FMO DATABASE

FMODB ID: MVR4Z

Calculation Name: 1B4A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1B4A

Chain ID: A

ChEMBL ID:

UniProt ID: O31408

Base Structure: X-ray

Registration Date: 2023-06-22

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	146
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1245441.75442
FMO2-HF: Nuclear repulsion	1187272.213851
FMO2-HF: Total energy	-58169.540568
FMO2-MP2: Total energy	-58337.191992

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:GLY)

Summations of interaction energy for fragment #1(A:4: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.
-1.118	1.574	0.226	-1.111	-1.807	0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.056 / q_NPA : 0.028

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	ARG	1	0.886	0.926	3.643	-1.576	-0.162	-0.002	-0.670	-0.742	0.002
4	A	7	HIS	0	0.008	-0.003	2.766	-0.926	-0.272	0.194	-0.217	-0.631	0.000
5	A	8	ILE	0	-0.021	-0.011	3.317	0.383	1.007	0.034	-0.224	-0.434	-0.001
6	A	9	LYS	1	0.946	0.980	5.570	0.797	0.797	0.000	0.000	0.000	0.000
7	A	10	ILE	0	0.007	0.011	7.707	0.195	0.195	0.000	0.000	0.000	0.000
8	A	11	ARG	1	0.923	0.965	6.960	0.889	0.889	0.000	0.000	0.000	0.000
9	A	12	GLU	-1	-0.901	-0.950	10.001	-0.195	-0.195	0.000	0.000	0.000	0.000
10	A	13	ILE	0	-0.005	-0.004	12.019	0.074	0.074	0.000	0.000	0.000	0.000
11	A	14	ILE	0	-0.050	-0.032	11.720	0.047	0.047	0.000	0.000	0.000	0.000
12	A	15	MET	0	-0.038	-0.019	13.152	0.031	0.031	0.000	0.000	0.000	0.000
13	A	16	SER	0	-0.022	0.002	15.920	0.042	0.042	0.000	0.000	0.000	0.000
14	A	17	ASN	0	-0.072	-0.032	17.782	0.027	0.027	0.000	0.000	0.000	0.000
15	A	18	ASP	-1	-0.845	-0.943	19.210	-0.166	-0.166	0.000	0.000	0.000	0.000
16	A	19	ILE	0	-0.024	0.003	16.560	0.010	0.010	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.879	-0.955	19.501	-0.121	-0.121	0.000	0.000	0.000	0.000
18	A	21	THR	0	-0.071	-0.025	21.049	0.001	0.001	0.000	0.000	0.000	0.000
19	A	22	GLN	0	0.046	0.013	16.107	-0.035	-0.035	0.000	0.000	0.000	0.000
20	A	23	ASP	-1	-0.868	-0.945	17.218	-0.098	-0.098	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.822	-0.907	18.990	-0.124	-0.124	0.000	0.000	0.000	0.000
22	A	25	LEU	0	-0.036	-0.025	12.520	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	26	VAL	0	-0.053	-0.041	14.447	-0.011	-0.011	0.000	0.000	0.000	0.000
24	A	27	ASP	-1	-0.892	-0.938	15.512	-0.037	-0.037	0.000	0.000	0.000	0.000
25	A	28	ARG	1	0.926	0.961	15.827	0.154	0.154	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.073	-0.034	9.825	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	30	ARG	1	0.884	0.928	13.220	0.058	0.058	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.903	-0.941	15.387	0.020	0.020	0.000	0.000	0.000	0.000
29	A	32	ALA	0	-0.115	-0.050	12.937	0.006	0.006	0.000	0.000	0.000	0.000
30	A	33	GLY	0	0.021	0.018	13.608	0.027	0.027	0.000	0.000	0.000	0.000
31	A	34	PHE	0	-0.056	-0.029	6.402	0.138	0.138	0.000	0.000	0.000	0.000
