FMO DATABASE

FMODB ID: YVRV2

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	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	-1423603.458499
FMO2-HF: Nuclear repulsion	1365982.641974
FMO2-HF: Total energy	-57620.816525
FMO2-MP2: Total energy	-57790.437063

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.
-1.42	1.686	1.978	-2.055	-3.029	-0.004

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 : 0.021 / 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	34	VAL	0	0.056	0.021	3.374	-1.169	0.428	0.044	-0.894	-0.747	0.002
4	A	35	PRO	0	0.039	0.006	6.027	0.281	0.281	0.000	0.000	0.000	0.000
5	A	36	HIS	0	0.012	0.019	2.322	-0.425	0.007	1.650	-0.657	-1.425	-0.002
6	A	37	THR	0	0.011	-0.001	2.820	-0.856	0.159	0.284	-0.491	-0.808	-0.004
7	A	38	MET	0	0.013	0.003	4.498	0.216	0.278	0.000	-0.013	-0.049	0.000
8	A	39	SER	0	-0.063	-0.041	6.956	0.171	0.171	0.000	0.000	0.000	0.000
9	A	40	THR	0	-0.062	-0.008	6.659	0.116	0.116	0.000	0.000	0.000	0.000
10	A	41	MET	0	-0.052	0.006	8.105	0.015	0.015	0.000	0.000	0.000	0.000
11	A	42	LYS	1	0.965	0.989	11.816	0.239	0.239	0.000	0.000	0.000	0.000
12	A	43	THR	0	0.016	-0.008	15.461	-0.041	-0.041	0.000	0.000	0.000	0.000
13	A	44	ALA	0	0.032	0.017	17.771	0.014	0.014	0.000	0.000	0.000	0.000
14	A	45	ASP	-1	-0.861	-0.913	20.914	-0.149	-0.149	0.000	0.000	0.000	0.000
15	A	46	ASN	0	-0.047	-0.036	19.813	0.004	0.004	0.000	0.000	0.000	0.000
16	A	47	ARG	1	0.824	0.925	18.543	0.155	0.155	0.000	0.000	0.000	0.000
17	A	48	PRO	0	0.047	0.011	14.762	-0.030	-0.030	0.000	0.000	0.000	0.000
18	A	49	ALA	0	0.068	0.020	12.174	0.017	0.017	0.000	0.000	0.000	0.000
19	A	50	SER	0	0.026	0.017	11.490	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	51	VAL	0	-0.023	-0.004	12.754	0.024	0.024	0.000	0.000	0.000	0.000
21	A	52	TYR	0	0.011	-0.007	15.516	0.033	0.033	0.000	0.000	0.000	0.000
22	A	53	LEU	0	-0.046	-0.002	9.840	-0.008	-0.008	0.000	0.000	0.000	0.000
23	A	54	LYS	1	0.837	0.919	13.710	0.151	0.151	0.000	0.000	0.000	0.000
24	A	55	LYS	1	1.021	0.999	11.298	-0.079	-0.079	0.000	0.000	0.000	0.000
25	A	56	ASP	-1	-0.928	-0.963	16.013	0.013	0.013	0.000	0.000	0.000	0.000
26	A	57	LYS	1	0.882	0.958	16.580	0.116	0.116	0.000	0.000	0.000	0.000
27	A	58	PRO	0	-0.006	0.014	15.508	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	59	THR	0	0.003	-0.007	13.189	0.023	0.023	0.000	0.000	0.000	0.000
29	A	60	LEU	0	-0.023	0.004	15.269	-0.047	-0.047	0.000	0.000	0.000	0.000
30	A	61	ILE	0	-0.001	-0.009	11.781	0.013	0.013	0.000	0.000	0.000	0.000
31	A	62	LYS	1	0.856	0.925	16.262	0.232	0.232	0.000	0.000	0.000	0.000
32	A	63	PHE	0	0.010	-0.006	11.964	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	64	TRP	0	-0.021	-0.049	17.732	0.050	0.050	0.000	0.000	0.000	0.000
34	A	65	ALA	0	0.053	0.029	19.823	-0.025	-0.025	0.000	0.000	0.000	0.000
35	A	66	SER	0	-0.077	-0.089	22.438	0.025	0.025	0.000	0.000	0.000	0.000
