FMO DATABASE

FMODB ID: 1N9NZ

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	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	151
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1425884.445776
FMO2-HF: Nuclear repulsion	1368262.645929
FMO2-HF: Total energy	-57621.799847
FMO2-MP2: Total energy	-57791.165224

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.
-2.963	1.564	2.205	-2.864	-3.866	-0.006

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 : 0.043 / q_NPA : 0.027

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	0.060	0.038	3.263	-1.569	0.808	0.077	-1.400	-1.054	0.004
4	A	35	PRO	0	0.029	0.003	5.935	0.408	0.408	0.000	0.000	0.000	0.000
5	A	36	HIS	0	0.013	0.027	2.424	-0.572	0.110	1.411	-0.616	-1.476	-0.002
6	A	37	THR	0	-0.003	-0.015	2.836	-1.016	0.371	0.712	-0.831	-1.267	-0.008
7	A	38	MET	0	0.023	0.018	3.999	0.216	0.297	0.005	-0.017	-0.069	0.000
8	A	39	SER	0	-0.061	-0.053	6.777	0.109	0.109	0.000	0.000	0.000	0.000
9	A	40	THR	0	-0.068	-0.025	6.310	0.076	0.076	0.000	0.000	0.000	0.000
10	A	41	MET	0	-0.025	0.018	7.811	-0.040	-0.040	0.000	0.000	0.000	0.000
11	A	42	LYS	1	0.893	0.949	11.543	-0.017	-0.017	0.000	0.000	0.000	0.000
12	A	43	THR	0	0.008	-0.021	15.102	-0.044	-0.044	0.000	0.000	0.000	0.000
13	A	44	ALA	0	0.036	0.009	17.529	0.024	0.024	0.000	0.000	0.000	0.000
14	A	45	ASP	-1	-0.795	-0.864	20.718	-0.051	-0.051	0.000	0.000	0.000	0.000
15	A	46	ASN	0	-0.023	-0.016	19.539	0.028	0.028	0.000	0.000	0.000	0.000
16	A	47	ARG	1	0.870	0.945	18.249	0.078	0.078	0.000	0.000	0.000	0.000
17	A	48	PRO	0	0.048	0.012	14.282	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	49	ALA	0	0.028	0.005	11.809	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	50	SER	0	0.051	0.015	10.933	-0.053	-0.053	0.000	0.000	0.000	0.000
20	A	51	VAL	0	-0.031	0.001	12.337	-0.015	-0.015	0.000	0.000	0.000	0.000
21	A	52	TYR	0	-0.023	-0.021	15.126	0.003	0.003	0.000	0.000	0.000	0.000
22	A	53	LEU	0	-0.050	-0.003	9.330	-0.032	-0.032	0.000	0.000	0.000	0.000
23	A	54	LYS	1	0.860	0.928	13.421	0.123	0.123	0.000	0.000	0.000	0.000
24	A	55	LYS	1	1.012	0.999	10.832	0.077	0.077	0.000	0.000	0.000	0.000
25	A	56	ASP	-1	-0.878	-0.959	15.699	-0.140	-0.140	0.000	0.000	0.000	0.000
26	A	57	LYS	1	0.855	0.954	16.786	0.186	0.186	0.000	0.000	0.000	0.000
27	A	58	PRO	0	-0.002	0.010	15.609	-0.041	-0.041	0.000	0.000	0.000	0.000
28	A	59	THR	0	-0.014	-0.021	12.857	0.070	0.070	0.000	0.000	0.000	0.000
29	A	60	LEU	0	0.007	0.010	14.643	-0.080	-0.080	0.000	0.000	0.000	0.000
30	A	61	ILE	0	-0.011	-0.010	11.450	0.031	0.031	0.000	0.000	0.000	0.000
31	A	62	LYS	1	0.831	0.923	15.787	0.199	0.199	0.000	0.000	0.000	0.000
32	A	63	PHE	0	0.017	-0.010	11.596	0.005	0.005	0.000	0.000	0.000	0.000
33	A	64	TRP	0	-0.020	-0.047	17.433	0.036	0.036	0.000	0.000	0.000	0.000
34	A	65	ALA	0	0.051	0.028	19.328	-0.010	-0.010	0.000	0.000	0.000	0.000
35	A	66	SER	0	-0.077	-0.084	21.928	0.011	0.011	0.000	0.000	0.000	0.000
