006	0.006	0.000	0.000	0.000
11	A	14	GLY	0	0.004	-0.007	15.781	0.007	0.007	0.000	0.000	0.000
12	A	15	GLU	-1	-0.946	-0.990	18.677	0.047	0.047	0.000	0.000	0.000
13	A	16	TRP	0	-0.097	-0.035	14.077	0.008	0.008	0.000	0.000	0.000
14	A	17	ARG	1	0.898	0.948	19.702	-0.079	-0.079	0.000	0.000	0.000
15	A	18	ILE	0	0.019	0.019	19.375	0.014	0.014	0.000	0.000	0.000
16	A	19	ILE	0	-0.078	-0.038	20.193	-0.014	-0.014	0.000	0.000	0.000
17	A	20	TYR	0	-0.028	-0.029	19.786	-0.019	-0.019	0.000	0.000	0.000
18	A	21	ALA	0	0.058	0.044	19.221	0.011	0.011	0.000	0.000	0.000
19	A	22	ALA	0	0.024	0.019	18.413	-0.009	-0.009	0.000	0.000	0.000
20	A	23	ALA	0	0.046	0.016	18.628	0.007	0.007	0.000	0.000	0.000
21	A	24	ASP	-1	-0.772	-0.901	20.007	0.060	0.060	0.000	0.000	0.000
22	A	25	ASN	0	-0.070	-0.031	21.646	-0.008	-0.008	0.000	0.000	0.000
23	A	26	LYS	1	0.989	0.985	24.212	-0.052	-0.052	0.000	0.000	0.000
24	A	27	ASP	-1	-0.835	-0.899	25.701	0.042	0.042	0.000	0.000	0.000
25	A	28	LYS	1	0.894	0.926	23.377	-0.040	-0.040	0.000	0.000	0.000
26	A	29	ILE	0	0.005	0.017	21.311	0.000	0.000	0.000	0.000	0.000
27	A	30	VAL	0	0.006	0.024	24.708	0.002	0.002	0.000	0.000	0.000
28	A	31	GLU	-1	-0.951	-0.998	28.206	0.044	0.044	0.000	0.000	0.000
29	A	32	GLY	0	-0.043	-0.023	30.294	-0.003	-0.003	0.000	0.000	0.000
30	A	33	GLY	0	-0.006	0.015	27.696	-0.003	-0.003	0.000	0.000	0.000
31	A	34	PRO	0	-0.026	-0.016	25.623	0.002	0.002	0.000	0.000	0.000
32	A	35	LEU	0	-0.005	-0.010	20.276	0.000	0.000	0.000	0.000	0.000
33	A	36	ARG	1	0.762	0.873	22.024	-0.052	-0.052	0.000	0.000	0.000
34	A	37	ASN	0	0.042	0.021	20.889	-0.013	-0.013	0.000	0.000	0.000
35	A	38	TYR	0	-0.037	-0.036	22.434	0.008	0.008	0.000	0.000	0.000
36	A	39	TYR	0	-0.032	-0.039	16.712	-0.009	-0.009	0.000	0.000	0.000
37	A	40	ARG	1	0.666	0.804	21.757	-0.057	-0.057	0.000	0.000	0.000
38	A	41	ARG	1	0.856	0.914	20.630	-0.030	-0.030	0.000	0.000	0.000
39	A	42	ILE	0	0.013	0.027	14.447	0.000	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.838	-0.899	17.707	0.025	0.025	0.000	0.000	0.000
41	A	44	CYS	0	-0.055	-0.021	10.923	-0.011	-0.011	0.000	0.000	0.000
42	A	45	ILE	0	0.002	-0.002	16.002	-0.004	-0.004	0.000	0.000	0.000
43	A	46	ASN	0	-0.053	-0.040	16.018	-0.005	-0.005	0.000	0.000	0.000
44	A	47	ASP	-1	-0.872	-0.931	13.959	-0.083	-0.083	0.000	0.000	0.000
45	A	49	GLU	-1	-0.809	-0.876	11.417	-0.084	-0.084	0.000	0.000	0.000
