FMO DATABASE

FMODB ID: ZV67N

Calculation Name: 2P38-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2P38

Chain ID: A

ChEMBL ID:

UniProt ID: Q9V219

Base Structure: X-ray

Registration Date: 2023-09-21

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	155
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1547657.111973
FMO2-HF: Nuclear repulsion	1485797.245359
FMO2-HF: Total energy	-61859.866614
FMO2-MP2: Total energy	-62044.81973

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:5:LEU)

Summations of interaction energy for fragment #1(A:5:LEU)

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.
-11.633	-6.937	6.643	-2.845	-8.494	-0.017

Interaction energy analysis for fragmet #1(A:5:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.008 / q_NPA : 0.000

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	7	VAL	0	-0.033	-0.025	3.225	-1.655	0.738	0.046	-1.082	-1.356	0.004
4	A	8	ARG	1	0.710	0.826	5.456	1.435	1.435	0.000	0.000	0.000	0.000
5	A	9	ARG	1	0.912	0.950	9.137	0.926	0.926	0.000	0.000	0.000	0.000
6	A	10	ALA	0	-0.066	-0.022	11.839	-0.108	-0.108	0.000	0.000	0.000	0.000
7	A	11	SER	0	-0.005	-0.033	13.360	0.055	0.055	0.000	0.000	0.000	0.000
8	A	12	SER	0	0.008	-0.014	15.917	0.034	0.034	0.000	0.000	0.000	0.000
9	A	13	TRP	0	0.006	-0.006	16.614	0.029	0.029	0.000	0.000	0.000	0.000
10	A	14	GLU	-1	-0.732	-0.801	12.084	-0.652	-0.652	0.000	0.000	0.000	0.000
11	A	15	LEU	0	0.042	0.017	16.060	0.035	0.035	0.000	0.000	0.000	0.000
12	A	16	ASP	-1	-0.808	-0.898	18.339	-0.183	-0.183	0.000	0.000	0.000	0.000
13	A	17	LEU	0	-0.085	-0.042	16.781	0.034	0.034	0.000	0.000	0.000	0.000
14	A	18	ILE	0	-0.051	-0.025	14.286	0.031	0.031	0.000	0.000	0.000	0.000
15	A	19	LEU	0	0.036	0.021	18.553	0.027	0.027	0.000	0.000	0.000	0.000
16	A	20	LYS	1	0.982	0.999	22.228	0.102	0.102	0.000	0.000	0.000	0.000
17	A	21	GLU	-1	-0.847	-0.906	19.819	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	22	ALA	0	0.038	0.007	22.112	0.018	0.018	0.000	0.000	0.000	0.000
19	A	23	GLU	-1	-0.877	-0.933	23.614	-0.086	-0.086	0.000	0.000	0.000	0.000
20	A	24	LYS	1	0.663	0.805	23.435	0.030	0.030	0.000	0.000	0.000	0.000
21	A	25	TYR	0	-0.093	-0.070	24.346	0.011	0.011	0.000	0.000	0.000	0.000
22	A	26	GLY	0	-0.001	-0.017	27.705	0.007	0.007	0.000	0.000	0.000	0.000
23	A	27	GLU	-1	-0.861	-0.916	27.853	-0.071	-0.071	0.000	0.000	0.000	0.000
24	A	28	LEU	0	-0.056	-0.031	20.511	0.009	0.009	0.000	0.000	0.000	0.000
25	A	29	LEU	0	-0.022	-0.009	24.852	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	30	HIS	0	-0.073	-0.035	17.388	0.020	0.020	0.000	0.000	0.000	0.000
27	A	31	GLU	-1	-0.882	-0.942	21.007	-0.200	-0.200	0.000	0.000	0.000	0.000
28	A	32	PHE	0	0.013	0.010	17.383	-0.031	-0.031	0.000	0.000	0.000	0.000
29	A	33	PHE	0	0.035	0.013	14.168	0.021	0.021	0.000	0.000	0.000	0.000
30	A	34	CYS	0	-0.026	-0.003	9.515	-0.052	-0.052	0.000	0.000	0.000	0.000
31	A	35	VAL	0	-0.007	-0.007	7.391	0.165	0.165	0.000	0.000	0.000	0.000
32	A	36	VAL	0	-0.002	0.005	2.362	-1.431	-0.887	2.054	-0.571	-2.028	-0.004
33	A	37	GLU	-1	-0.803	-0.881	3.903	-1.540	-1.058	0.002	-0.115	-0.369	0.000