32	A	35	ASN	0	0.030	0.021	11.657	-0.110	-0.110	0.000	0.000	0.000	0.000
33	A	36	VAL	0	0.005	0.013	9.645	0.044	0.044	0.000	0.000	0.000	0.000
34	A	37	THR	0	0.049	0.037	12.521	-0.033	-0.033	0.000	0.000	0.000	0.000
35	A	38	GLN	0	0.109	0.022	13.865	-0.034	-0.034	0.000	0.000	0.000	0.000
36	A	39	ALA	0	0.002	0.006	15.475	-0.029	-0.029	0.000	0.000	0.000	0.000
37	A	40	THR	0	-0.054	-0.046	9.089	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	41	VAL	0	0.061	0.041	10.590	-0.081	-0.081	0.000	0.000	0.000	0.000
39	A	42	SER	0	-0.014	-0.018	11.884	-0.053	-0.053	0.000	0.000	0.000	0.000
40	A	43	ARG	1	0.916	0.962	9.396	0.197	0.197	0.000	0.000	0.000	0.000
41	A	44	ASP	-1	-0.738	-0.859	7.767	-0.719	-0.719	0.000	0.000	0.000	0.000
42	A	45	ILE	0	-0.005	0.008	9.477	-0.069	-0.069	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.950	0.975	12.591	0.234	0.234	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.961	-0.985	8.013	-0.733	-0.733	0.000	0.000	0.000	0.000
45	A	48	MET	0	-0.065	-0.024	6.858	-0.037	-0.037	0.000	0.000	0.000	0.000
46	A	49	GLN	0	-0.047	-0.026	9.806	0.073	0.073	0.000	0.000	0.000	0.000
47	A	50	LEU	0	-0.022	-0.006	10.913	0.025	0.025	0.000	0.000	0.000	0.000
48	A	51	VAL	0	-0.028	-0.017	14.379	0.041	0.041	0.000	0.000	0.000	0.000
49	A	52	LYS	1	0.932	0.964	18.091	0.162	0.162	0.000	0.000	0.000	0.000
50	A	53	VAL	0	-0.018	-0.006	20.528	0.012	0.012	0.000	0.000	0.000	0.000
51	A	54	PRO	0	0.028	0.020	22.924	0.000	0.000	0.000	0.000	0.000	0.000
52	A	55	MET	0	-0.053	-0.009	24.606	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	56	ALA	0	0.010	0.000	26.709	0.005	0.005	0.000	0.000	0.000	0.000
54	A	57	ASN	0	0.061	0.013	28.846	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	58	GLY	0	0.077	0.048	29.950	0.006	0.006	0.000	0.000	0.000	0.000
56	A	59	ARG	1	0.870	0.951	26.963	0.092	0.092	0.000	0.000	0.000	0.000
57	A	60	TYR	0	-0.014	-0.021	23.917	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	61	LYS	1	0.965	1.004	20.388	0.182	0.182	0.000	0.000	0.000	0.000
59	A	62	TYR	0	-0.032	-0.030	16.115	0.004	0.004	0.000	0.000	0.000	0.000
60	A	63	SER	0	-0.048	-0.063	16.623	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	64	LEU	0	0.053	0.032	10.836	-0.035	-0.035	0.000	0.000	0.000	0.000
62	A	65	PRO	0	0.038	0.027	12.479	0.050	0.050	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.033	-0.040	14.097	0.021	0.021	0.000	0.000	0.000	0.000
64	A	67	ASP	-1	-0.807	-0.867	16.143	-0.189	-0.189	0.000	0.000	0.000	0.000
65	A	68	GLN	0	-0.037	-0.024	18.902	0.012	0.012	0.000	0.000	0.000	0.000
66	A	69	ARG	1	0.922	0.982	21.951	0.163	0.163	0.000	0.000	0.000	0.000
67	A	70	PHE	0	0.045	0.029	22.741	0.012	0.012	0.000	0.000	0.000	0.000
68	A	71	ASN	0	-0.034	-0.041	21.973	-0.013	-0.013	0.000	0.000	0.000	0.000
69	A	72	PRO	0	0.128	0.061	23.642	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	73	LEU	0	0.107	0.034	25.428	0.001	0.001	0.000	0.000	0.000	0.000