46	A	50	SER	0	-0.028	-0.042	13.300	0.007	0.007	0.000	0.000	0.000
47	A	51	LEU	0	-0.008	0.013	11.547	-0.001	-0.001	0.000	0.000	0.000
48	A	52	SER	0	-0.007	0.004	15.593	-0.002	-0.002	0.000	0.000	0.000
49	A	53	ILE	0	0.043	0.015	15.589	0.006	0.006	0.000	0.000	0.000
50	A	54	THR	0	-0.010	-0.013	19.544	-0.006	-0.006	0.000	0.000	0.000
51	A	55	PHE	0	0.002	-0.013	22.007	0.009	0.009	0.000	0.000	0.000
52	A	56	TYR	0	0.014	0.000	24.115	-0.007	-0.007	0.000	0.000	0.000
53	A	57	LEU	0	0.064	0.051	26.358	0.005	0.005	0.000	0.000	0.000
54	A	58	LYS	1	0.866	0.921	28.432	-0.046	-0.046	0.000	0.000	0.000
55	A	59	ASP	-1	-0.897	-0.939	31.663	0.025	0.025	0.000	0.000	0.000
56	A	60	GLN	0	0.014	-0.010	34.194	-0.001	-0.001	0.000	0.000	0.000
57	A	61	GLY	0	-0.030	-0.010	35.525	-0.001	-0.001	0.000	0.000	0.000
58	A	62	THR	0	-0.033	-0.013	36.262	0.000	0.000	0.000	0.000	0.000
59	A	63	CYS	0	-0.063	-0.008	29.758	-0.002	-0.002	0.000	0.000	0.000
60	A	64	LEU	0	0.021	0.006	31.278	-0.002	-0.002	0.000	0.000	0.000
61	A	65	LEU	0	-0.036	-0.016	27.392	0.003	0.003	0.000	0.000	0.000
62	A	66	LEU	0	0.002	0.006	26.148	-0.004	-0.004	0.000	0.000	0.000
63	A	67	THR	0	-0.001	-0.010	22.970	0.004	0.004	0.000	0.000	0.000
64	A	68	GLU	-1	-0.906	-0.936	21.008	0.023	0.023	0.000	0.000	0.000
65	A	69	VAL	0	-0.033	-0.024	18.848	0.003	0.003	0.000	0.000	0.000
66	A	70	ALA	0	0.001	0.017	14.846	-0.001	-0.001	0.000	0.000	0.000
67	A	71	LYS	1	0.863	0.933	15.114	0.038	0.038	0.000	0.000	0.000
68	A	72	ARG	1	0.872	0.934	7.759	0.131	0.131	0.000	0.000	0.000
69	A	73	GLN	0	-0.075	-0.030	10.575	0.009	0.009	0.000	0.000	0.000
70	A	74	GLU	-1	-0.881	-0.961	7.803	-0.132	-0.132	0.000	0.000	0.000
71	A	75	GLY	0	-0.010	0.008	4.172	-0.083	0.004	-0.001	-0.015	-0.070
72	A	76	TYR	0	-0.022	-0.021	3.033	-0.529	0.203	0.092	-0.202	-0.622
73	A	77	VAL	0	0.054	0.036	5.744	0.103	0.103	0.000	0.000	0.000
74	A	78	TYR	0	-0.078	-0.050	8.166	-0.032	-0.032	0.000	0.000	0.000
75	A	79	VAL	0	0.033	0.017	11.624	0.009	0.009	0.000	0.000	0.000
76	A	80	LEU	0	-0.009	-0.020	15.106	-0.002	-0.002	0.000	0.000	0.000
77	A	81	GLU	-1	-0.833	-0.856	18.343	0.015	0.015	0.000	0.000	0.000
78	A	82	PHE	0	-0.008	-0.009	21.332	0.001	0.001	0.000	0.000	0.000
79	A	83	TYR	0	-0.023	-0.016	22.502	0.002	0.002	0.000	0.000	0.000
80	A	84	GLY	0	0.035	0.034	23.466	0.002	0.002	0.000	0.000	0.000
81	A	85	THR	0	-0.051	-0.077	18.665	0.000	0.000	0.000	0.000	0.000