34	A	38	GLY	0	0.042	0.001	2.364	-3.877	-1.682	3.633	-2.762	-3.066	-0.018
35	A	39	LYS	1	0.871	0.941	3.088	0.720	-1.349	0.183	2.111	-0.225	-0.001
36	A	40	TYR	0	0.014	-0.002	5.922	-0.193	-0.193	0.000	0.000	0.000	0.000
37	A	41	ARG	1	0.864	0.910	5.577	0.356	0.356	0.000	0.000	0.000	0.000
38	A	42	ASP	-1	-0.856	-0.898	5.728	0.555	0.555	0.000	0.000	0.000	0.000
39	A	43	VAL	0	0.019	0.003	7.528	-0.249	-0.249	0.000	0.000	0.000	0.000
40	A	44	TYR	0	-0.014	-0.025	5.942	0.203	0.203	0.000	0.000	0.000	0.000
41	A	45	ALA	0	0.023	0.025	10.928	-0.074	-0.074	0.000	0.000	0.000	0.000
42	A	46	VAL	0	-0.028	-0.019	11.933	0.036	0.036	0.000	0.000	0.000	0.000
43	A	47	ASN	0	0.028	-0.007	14.896	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	48	GLU	-1	-0.783	-0.882	17.301	-0.254	-0.254	0.000	0.000	0.000	0.000
45	A	49	GLU	-1	-0.876	-0.930	18.683	-0.202	-0.202	0.000	0.000	0.000	0.000
46	A	50	VAL	0	0.021	-0.001	12.879	-0.046	-0.046	0.000	0.000	0.000	0.000
47	A	51	TRP	0	-0.038	-0.030	14.293	-0.091	-0.091	0.000	0.000	0.000	0.000
48	A	52	LYS	1	0.819	0.904	15.588	0.194	0.194	0.000	0.000	0.000	0.000
49	A	53	ILE	0	0.034	0.016	13.910	-0.047	-0.047	0.000	0.000	0.000	0.000
50	A	54	ILE	0	-0.060	-0.022	8.308	-0.085	-0.085	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.867	-0.940	11.907	-0.833	-0.833	0.000	0.000	0.000	0.000
52	A	56	ASP	-1	-0.929	-0.951	14.040	-0.594	-0.594	0.000	0.000	0.000	0.000
53	A	57	ILE	0	-0.048	-0.028	11.537	-0.043	-0.043	0.000	0.000	0.000	0.000
54	A	58	ASN	0	0.009	0.000	4.665	-0.355	-0.345	-0.001	-0.011	0.002	0.000
55	A	59	MET	0	0.004	0.011	7.778	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	60	ARG	1	0.959	0.974	2.987	-2.522	-1.935	0.030	-0.178	-0.439	0.002
57	A	61	PRO	0	0.084	0.020	2.577	-0.643	-0.089	0.696	-0.237	-1.013	0.000
58	A	62	TYR	0	-0.058	-0.029	5.666	-0.103	-0.103	0.000	0.000	0.000	0.000
59	A	63	SER	0	-0.029	-0.013	8.561	-0.028	-0.028	0.000	0.000	0.000	0.000
60	A	64	LEU	0	-0.035	0.010	6.840	-0.082	-0.082	0.000	0.000	0.000	0.000
61	A	65	GLY	0	0.061	0.020	10.684	-0.031	-0.031	0.000	0.000	0.000	0.000
62	A	66	THR	0	0.016	0.017	11.536	0.067	0.067	0.000	0.000	0.000	0.000
63	A	67	PHE	0	0.016	0.016	8.976	-0.032	-0.032	0.000	0.000	0.000	0.000
64	A	68	VAL	0	0.005	0.005	11.050	0.022	0.022	0.000	0.000	0.000	0.000
65	A	69	GLY	0	0.020	0.015	11.827	0.008	0.008	0.000	0.000	0.000	0.000
66	A	70	THR	0	-0.048	-0.033	8.866	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	71	ILE	0	-0.004	0.004	10.725	0.025	0.025	0.000	0.000	0.000	0.000
68	A	72	ARG	1	0.818	0.910	11.241	-0.156	-0.156	0.000	0.000	0.000	0.000
69	A	73	VAL	0	0.051	0.041	13.690	-0.015	-0.015	0.000	0.000	0.000	0.000
70	A	74	ASP	-1	-0.857	-0.925	16.894	0.039	0.039	0.000	0.000	0.000	0.000
71	A	75	GLU	-1	-0.918	-0.956	19.697	0.078	0.078	0.000	0.000	0.000	0.000
72	A	76	ASN	0	-0.136	-0.074	22.816	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	77	LEU	0	-0.029	-0.017	21.231	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	78	VAL	0	-0.012	-0.003	21.649	-0.022	-0.022	0.000	0.000	0.000	0.000