71	A	74	GLN	0	-0.070	-0.032	22.613	0.010	0.010	0.000	0.000	0.000	0.000
72	A	75	LYS	1	0.861	0.953	19.148	0.207	0.207	0.000	0.000	0.000	0.000
73	A	76	LEU	0	0.053	0.039	22.995	0.001	0.001	0.000	0.000	0.000	0.000
74	A	77	LYS	1	0.949	0.969	26.425	0.098	0.098	0.000	0.000	0.000	0.000
75	A	78	ARG	1	0.875	0.942	20.621	0.164	0.164	0.000	0.000	0.000	0.000
76	A	79	ALA	0	0.089	0.055	23.681	0.002	0.002	0.000	0.000	0.000	0.000
77	A	80	LEU	0	0.000	-0.009	24.563	0.007	0.007	0.000	0.000	0.000	0.000
78	A	81	VAL	0	-0.084	-0.039	25.578	0.007	0.007	0.000	0.000	0.000	0.000
79	A	82	ASP	-1	-0.913	-0.938	22.447	-0.125	-0.125	0.000	0.000	0.000	0.000
80	A	83	VAL	0	-0.054	-0.034	25.119	0.007	0.007	0.000	0.000	0.000	0.000
81	A	84	PHE	0	0.008	0.002	27.712	0.007	0.007	0.000	0.000	0.000	0.000
82	A	85	ILE	0	-0.043	-0.004	31.154	0.002	0.002	0.000	0.000	0.000	0.000
83	A	86	LYS	1	0.848	0.912	34.094	0.046	0.046	0.000	0.000	0.000	0.000
84	A	87	LEU	0	0.001	0.013	36.759	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	88	ASP	-1	-0.873	-0.929	38.764	-0.041	-0.041	0.000	0.000	0.000	0.000
86	A	89	GLY	0	0.038	0.004	41.728	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	90	THR	0	-0.056	-0.011	44.323	0.002	0.002	0.000	0.000	0.000	0.000
88	A	91	GLY	0	0.040	0.023	47.222	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	92	ASN	0	-0.061	-0.041	45.872	0.001	0.001	0.000	0.000	0.000	0.000
90	A	93	LEU	0	0.013	0.014	43.227	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	94	LEU	0	-0.020	-0.013	39.187	0.001	0.001	0.000	0.000	0.000	0.000
92	A	95	VAL	0	-0.013	-0.008	39.149	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	96	LEU	0	0.018	0.006	32.236	0.001	0.001	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.932	0.965	35.019	0.045	0.045	0.000	0.000	0.000	0.000
95	A	98	THR	0	0.030	-0.006	29.567	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	99	LEU	0	0.005	0.010	26.555	0.005	0.005	0.000	0.000	0.000	0.000
97	A	100	PRO	0	0.013	-0.006	29.252	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	101	GLY	0	0.031	0.028	27.292	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	102	ASN	0	-0.060	-0.041	24.677	-0.015	-0.015	0.000	0.000	0.000	0.000
100	A	103	ALA	0	0.006	0.014	26.987	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	104	HIS	0	0.065	0.009	26.911	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	105	ALA	0	0.018	0.011	23.897	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	106	ILE	0	0.000	-0.009	25.540	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	107	GLY	0	0.061	0.013	28.031	0.001	0.001	0.000	0.000	0.000	0.000
105	A	108	VAL	0	0.020	0.030	24.871	0.000	0.000	0.000	0.000	0.000	0.000
106	A	109	LEU	0	-0.071	-0.036	23.304	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	110	LEU	0	-0.030	-0.038	27.166	0.001	0.001	0.000	0.000	0.000	0.000
108	A	111	ASP	-1	-0.881	-0.937	30.142	-0.078	-0.078	0.000	0.000	0.000	0.000
109	A	112	ASN	0	-0.072	-0.039	25.227	0.003	0.003	0.000	0.000	0.000	0.000