82	A	86	ASN	0	-0.047	-0.025	16.566	0.009	0.009	0.000	0.000	0.000
83	A	87	THR	0	0.005	0.004	11.693	-0.003	-0.003	0.000	0.000	0.000
84	A	88	LEU	0	0.011	0.002	11.169	0.014	0.014	0.000	0.000	0.000
85	A	89	GLU	-1	-0.918	-0.969	4.191	-0.286	-0.066	-0.001	-0.036	-0.184
86	A	90	VAL	0	-0.028	-0.012	6.779	0.028	0.028	0.000	0.000	0.000
87	A	91	ILE	0	-0.018	-0.011	5.428	0.231	0.231	0.000	0.000	0.000
88	A	92	HIS	0	0.004	-0.005	6.530	0.521	0.521	0.000	0.000	0.000
89	A	93	VAL	0	-0.025	-0.006	7.341	-0.203	-0.203	0.000	0.000	0.000
90	A	94	SER	0	-0.033	-0.008	9.536	-0.016	-0.016	0.000	0.000	0.000
91	A	95	GLU	-1	-0.840	-0.936	12.329	0.055	0.055	0.000	0.000	0.000
92	A	96	ASN	0	-0.017	-0.020	15.694	-0.024	-0.024	0.000	0.000	0.000
93	A	97	MET	0	-0.026	0.000	13.751	-0.009	-0.009	0.000	0.000	0.000
94	A	98	LEU	0	0.022	0.015	10.859	0.035	0.035	0.000	0.000	0.000
95	A	99	VAL	0	-0.026	-0.009	10.709	-0.058	-0.058	0.000	0.000	0.000
96	A	100	THR	0	-0.019	-0.015	9.949	0.101	0.101	0.000	0.000	0.000
97	A	101	TYR	0	-0.044	-0.062	9.252	0.000	0.000	0.000	0.000	0.000
98	A	102	VAL	0	0.027	-0.001	11.078	-0.018	-0.018	0.000	0.000	0.000
99	A	103	GLU	-1	-0.868	-0.886	12.890	0.035	0.035	0.000	0.000	0.000
100	A	104	ASN	0	-0.047	-0.043	15.346	-0.010	-0.010	0.000	0.000	0.000
101	A	105	TYR	0	-0.006	0.006	18.804	-0.002	-0.002	0.000	0.000	0.000
102	A	106	ASP	-1	-0.758	-0.861	21.414	0.026	0.026	0.000	0.000	0.000
103	A	107	GLY	0	-0.020	-0.011	24.868	-0.002	-0.002	0.000	0.000	0.000
104	A	108	GLU	-1	-1.027	-1.006	26.779	0.017	0.017	0.000	0.000	0.000
105	A	109	ARG	1	0.779	0.851	24.582	-0.035	-0.035	0.000	0.000	0.000
106	A	110	ILE	0	0.009	0.003	18.394	-0.001	-0.001	0.000	0.000	0.000
107	A	111	THR	0	-0.035	-0.009	19.717	0.001	0.001	0.000	0.000	0.000
108	A	112	LYS	1	0.838	0.936	14.485	-0.075	-0.075	0.000	0.000	0.000
109	A	113	MET	0	-0.013	-0.017	15.693	-0.005	-0.005	0.000	0.000	0.000
110	A	114	THR	0	-0.011	-0.025	12.896	0.008	0.008	0.000	0.000	0.000
111	A	115	GLU	-1	-0.829	-0.893	14.603	0.099	0.099	0.000	0.000	0.000
112	A	116	GLY	0	0.023	0.007	14.753	0.044	0.044	0.000	0.000	0.000
113	A	117	LEU	0	-0.011	-0.006	15.140	-0.036	-0.036	0.000	0.000	0.000
114	A	118	ALA	0	0.027	-0.003	16.577	0.022	0.022	0.000	0.000	0.000
115	A	119	LYS	1	0.961	1.011	17.163	-0.108	-0.108	0.000	0.000	0.000
116	A	120	GLY	0	-0.027	-0.001	20.606	-0.014	-0.014	0.000	0.000	0.000
117	A	121	THR	0	-0.004	-0.027	23.554	0.002	0.002	0.000	0.000	0.000