36	A	67	TRP	0	-0.019	-0.008	22.827	0.007	0.007	0.000	0.000	0.000	0.000
37	A	68	CYS	0	-0.026	0.015	25.290	0.008	0.008	0.000	0.000	0.000	0.000
38	A	69	PRO	0	0.042	0.013	27.181	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	70	LEU	0	0.026	0.020	27.999	0.003	0.003	0.000	0.000	0.000	0.000
40	A	71	CYS	0	-0.008	-0.015	24.182	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	72	LEU	0	-0.002	-0.004	26.183	0.001	0.001	0.000	0.000	0.000	0.000
42	A	73	SER	0	-0.063	-0.036	28.401	0.006	0.006	0.000	0.000	0.000	0.000
43	A	74	GLU	-1	-0.801	-0.862	26.143	-0.198	-0.198	0.000	0.000	0.000	0.000
44	A	75	LEU	0	-0.004	0.012	24.230	-0.011	-0.011	0.000	0.000	0.000	0.000
45	A	76	GLY	0	0.084	0.036	26.769	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	77	GLN	0	-0.019	-0.008	27.004	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	78	ALA	0	0.028	0.007	23.244	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	79	GLU	-1	-0.819	-0.918	24.890	-0.108	-0.108	0.000	0.000	0.000	0.000
49	A	80	LYS	1	0.835	0.903	26.550	0.133	0.133	0.000	0.000	0.000	0.000
50	A	81	TRP	0	-0.053	-0.051	24.318	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	82	ALA	0	-0.007	-0.002	23.106	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	83	GLN	0	-0.066	-0.040	24.281	0.016	0.016	0.000	0.000	0.000	0.000
53	A	84	ASP	-1	-0.819	-0.868	27.501	-0.116	-0.116	0.000	0.000	0.000	0.000
54	A	85	ALA	0	0.067	0.020	27.648	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	86	LYS	1	0.787	0.887	28.599	0.126	0.126	0.000	0.000	0.000	0.000
56	A	87	PHE	0	0.039	0.003	23.381	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	88	SER	0	-0.033	-0.013	23.406	-0.013	-0.013	0.000	0.000	0.000	0.000
58	A	89	SER	0	0.009	0.013	23.556	0.001	0.001	0.000	0.000	0.000	0.000
59	A	90	ALA	0	0.016	0.007	19.316	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	91	ASN	0	-0.059	-0.041	14.881	0.073	0.073	0.000	0.000	0.000	0.000
61	A	92	LEU	0	-0.009	-0.013	17.741	-0.040	-0.040	0.000	0.000	0.000	0.000
62	A	93	ILE	0	-0.012	-0.003	12.887	0.033	0.033	0.000	0.000	0.000	0.000
63	A	94	THR	0	-0.024	-0.028	17.421	-0.021	-0.021	0.000	0.000	0.000	0.000
64	A	95	VAL	0	-0.013	-0.007	12.578	0.007	0.007	0.000	0.000	0.000	0.000
65	A	96	ALA	0	0.046	0.053	15.736	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	97	SER	0	0.004	-0.021	14.006	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	98	PRO	0	0.020	-0.001	16.054	0.012	0.012	0.000	0.000	0.000	0.000
68	A	99	GLY	0	-0.021	0.000	17.256	0.002	0.002	0.000	0.000	0.000	0.000
69	A	100	PHE	0	0.000	0.014	15.753	0.002	0.002	0.000	0.000	0.000	0.000
70	A	101	LEU	0	0.000	-0.010	17.984	0.006	0.006	0.000	0.000	0.000	0.000
71	A	102	HIS	0	0.016	0.002	20.630	0.007	0.007	0.000	0.000	0.000	0.000
72	A	103	GLU	-1	-0.764	-0.818	19.770	-0.140	-0.140	0.000	0.000	0.000	0.000
73	A	104	LYS	1	0.819	0.905	22.158	0.091	0.091	0.000	0.000	0.000	0.000
74	A	105	LYS	1	1.001	0.984	21.358	0.052	0.052	0.000	0.000	0.000	0.000