110	A	113	LEU	0	-0.121	-0.054	29.119	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	114	ASP	-1	-0.935	-0.949	31.081	-0.080	-0.080	0.000	0.000	0.000	0.000
112	A	115	TRP	0	-0.047	-0.024	33.337	0.003	0.003	0.000	0.000	0.000	0.000
113	A	116	ASP	-1	-0.836	-0.918	36.639	-0.057	-0.057	0.000	0.000	0.000	0.000
114	A	117	GLU	-1	-0.979	-1.007	39.249	-0.057	-0.057	0.000	0.000	0.000	0.000
115	A	118	ILE	0	-0.022	-0.020	35.583	0.003	0.003	0.000	0.000	0.000	0.000
116	A	119	VAL	0	-0.088	-0.034	38.798	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.061	0.024	37.195	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	121	THR	0	-0.050	-0.022	33.780	0.002	0.002	0.000	0.000	0.000	0.000
119	A	122	ILE	0	0.020	0.023	35.547	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	123	CYS	0	-0.045	0.007	30.702	0.001	0.001	0.000	0.000	0.000	0.000
121	A	124	GLY	0	0.006	0.021	33.902	0.002	0.002	0.000	0.000	0.000	0.000
122	A	125	ASP	-1	-0.859	-0.931	31.156	-0.062	-0.062	0.000	0.000	0.000	0.000
123	A	126	ASP	-1	-0.924	-0.973	30.542	-0.058	-0.058	0.000	0.000	0.000	0.000
124	A	127	THR	0	-0.072	-0.050	32.618	0.003	0.003	0.000	0.000	0.000	0.000
125	A	128	CYS	0	-0.045	-0.032	32.909	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	129	LEU	0	0.000	0.007	35.017	0.002	0.002	0.000	0.000	0.000	0.000
127	A	130	ILE	0	0.048	0.018	35.213	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	131	ILE	0	-0.009	-0.005	38.357	0.003	0.003	0.000	0.000	0.000	0.000
129	A	132	CYS	0	0.018	0.020	40.762	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	133	ARG	1	0.923	0.979	42.102	0.052	0.052	0.000	0.000	0.000	0.000
131	A	134	THR	0	0.008	-0.008	45.218	0.003	0.003	0.000	0.000	0.000	0.000
132	A	135	PRO	0	0.059	0.010	46.234	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	136	LYS	1	0.946	0.972	47.012	0.039	0.039	0.000	0.000	0.000	0.000
134	A	137	ASP	-1	-0.814	-0.921	43.317	-0.048	-0.048	0.000	0.000	0.000	0.000
135	A	138	ALA	0	0.046	0.033	42.518	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	139	LYS	1	0.942	0.957	42.295	0.038	0.038	0.000	0.000	0.000	0.000
137	A	140	LYS	1	0.840	0.930	42.079	0.049	0.049	0.000	0.000	0.000	0.000
138	A	141	VAL	0	0.084	0.042	36.990	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	142	SER	0	0.019	0.010	37.835	-0.003	-0.003	0.000	0.000	0.000	0.000
140	A	143	ASN	0	-0.030	-0.027	38.582	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	144	GLN	0	0.018	0.032	34.361	0.002	0.002	0.000	0.000	0.000	0.000
142	A	145	LEU	0	0.005	-0.010	32.797	-0.004	-0.004	0.000	0.000	0.000	0.000
143	A	146	LEU	0	0.029	0.001	34.009	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	147	SER	0	-0.096	-0.029	35.532	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	148	MET	0	-0.091	-0.042	30.516	-0.005	-0.005	0.000	0.000	0.000	0.000
146	A	149	LEU	0	-0.023	0.012	30.616	-0.005	-0.005	0.000	0.000	0.000	0.000

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