36	A	67	TRP	0	-0.021	-0.006	22.542	0.022	0.022	0.000	0.000	0.000	0.000
37	A	68	CYS	0	-0.027	0.043	25.528	0.012	0.012	0.000	0.000	0.000	0.000
38	A	69	PRO	0	0.073	0.021	27.409	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	70	LEU	0	0.033	0.023	27.927	0.005	0.005	0.000	0.000	0.000	0.000
40	A	71	CYS	0	0.013	-0.008	24.180	-0.009	-0.009	0.000	0.000	0.000	0.000
41	A	72	LEU	0	-0.016	-0.014	26.362	0.002	0.002	0.000	0.000	0.000	0.000
42	A	73	SER	0	-0.088	-0.055	28.447	0.008	0.008	0.000	0.000	0.000	0.000
43	A	74	GLU	-1	-0.760	-0.849	26.427	-0.195	-0.195	0.000	0.000	0.000	0.000
44	A	75	LEU	0	-0.030	-0.008	24.355	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	76	GLY	0	0.078	0.032	27.184	0.000	0.000	0.000	0.000	0.000	0.000
46	A	77	GLN	0	-0.043	-0.019	28.516	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	78	ALA	0	0.017	0.006	23.706	0.002	0.002	0.000	0.000	0.000	0.000
48	A	79	GLU	-1	-0.825	-0.918	25.306	-0.135	-0.135	0.000	0.000	0.000	0.000
49	A	80	LYS	1	0.957	0.977	26.807	0.118	0.118	0.000	0.000	0.000	0.000
50	A	81	TRP	0	-0.019	-0.013	24.647	0.003	0.003	0.000	0.000	0.000	0.000
51	A	82	ALA	0	-0.020	-0.005	23.332	0.004	0.004	0.000	0.000	0.000	0.000
52	A	83	GLN	0	-0.043	-0.027	24.671	0.012	0.012	0.000	0.000	0.000	0.000
53	A	84	ASP	-1	-0.848	-0.897	27.657	-0.084	-0.084	0.000	0.000	0.000	0.000
54	A	85	ALA	0	0.054	0.013	27.797	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	86	LYS	1	0.829	0.911	28.583	0.095	0.095	0.000	0.000	0.000	0.000
56	A	87	PHE	0	0.010	-0.004	23.764	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	88	SER	0	-0.025	-0.002	23.640	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	89	SER	0	-0.029	-0.018	23.391	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	90	ALA	0	0.019	0.008	19.457	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	91	ASN	0	-0.037	-0.027	15.019	0.045	0.045	0.000	0.000	0.000	0.000
61	A	92	LEU	0	0.005	0.008	17.716	-0.033	-0.033	0.000	0.000	0.000	0.000
62	A	93	ILE	0	-0.024	-0.016	13.131	0.012	0.012	0.000	0.000	0.000	0.000
63	A	94	THR	0	-0.014	-0.010	17.680	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	95	VAL	0	-0.026	-0.017	13.006	-0.010	-0.010	0.000	0.000	0.000	0.000
65	A	96	ALA	0	0.048	0.045	16.015	0.013	0.013	0.000	0.000	0.000	0.000
66	A	97	SER	0	0.011	-0.010	14.366	-0.043	-0.043	0.000	0.000	0.000	0.000
67	A	98	PRO	0	0.035	0.006	16.444	0.018	0.018	0.000	0.000	0.000	0.000
68	A	99	GLY	0	-0.027	0.000	17.555	-0.029	-0.029	0.000	0.000	0.000	0.000
69	A	100	PHE	0	0.019	0.023	15.949	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	101	LEU	0	0.005	-0.007	18.314	0.023	0.023	0.000	0.000	0.000	0.000
71	A	102	HIS	0	0.010	-0.007	20.953	0.016	0.016	0.000	0.000	0.000	0.000
72	A	103	GLU	-1	-0.784	-0.806	20.180	-0.239	-0.239	0.000	0.000	0.000	0.000
73	A	104	LYS	1	0.914	0.945	22.489	0.178	0.178	0.000	0.000	0.000	0.000
74	A	105	LYS	1	0.997	0.989	21.709	0.198	0.198	0.000	0.000	0.000	0.000