75	A	79	GLU	-1	-0.840	-0.891	15.488	-0.211	-0.211	0.000	0.000	0.000	0.000
76	A	80	LYN	0	0.023	0.009	17.168	0.003	0.003	0.000	0.000	0.000	0.000
77	A	81	PHE	0	0.065	0.022	13.276	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	82	TYR	0	-0.032	-0.023	14.618	0.040	0.040	0.000	0.000	0.000	0.000
79	A	83	PRO	0	0.029	0.038	14.888	0.026	0.026	0.000	0.000	0.000	0.000
80	A	84	ASN	0	-0.020	-0.027	13.462	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	85	LEU	0	0.009	-0.001	16.793	-0.020	-0.020	0.000	0.000	0.000	0.000
82	A	86	GLU	-1	-0.842	-0.923	16.436	0.065	0.065	0.000	0.000	0.000	0.000
83	A	87	PHE	0	-0.013	0.001	17.100	-0.017	-0.017	0.000	0.000	0.000	0.000
84	A	88	PHE	0	-0.005	-0.022	18.491	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	89	SER	0	-0.021	-0.011	20.107	-0.010	-0.010	0.000	0.000	0.000	0.000
86	A	90	LEU	0	-0.008	-0.001	17.638	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	91	ILE	0	-0.032	-0.004	22.288	-0.013	-0.013	0.000	0.000	0.000	0.000
88	A	92	LYS	1	0.991	1.016	25.190	0.039	0.039	0.000	0.000	0.000	0.000
89	A	93	LEU	0	-0.059	-0.033	28.238	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	94	GLU	-1	-0.845	-0.905	30.013	-0.042	-0.042	0.000	0.000	0.000	0.000
91	A	95	LYS	1	0.770	0.883	30.278	0.046	0.046	0.000	0.000	0.000	0.000
92	A	96	ASN	0	-0.042	-0.025	30.077	0.006	0.006	0.000	0.000	0.000	0.000
93	A	97	TYR	0	-0.008	-0.017	30.304	0.003	0.003	0.000	0.000	0.000	0.000
94	A	98	VAL	0	-0.023	-0.026	32.219	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	99	ILE	0	0.025	0.031	33.537	0.003	0.003	0.000	0.000	0.000	0.000
96	A	100	LEU	0	-0.017	-0.008	33.585	0.000	0.000	0.000	0.000	0.000	0.000
97	A	101	GLY	0	0.030	0.014	36.887	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	102	PRO	0	0.035	0.032	37.481	0.004	0.004	0.000	0.000	0.000	0.000
99	A	103	LYS	1	0.945	0.958	37.184	-0.038	-0.038	0.000	0.000	0.000	0.000
100	A	104	ALA	0	0.022	0.008	37.296	0.004	0.004	0.000	0.000	0.000	0.000
101	A	105	SER	0	0.012	-0.007	33.786	0.003	0.003	0.000	0.000	0.000	0.000
102	A	106	PHE	0	0.022	0.018	32.648	0.005	0.005	0.000	0.000	0.000	0.000
103	A	107	LEU	0	-0.017	-0.007	32.876	0.006	0.006	0.000	0.000	0.000	0.000
104	A	108	PHE	0	0.026	0.008	27.780	0.006	0.006	0.000	0.000	0.000	0.000
105	A	109	THR	0	-0.018	-0.002	28.367	0.004	0.004	0.000	0.000	0.000	0.000
106	A	110	THR	0	-0.025	-0.012	28.992	0.006	0.006	0.000	0.000	0.000	0.000
107	A	111	GLY	0	0.052	0.029	28.089	0.002	0.002	0.000	0.000	0.000	0.000
108	A	112	LYS	1	0.767	0.886	28.765	-0.103	-0.103	0.000	0.000	0.000	0.000
109	A	113	ASP	-1	-0.821	-0.905	32.097	0.076	0.076	0.000	0.000	0.000	0.000
110	A	114	ALA	0	0.026	0.015	33.697	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	115	PRO	0	-0.043	-0.017	36.096	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	116	LYS	1	0.891	0.907	39.670	-0.027	-0.027	0.000	0.000	0.000	0.000
113	A	117	GLU	-1	-0.813	-0.864	41.196	0.037	0.037	0.000	0.000	0.000	0.000
114	A	118	ALA	0	-0.044	-0.015	39.181	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	119	VAL	0	-0.031	-0.016	37.629	0.001	0.001	0.000	0.000	0.000	0.000