118	A	122	SER	0	-0.026	-0.022	23.648	-0.003	-0.003	0.000	0.000	0.000
119	A	123	PHE	0	0.057	0.043	16.763	0.006	0.006	0.000	0.000	0.000
120	A	124	THR	0	-0.019	-0.017	20.927	-0.010	-0.010	0.000	0.000	0.000
121	A	125	PRO	0	0.020	-0.013	21.692	0.011	0.011	0.000	0.000	0.000
122	A	126	GLU	-1	-0.890	-0.936	17.786	0.158	0.158	0.000	0.000	0.000
123	A	127	GLU	-1	-0.851	-0.932	17.203	0.177	0.177	0.000	0.000	0.000
124	A	128	LEU	0	-0.024	-0.017	17.185	0.025	0.025	0.000	0.000	0.000
125	A	129	GLU	-1	-0.970	-0.977	16.777	0.201	0.201	0.000	0.000	0.000
126	A	130	LYS	1	1.000	0.995	13.299	-0.248	-0.248	0.000	0.000	0.000
127	A	131	TYR	0	-0.043	-0.027	13.523	0.028	0.028	0.000	0.000	0.000
128	A	132	GLN	0	0.002	-0.007	14.810	-0.006	-0.006	0.000	0.000	0.000
129	A	133	GLN	0	0.022	0.020	12.505	-0.036	-0.036	0.000	0.000	0.000
130	A	134	LEU	0	-0.002	-0.006	8.528	0.000	0.000	0.000	0.000	0.000
131	A	135	ASN	0	0.022	0.028	11.634	0.000	0.000	0.000	0.000	0.000
132	A	136	SER	0	-0.019	-0.008	14.418	-0.029	-0.029	0.000	0.000	0.000
133	A	137	GLU	-1	-0.927	-0.964	9.047	0.396	0.396	0.000	0.000	0.000
134	A	138	ARG	1	0.869	0.946	5.918	-0.475	-0.475	0.000	0.000	0.000
135	A	139	GLY	0	-0.022	-0.003	12.538	-0.020	-0.020	0.000	0.000	0.000
136	A	140	VAL	0	-0.028	-0.005	15.056	-0.014	-0.014	0.000	0.000	0.000
137	A	141	PRO	0	0.005	0.015	17.351	0.009	0.009	0.000	0.000	0.000
138	A	142	ASN	0	0.068	0.008	17.912	0.010	0.010	0.000	0.000	0.000
139	A	143	GLU	-1	-0.950	-0.974	21.157	0.076	0.076	0.000	0.000	0.000
140	A	144	ASN	0	-0.101	-0.054	22.885	-0.010	-0.010	0.000	0.000	0.000
141	A	145	ILE	0	-0.037	-0.003	20.086	0.002	0.002	0.000	0.000	0.000
142	A	146	GLU	-1	-0.868	-0.919	23.092	0.054	0.054	0.000	0.000	0.000
143	A	147	ASN	0	-0.017	-0.029	23.818	0.006	0.006	0.000	0.000	0.000
144	A	148	LEU	0	0.041	0.012	22.456	-0.008	-0.008	0.000	0.000	0.000
145	A	149	ILE	0	0.018	0.021	24.926	-0.008	-0.008	0.000	0.000	0.000
146	A	150	LYS	1	0.881	0.937	26.599	-0.069	-0.069	0.000	0.000	0.000
147	A	151	THR	0	0.001	0.035	28.993	-0.004	-0.004	0.000	0.000	0.000
148	A	152	ASP	-1	-0.791	-0.873	26.682	0.055	0.055	0.000	0.000	0.000
149	A	153	ASN	0	-0.039	-0.021	29.536	0.001	0.001	0.000	0.000	0.000
150	A	155	PRO	0	0.006	0.009	31.402	0.001	0.001	0.000	0.000	0.000
151	A	156	PRO	0	0.041	0.029	28.396	0.001	0.001	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:4:PRO)