FMO DATABASE

FMODB ID: VQYQ1

Calculation Name: 2H30-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2H30

Chain ID: A

ChEMBL ID:

UniProt ID: P14930

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	-1423432.285572
FMO2-HF: Nuclear repulsion	1365810.865477
FMO2-HF: Total energy	-57621.420095
FMO2-MP2: Total energy	-57790.9485

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:32:ALA)

Summations of interaction energy for fragment #1(A:32:ALA)

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.
-2.317	1.968	1.53	-2.569	-3.246	0

Interaction energy analysis for fragmet #1(A:32:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.035 / 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	34	VAL	0	0.058	0.023	3.527	-1.468	1.063	0.016	-1.451	-1.096	0.007
4	A	35	PRO	0	0.041	0.011	6.178	0.413	0.413	0.000	0.000	0.000	0.000
5	A	36	HIS	0	0.017	0.030	2.402	-0.640	0.092	1.344	-0.668	-1.408	-0.004
6	A	37	THR	0	-0.001	-0.013	3.104	-0.641	0.329	0.171	-0.439	-0.702	-0.003
7	A	38	MET	0	0.021	0.012	4.550	0.177	0.229	-0.001	-0.011	-0.040	0.000
8	A	39	SER	0	-0.060	-0.043	7.012	0.109	0.109	0.000	0.000	0.000	0.000
9	A	40	THR	0	-0.074	-0.020	6.865	0.098	0.098	0.000	0.000	0.000	0.000
10	A	41	MET	0	-0.044	0.007	8.147	-0.034	-0.034	0.000	0.000	0.000	0.000
11	A	42	LYS	1	0.899	0.952	11.848	0.027	0.027	0.000	0.000	0.000	0.000
12	A	43	THR	0	0.000	-0.041	15.491	-0.041	-0.041	0.000	0.000	0.000	0.000
13	A	44	ALA	0	0.021	0.008	17.827	0.023	0.023	0.000	0.000	0.000	0.000
14	A	45	ASP	-1	-0.826	-0.878	20.967	-0.080	-0.080	0.000	0.000	0.000	0.000
15	A	46	ASN	0	-0.022	-0.015	19.811	0.025	0.025	0.000	0.000	0.000	0.000
16	A	47	ARG	1	0.861	0.943	18.773	0.103	0.103	0.000	0.000	0.000	0.000
17	A	48	PRO	0	0.059	0.022	14.754	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	49	ALA	0	0.061	0.023	12.233	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	50	SER	0	0.048	0.020	11.325	-0.038	-0.038	0.000	0.000	0.000	0.000
20	A	51	VAL	0	-0.042	-0.010	12.819	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	52	TYR	0	0.003	-0.015	15.610	0.010	0.010	0.000	0.000	0.000	0.000
22	A	53	LEU	0	-0.043	-0.001	9.918	-0.025	-0.025	0.000	0.000	0.000	0.000
23	A	54	LYS	1	0.852	0.927	13.816	0.139	0.139	0.000	0.000	0.000	0.000
24	A	55	LYS	1	1.016	0.999	11.203	0.078	0.078	0.000	0.000	0.000	0.000
25	A	56	ASP	-1	-0.896	-0.959	16.112	-0.136	-0.136	0.000	0.000	0.000	0.000
26	A	57	LYS	1	0.867	0.944	16.705	0.190	0.190	0.000	0.000	0.000	0.000
27	A	58	PRO	0	-0.006	0.014	15.643	-0.036	-0.036	0.000	0.000	0.000	0.000
28	A	59	THR	0	-0.005	-0.010	13.350	0.062	0.062	0.000	0.000	0.000	0.000
29	A	60	LEU	0	-0.011	0.006	15.424	-0.070	-0.070	0.000	0.000	0.000	0.000
30	A	61	ILE	0	-0.015	-0.013	11.896	0.034	0.034	0.000	0.000	0.000	0.000
31	A	62	LYS	1	0.850	0.923	16.342	0.224	0.224	0.000	0.000	0.000	0.000
32	A	63	PHE	0	0.015	-0.007	11.991	0.008	0.008	0.000	0.000	0.000	0.000
33	A	64	TRP	0	-0.014	-0.041	17.782	0.039	0.039	0.000	0.000	0.000	0.000