75	A	106	ASP	-1	-0.851	-0.929	19.133	-0.257	-0.257	0.000	0.000	0.000	0.000
76	A	107	GLY	0	-0.011	0.001	20.950	0.020	0.020	0.000	0.000	0.000	0.000
77	A	108	GLU	-1	-0.917	-0.969	23.882	-0.165	-0.165	0.000	0.000	0.000	0.000
78	A	109	PHE	0	-0.033	-0.018	21.297	0.007	0.007	0.000	0.000	0.000	0.000
79	A	110	GLN	0	0.083	0.023	19.705	0.017	0.017	0.000	0.000	0.000	0.000
80	A	111	LYS	1	0.867	0.952	24.213	0.143	0.143	0.000	0.000	0.000	0.000
81	A	112	TRP	0	0.043	0.015	24.916	0.004	0.004	0.000	0.000	0.000	0.000
82	A	113	TYR	0	0.036	-0.004	24.396	0.004	0.004	0.000	0.000	0.000	0.000
83	A	114	ALA	0	-0.023	-0.009	26.769	0.006	0.006	0.000	0.000	0.000	0.000
84	A	115	GLY	0	-0.019	0.002	28.713	0.009	0.009	0.000	0.000	0.000	0.000
85	A	116	LEU	0	-0.068	-0.023	27.736	0.005	0.005	0.000	0.000	0.000	0.000
86	A	117	ASN	0	0.008	-0.010	30.298	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	118	TYR	0	-0.022	-0.001	26.974	0.005	0.005	0.000	0.000	0.000	0.000
88	A	119	PRO	0	0.001	0.009	26.609	-0.011	-0.011	0.000	0.000	0.000	0.000
89	A	120	LYS	1	0.883	0.931	26.094	0.104	0.104	0.000	0.000	0.000	0.000
90	A	121	LEU	0	-0.001	0.014	22.531	-0.006	-0.006	0.000	0.000	0.000	0.000
91	A	122	PRO	0	-0.026	-0.005	18.583	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	123	VAL	0	0.023	0.029	18.986	-0.020	-0.020	0.000	0.000	0.000	0.000
93	A	124	VAL	0	-0.017	-0.028	12.361	0.025	0.025	0.000	0.000	0.000	0.000
94	A	125	THR	0	-0.024	-0.008	15.743	0.006	0.006	0.000	0.000	0.000	0.000
95	A	126	ASP	-1	-0.796	-0.913	10.544	-0.948	-0.948	0.000	0.000	0.000	0.000
96	A	127	ASN	0	0.026	0.005	13.146	0.006	0.006	0.000	0.000	0.000	0.000
97	A	128	GLY	0	0.028	0.012	13.120	-0.054	-0.054	0.000	0.000	0.000	0.000
98	A	129	GLY	0	-0.024	-0.023	13.081	-0.017	-0.017	0.000	0.000	0.000	0.000
99	A	130	THR	0	0.018	0.011	6.611	-0.054	-0.054	0.000	0.000	0.000	0.000
100	A	131	ILE	0	-0.033	-0.029	7.154	-0.212	-0.212	0.000	0.000	0.000	0.000
101	A	132	ALA	0	0.001	-0.004	8.818	-0.019	-0.019	0.000	0.000	0.000	0.000
102	A	133	GLN	0	-0.021	-0.002	10.887	0.067	0.067	0.000	0.000	0.000	0.000
103	A	134	ASN	0	-0.021	-0.011	5.396	0.443	0.443	0.000	0.000	0.000	0.000
104	A	135	LEU	0	-0.069	-0.030	8.494	0.074	0.074	0.000	0.000	0.000	0.000
105	A	136	ASN	0	-0.033	-0.012	10.728	0.180	0.180	0.000	0.000	0.000	0.000
106	A	137	ILE	0	-0.041	-0.012	13.706	0.106	0.106	0.000	0.000	0.000	0.000
107	A	138	SER	0	0.016	0.000	15.886	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	139	VAL	0	-0.053	-0.029	19.064	0.039	0.039	0.000	0.000	0.000	0.000
109	A	140	TYR	0	0.009	0.047	17.047	-0.021	-0.021	0.000	0.000	0.000	0.000
110	A	141	PRO	0	0.037	-0.016	21.870	0.020	0.020	0.000	0.000	0.000	0.000
111	A	142	SER	0	-0.032	-0.018	18.453	0.018	0.018	0.000	0.000	0.000	0.000
112	A	143	TRP	0	-0.006	-0.009	18.229	-0.017	-0.017	0.000	0.000	0.000	0.000
113	A	144	ALA	0	0.007	0.006	13.464	-0.010	-0.010	0.000	0.000	0.000	0.000