116	A	120	ARG	1	0.868	0.923	39.742	-0.030	-0.030	0.000	0.000	0.000	0.000
117	A	121	GLU	-1	-0.825	-0.887	38.245	0.002	0.002	0.000	0.000	0.000	0.000
118	A	122	ILE	0	-0.036	-0.024	36.629	0.004	0.004	0.000	0.000	0.000	0.000
119	A	123	LYS	1	0.893	0.961	35.550	0.011	0.011	0.000	0.000	0.000	0.000
120	A	124	TRP	0	-0.056	-0.047	32.743	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	125	GLN	0	0.021	-0.002	34.109	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	126	GLY	0	0.061	0.031	33.676	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	127	SER	0	-0.029	-0.002	27.262	0.003	0.003	0.000	0.000	0.000	0.000
124	A	128	LYS	1	0.878	0.930	28.361	-0.023	-0.023	0.000	0.000	0.000	0.000
125	A	129	ARG	1	0.962	0.987	23.163	-0.052	-0.052	0.000	0.000	0.000	0.000
126	A	130	VAL	0	0.018	0.023	27.498	-0.009	-0.009	0.000	0.000	0.000	0.000
127	A	131	VAL	0	0.061	0.030	26.316	0.009	0.009	0.000	0.000	0.000	0.000
128	A	132	VAL	0	-0.044	-0.026	28.218	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	133	LEU	0	0.000	0.011	29.364	0.004	0.004	0.000	0.000	0.000	0.000
130	A	134	ASN	0	0.006	-0.017	31.821	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	135	ASP	-1	-0.847	-0.937	34.091	0.030	0.030	0.000	0.000	0.000	0.000
132	A	136	LEU	0	-0.046	-0.013	34.720	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	137	GLY	0	0.008	0.011	33.833	-0.004	-0.004	0.000	0.000	0.000	0.000
134	A	138	ASP	-1	-0.827	-0.897	29.593	0.035	0.035	0.000	0.000	0.000	0.000
135	A	139	ILE	0	-0.006	-0.026	24.963	0.003	0.003	0.000	0.000	0.000	0.000
136	A	140	ILE	0	-0.007	0.016	26.412	0.008	0.008	0.000	0.000	0.000	0.000
137	A	141	GLY	0	0.033	0.009	25.097	0.014	0.014	0.000	0.000	0.000	0.000
138	A	142	ILE	0	-0.076	-0.017	22.897	-0.011	-0.011	0.000	0.000	0.000	0.000
139	A	143	GLY	0	0.054	0.033	25.919	0.011	0.011	0.000	0.000	0.000	0.000
140	A	144	LEU	0	-0.060	-0.034	26.784	-0.008	-0.008	0.000	0.000	0.000	0.000
141	A	145	ILE	0	0.051	0.042	29.483	0.003	0.003	0.000	0.000	0.000	0.000
142	A	146	ASN	0	-0.042	-0.026	32.946	0.000	0.000	0.000	0.000	0.000	0.000
143	A	147	PRO	0	0.004	-0.012	35.504	0.001	0.001	0.000	0.000	0.000	0.000
144	A	148	LYS	1	0.994	1.008	38.629	-0.036	-0.036	0.000	0.000	0.000	0.000
145	A	149	SER	0	-0.035	-0.014	38.568	0.002	0.002	0.000	0.000	0.000	0.000
146	A	150	ASP	-1	-0.765	-0.879	40.019	0.030	0.030	0.000	0.000	0.000	0.000
147	A	151	ARG	1	0.818	0.857	40.860	-0.040	-0.040	0.000	0.000	0.000	0.000
148	A	152	ARG	1	0.917	0.955	35.447	-0.067	-0.067	0.000	0.000	0.000	0.000
149	A	153	PHE	0	0.033	0.034	35.980	0.001	0.001	0.000	0.000	0.000	0.000
150	A	154	ILE	0	0.007	0.001	31.816	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	155	LYS	1	0.855	0.926	30.878	-0.053	-0.053	0.000	0.000	0.000	0.000
152	A	156	ASN	0	0.023	0.000	27.403	0.002	0.002	0.000	0.000	0.000	0.000
153	A	157	LEU	0	-0.078	-0.056	23.980	-0.003	-0.003	0.000	0.000	0.000	0.000
154	A	158	LYS	1	0.820	0.914	19.474	-0.070	-0.070	0.000	0.000	0.000	0.000
155	A	159	ASP	-1	-0.841	-0.914	23.344	0.124	0.124	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LEU)