34	A	65	ALA	0	0.040	0.024	19.859	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	66	SER	0	-0.067	-0.082	22.471	0.013	0.013	0.000	0.000	0.000	0.000
36	A	67	TRP	0	-0.015	-0.009	22.730	0.009	0.009	0.000	0.000	0.000	0.000
37	A	68	CYS	0	-0.020	0.025	25.540	0.009	0.009	0.000	0.000	0.000	0.000
38	A	69	PRO	0	0.060	0.022	27.446	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	70	LEU	0	0.022	0.021	28.259	0.003	0.003	0.000	0.000	0.000	0.000
40	A	71	CYS	0	0.012	-0.003	24.309	-0.011	-0.011	0.000	0.000	0.000	0.000
41	A	72	LEU	0	-0.013	-0.011	26.408	0.001	0.001	0.000	0.000	0.000	0.000
42	A	73	SER	0	-0.083	-0.048	28.490	0.006	0.006	0.000	0.000	0.000	0.000
43	A	74	GLU	-1	-0.772	-0.840	26.448	-0.210	-0.210	0.000	0.000	0.000	0.000
44	A	75	LEU	0	-0.030	-0.003	24.451	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	76	GLY	0	0.080	0.034	27.233	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	77	GLN	0	-0.025	-0.013	27.928	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	78	ALA	0	0.012	0.002	23.845	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	79	GLU	-1	-0.823	-0.911	25.438	-0.124	-0.124	0.000	0.000	0.000	0.000
49	A	80	LYS	1	0.860	0.913	26.931	0.138	0.138	0.000	0.000	0.000	0.000
50	A	81	TRP	0	-0.045	-0.037	24.944	0.000	0.000	0.000	0.000	0.000	0.000
51	A	82	ALA	0	-0.017	-0.002	23.446	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	83	GLN	0	-0.047	-0.028	24.803	0.013	0.013	0.000	0.000	0.000	0.000
53	A	84	ASP	-1	-0.860	-0.906	27.785	-0.119	-0.119	0.000	0.000	0.000	0.000
54	A	85	ALA	0	0.066	0.020	27.935	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	86	LYS	1	0.791	0.898	28.724	0.132	0.132	0.000	0.000	0.000	0.000
56	A	87	PHE	0	0.015	-0.006	23.896	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	88	SER	0	-0.014	-0.001	23.783	-0.013	-0.013	0.000	0.000	0.000	0.000
58	A	89	SER	0	-0.021	-0.007	23.532	0.000	0.000	0.000	0.000	0.000	0.000
59	A	90	ALA	0	0.011	0.000	19.615	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	91	ASN	0	-0.053	-0.029	15.146	0.067	0.067	0.000	0.000	0.000	0.000
61	A	92	LEU	0	0.014	0.012	17.860	-0.043	-0.043	0.000	0.000	0.000	0.000
62	A	93	ILE	0	-0.027	-0.017	13.192	0.028	0.028	0.000	0.000	0.000	0.000
63	A	94	THR	0	-0.015	-0.016	17.807	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	95	VAL	0	-0.031	-0.016	12.958	0.003	0.003	0.000	0.000	0.000	0.000
65	A	96	ALA	0	0.042	0.044	16.057	0.000	0.000	0.000	0.000	0.000	0.000
66	A	97	SER	0	0.025	-0.003	14.307	-0.025	-0.025	0.000	0.000	0.000	0.000
67	A	98	PRO	0	0.028	0.002	16.463	0.013	0.013	0.000	0.000	0.000	0.000
68	A	99	GLY	0	-0.018	0.003	17.557	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	100	PHE	0	0.018	0.022	15.894	0.000	0.000	0.000	0.000	0.000	0.000
70	A	101	LEU	0	0.009	-0.002	18.321	0.006	0.006	0.000	0.000	0.000	0.000
71	A	102	HIS	0	-0.002	-0.011	20.968	0.007	0.007	0.000	0.000	0.000	0.000
72	A	103	GLU	-1	-0.769	-0.808	20.226	-0.164	-0.164	0.000	0.000	0.000	0.000
73	A	104	LYS	1	0.831	0.907	22.504	0.112	0.112	0.000	0.000	0.000	0.000