114	A	145	LEU	0	-0.028	0.006	15.488	0.024	0.024	0.000	0.000	0.000	0.000
115	A	146	ILE	0	-0.018	-0.008	9.914	-0.063	-0.063	0.000	0.000	0.000	0.000
116	A	147	GLY	0	0.100	0.048	12.688	0.080	0.080	0.000	0.000	0.000	0.000
117	A	148	LYS	1	0.898	0.942	12.623	-0.074	-0.074	0.000	0.000	0.000	0.000
118	A	149	ASP	-1	-0.899	-0.940	11.454	0.095	0.095	0.000	0.000	0.000	0.000
119	A	150	GLY	0	-0.074	-0.038	8.342	0.084	0.084	0.000	0.000	0.000	0.000
120	A	151	ASP	-1	-0.837	-0.923	7.998	-0.630	-0.630	0.000	0.000	0.000	0.000
121	A	152	VAL	0	-0.003	-0.018	8.309	-0.007	-0.007	0.000	0.000	0.000	0.000
122	A	153	GLN	0	-0.037	-0.020	10.816	0.104	0.104	0.000	0.000	0.000	0.000
123	A	154	ARG	1	0.832	0.908	14.499	0.257	0.257	0.000	0.000	0.000	0.000
124	A	155	ILE	0	0.014	0.010	12.283	-0.058	-0.058	0.000	0.000	0.000	0.000
125	A	156	VAL	0	-0.046	-0.020	16.576	0.051	0.051	0.000	0.000	0.000	0.000
126	A	157	LYS	1	0.974	0.994	20.121	0.254	0.254	0.000	0.000	0.000	0.000
127	A	158	GLY	0	0.012	-0.005	21.597	0.027	0.027	0.000	0.000	0.000	0.000
128	A	159	SER	0	-0.028	-0.045	23.619	-0.019	-0.019	0.000	0.000	0.000	0.000
129	A	160	ILE	0	-0.020	-0.003	22.806	0.006	0.006	0.000	0.000	0.000	0.000
130	A	161	ASN	0	0.035	0.016	26.567	0.000	0.000	0.000	0.000	0.000	0.000
131	A	162	GLU	-1	-0.840	-0.952	28.009	-0.121	-0.121	0.000	0.000	0.000	0.000
132	A	163	ALA	0	0.003	0.009	28.527	-0.003	-0.003	0.000	0.000	0.000	0.000
133	A	164	GLN	0	0.014	-0.006	26.390	-0.006	-0.006	0.000	0.000	0.000	0.000
134	A	165	ALA	0	0.029	0.016	24.233	-0.008	-0.008	0.000	0.000	0.000	0.000
135	A	166	LEU	0	0.001	-0.007	24.285	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	167	ALA	0	-0.059	-0.029	26.151	0.007	0.007	0.000	0.000	0.000	0.000
137	A	168	LEU	0	-0.012	-0.007	20.512	0.004	0.004	0.000	0.000	0.000	0.000
138	A	169	ILE	0	-0.032	-0.009	20.752	-0.008	-0.008	0.000	0.000	0.000	0.000
139	A	170	ARG	1	0.928	0.991	22.251	0.098	0.098	0.000	0.000	0.000	0.000
140	A	171	ASN	0	-0.007	-0.018	23.221	0.012	0.012	0.000	0.000	0.000	0.000
141	A	172	PRO	0	0.118	0.059	18.386	-0.008	-0.008	0.000	0.000	0.000	0.000
142	A	173	ASN	0	-0.024	-0.005	20.351	-0.037	-0.037	0.000	0.000	0.000	0.000
143	A	174	ALA	0	-0.046	-0.008	22.351	0.012	0.012	0.000	0.000	0.000	0.000
144	A	175	ASP	-1	-0.786	-0.886	24.867	-0.119	-0.119	0.000	0.000	0.000	0.000
145	A	176	LEU	0	-0.017	-0.021	23.251	0.004	0.004	0.000	0.000	0.000	0.000
146	A	177	GLY	0	-0.002	0.011	27.493	0.001	0.001	0.000	0.000	0.000	0.000
147	A	178	SER	0	-0.005	-0.020	29.963	0.006	0.006	0.000	0.000	0.000	0.000
148	A	179	LEU	0	-0.010	0.000	29.770	0.005	0.005	0.000	0.000	0.000	0.000
149	A	180	LYS	1	0.913	0.961	30.854	0.121	0.121	0.000	0.000	0.000	0.000
150	A	181	HIS	0	-0.002	-0.001	32.412	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	182	SER	0	-0.026	-0.002	33.906	0.003	0.003	0.000	0.000	0.000	0.000

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