74	A	105	LYS	1	1.006	0.991	21.696	0.073	0.073	0.000	0.000	0.000	0.000
75	A	106	ASP	-1	-0.794	-0.899	18.451	-0.080	-0.080	0.000	0.000	0.000	0.000
76	A	107	GLY	0	-0.015	0.004	20.945	0.015	0.015	0.000	0.000	0.000	0.000
77	A	108	GLU	-1	-0.857	-0.931	23.878	-0.088	-0.088	0.000	0.000	0.000	0.000
78	A	109	PHE	0	-0.017	-0.010	21.249	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	110	GLN	0	0.069	0.011	19.605	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	111	LYS	1	0.878	0.955	24.224	0.056	0.056	0.000	0.000	0.000	0.000
81	A	112	TRP	0	0.048	0.013	24.841	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	113	TYR	0	0.036	0.000	24.524	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	114	ALA	0	-0.030	-0.013	26.792	0.001	0.001	0.000	0.000	0.000	0.000
84	A	115	GLY	0	-0.021	0.001	28.733	0.005	0.005	0.000	0.000	0.000	0.000
85	A	116	LEU	0	-0.060	-0.016	27.759	0.000	0.000	0.000	0.000	0.000	0.000
86	A	117	ASN	0	-0.015	-0.019	30.358	0.006	0.006	0.000	0.000	0.000	0.000
87	A	118	TYR	0	-0.016	-0.006	27.098	0.000	0.000	0.000	0.000	0.000	0.000
88	A	119	PRO	0	0.010	0.012	26.706	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	120	LYS	1	0.883	0.932	26.179	0.091	0.091	0.000	0.000	0.000	0.000
90	A	121	LEU	0	0.003	0.013	22.754	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	122	PRO	0	-0.028	-0.005	18.712	0.005	0.005	0.000	0.000	0.000	0.000
92	A	123	VAL	0	0.020	0.029	19.085	-0.024	-0.024	0.000	0.000	0.000	0.000
93	A	124	VAL	0	-0.010	-0.027	12.457	0.036	0.036	0.000	0.000	0.000	0.000
94	A	125	THR	0	-0.029	-0.009	15.763	-0.008	-0.008	0.000	0.000	0.000	0.000
95	A	126	ASP	-1	-0.803	-0.917	10.942	-0.569	-0.569	0.000	0.000	0.000	0.000
96	A	127	ASN	0	-0.045	-0.026	13.160	-0.021	-0.021	0.000	0.000	0.000	0.000
97	A	128	GLY	0	0.046	0.019	13.111	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	129	GLY	0	-0.038	-0.026	13.101	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	130	THR	0	0.013	0.004	6.712	-0.029	-0.029	0.000	0.000	0.000	0.000
100	A	131	ILE	0	-0.025	-0.026	7.029	-0.240	-0.240	0.000	0.000	0.000	0.000
101	A	132	ALA	0	0.014	0.002	8.854	-0.094	-0.094	0.000	0.000	0.000	0.000
102	A	133	GLN	0	-0.019	-0.001	10.929	0.028	0.028	0.000	0.000	0.000	0.000
103	A	134	ASN	0	-0.035	-0.019	5.204	0.315	0.315	0.000	0.000	0.000	0.000
104	A	135	LEU	0	-0.060	-0.021	8.442	-0.060	-0.060	0.000	0.000	0.000	0.000
105	A	136	ASN	0	-0.041	-0.017	10.853	0.178	0.178	0.000	0.000	0.000	0.000
106	A	137	ILE	0	-0.046	-0.013	13.769	0.091	0.091	0.000	0.000	0.000	0.000
107	A	138	SER	0	0.024	0.001	15.918	0.030	0.030	0.000	0.000	0.000	0.000
108	A	139	VAL	0	-0.065	-0.033	19.031	0.042	0.042	0.000	0.000	0.000	0.000
109	A	140	TYR	0	0.018	0.059	17.198	-0.025	-0.025	0.000	0.000	0.000	0.000
110	A	141	PRO	0	0.035	-0.018	21.905	0.023	0.023	0.000	0.000	0.000	0.000
111	A	142	SER	0	-0.044	-0.027	18.507	0.008	0.008	0.000	0.000	0.000	0.000
112	A	143	TRP	0	-0.002	-0.011	18.258	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	144	ALA	0	0.006	0.008	13.749	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	145	LEU	0	-0.026	0.007	15.772	0.046	0.046	0.000	0.000	0.000	0.000
115	A	146	ILE	0	-0.020	-0.011	10.053	-0.098	-0.098	0.000	0.000	0.000	0.000
116	A	147	GLY	0	0.103	0.050	12.690	0.136	0.136	0.000	0.000	0.000	0.000
117	A	148	LYS	1	0.814	0.897	12.636	0.184	0.184	0.000	0.000	0.000	0.000
118	A	149	ASP	-1	-0.861	-0.915	11.656	-0.255	-0.255	0.000	0.000	0.000	0.000
119	A	150	GLY	0	-0.052	-0.023	8.355	-0.023	-0.023	0.000	0.000	0.000	0.000
120	A	151	ASP	-1	-0.814	-0.897	7.998	-1.296	-1.296	0.000	0.000	0.000	0.000
121	A	152	VAL	0	-0.003	-0.020	8.513	0.177	0.177	0.000	0.000	0.000	0.000
122	A	153	GLN	0	-0.063	-0.046	11.069	0.138	0.138	0.000	0.000	0.000	0.000
123	A	154	ARG	1	0.824	0.900	14.660	0.438	0.438	0.000	0.000	0.000	0.000
124	A	155	ILE	0	0.017	0.010	12.543	-0.052	-0.052	0.000	0.000	0.000	0.000
125	A	156	VAL	0	-0.045	-0.018	16.898	0.053	0.053	0.000	0.000	0.000	0.000
126	A	157	LYS	1	0.967	0.990	20.333	0.323	0.323	0.000	0.000	0.000	0.000
127	A	158	GLY	0	0.032	0.008	21.791	0.025	0.025	0.000	0.000	0.000	0.000
128	A	159	SER	0	-0.032	-0.060	23.705	-0.022	-0.022	0.000	0.000	0.000	0.000
129	A	160	ILE	0	-0.028	-0.003	22.804	0.000	0.000	0.000	0.000	0.000	0.000
130	A	161	ASN	0	0.052	0.025	26.632	0.003	0.003	0.000	0.000	0.000	0.000
131	A	162	GLU	-1	-0.715	-0.856	28.077	-0.157	-0.157	0.000	0.000	0.000	0.000
132	A	163	ALA	0	0.012	0.005	28.681	-0.008	-0.008	0.000	0.000	0.000	0.000
133	A	164	GLN	0	0.014	-0.005	26.802	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	165	ALA	0	0.034	0.019	24.368	-0.019	-0.019	0.000	0.000	0.000	0.000
135	A	166	LEU	0	-0.002	-0.009	24.441	-0.011	-0.011	0.000	0.000	0.000	0.000
136	A	167	ALA	0	-0.066	-0.033	26.208	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	168	LEU	0	-0.006	-0.001	20.722	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	169	ILE	0	-0.033	-0.011	20.736	-0.025	-0.025	0.000	0.000	0.000	0.000
139	A	170	ARG	1	0.921	0.987	22.322	0.187	0.187	0.000	0.000	0.000	0.000
140	A	171	ASN	0	0.012	-0.010	23.191	-0.012	-0.012	0.000	0.000	0.000	0.000
141	A	172	PRO	0	0.112	0.062	18.553	0.008	0.008	0.000	0.000	0.000	0.000
142	A	173	ASN	0	-0.035	-0.019	20.346	-0.039	-0.039	0.000	0.000	0.000	0.000
143	A	174	ALA	0	-0.035	-0.002	22.476	0.024	0.024	0.000	0.000	0.000	0.000
144	A	175	ASP	-1	-0.781	-0.875	25.168	-0.213	-0.213	0.000	0.000	0.000	0.000
145	A	176	LEU	0	-0.016	-0.015	23.669	0.013	0.013	0.000	0.000	0.000	0.000
146	A	177	GLY	0	-0.002	0.008	27.888	0.010	0.010	0.000	0.000	0.000	0.000
147	A	178	SER	0	0.009	-0.021	30.345	0.014	0.014	0.000	0.000	0.000	0.000
148	A	179	LEU	0	-0.024	-0.008	30.209	0.009	0.009	0.000	0.000	0.000	0.000
149	A	180	LYS	1	0.930	0.979	31.219	0.172	0.172	0.000	0.000	0.000	0.000
150	A	181	HIS	0	-0.006	-0.002	32.731	0.000	0.000	0.000	0.000	0.000	0.000
151	A	182	SER	0	-0.033	-0.015	34.155	0.006	0.006	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:32:ALA)