75	A	106	ASP	-1	-0.778	-0.881	17.924	-0.033	-0.033	0.000	0.000	0.000	0.000
76	A	107	GLY	0	-0.006	0.013	20.740	0.012	0.012	0.000	0.000	0.000	0.000
77	A	108	GLU	-1	-0.857	-0.928	23.632	-0.069	-0.069	0.000	0.000	0.000	0.000
78	A	109	PHE	0	0.002	-0.002	20.888	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	110	GLN	0	0.038	0.005	19.340	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	111	LYS	1	0.884	0.953	23.961	0.032	0.032	0.000	0.000	0.000	0.000
81	A	112	TRP	0	0.041	0.006	24.536	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	113	TYR	0	0.036	0.007	24.333	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	114	ALA	0	-0.030	-0.017	26.550	0.000	0.000	0.000	0.000	0.000	0.000
84	A	115	GLY	0	-0.013	0.008	28.637	0.005	0.005	0.000	0.000	0.000	0.000
85	A	116	LEU	0	-0.064	-0.028	27.300	-0.002	-0.002	0.000	0.000	0.000	0.000
86	A	117	ASN	0	-0.032	-0.020	29.138	0.004	0.004	0.000	0.000	0.000	0.000
87	A	118	TYR	0	-0.004	0.001	26.779	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	119	PRO	0	-0.014	-0.006	26.259	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	120	LYS	1	0.887	0.939	25.671	0.080	0.080	0.000	0.000	0.000	0.000
90	A	121	LEU	0	-0.001	0.017	22.337	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	122	PRO	0	-0.025	-0.004	18.289	0.005	0.005	0.000	0.000	0.000	0.000
92	A	123	VAL	0	-0.001	0.023	18.703	-0.026	-0.026	0.000	0.000	0.000	0.000
93	A	124	VAL	0	0.010	-0.018	12.123	0.035	0.035	0.000	0.000	0.000	0.000
94	A	125	THR	0	-0.045	-0.023	15.269	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	126	ASP	-1	-0.755	-0.883	10.540	-0.469	-0.469	0.000	0.000	0.000	0.000
96	A	127	ASN	0	-0.070	-0.047	12.864	-0.029	-0.029	0.000	0.000	0.000	0.000
97	A	128	GLY	0	0.054	0.037	12.835	0.009	0.009	0.000	0.000	0.000	0.000
98	A	129	GLY	0	-0.034	-0.028	12.923	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	130	THR	0	-0.003	-0.009	6.766	-0.031	-0.031	0.000	0.000	0.000	0.000
100	A	131	ILE	0	-0.033	-0.032	6.969	-0.263	-0.263	0.000	0.000	0.000	0.000
101	A	132	ALA	0	0.013	0.006	8.723	-0.093	-0.093	0.000	0.000	0.000	0.000
102	A	133	GLN	0	-0.037	-0.018	10.680	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	134	ASN	0	-0.025	-0.012	4.860	0.288	0.288	0.000	0.000	0.000	0.000
104	A	135	LEU	0	-0.044	-0.011	8.626	-0.135	-0.135	0.000	0.000	0.000	0.000
105	A	136	ASN	0	-0.018	-0.008	11.407	0.162	0.162	0.000	0.000	0.000	0.000
106	A	137	ILE	0	-0.025	0.000	13.718	0.097	0.097	0.000	0.000	0.000	0.000
107	A	138	SER	0	0.017	-0.007	16.017	0.036	0.036	0.000	0.000	0.000	0.000
108	A	139	VAL	0	-0.040	-0.019	19.079	0.038	0.038	0.000	0.000	0.000	0.000
109	A	140	TYR	0	-0.001	0.036	16.943	-0.023	-0.023	0.000	0.000	0.000	0.000
110	A	141	PRO	0	0.058	0.013	21.998	0.021	0.021	0.000	0.000	0.000	0.000
111	A	142	SER	0	-0.057	-0.034	18.555	0.001	0.001	0.000	0.000	0.000	0.000
112	A	143	TRP	0	-0.002	-0.006	17.888	0.006	0.006	0.000	0.000	0.000	0.000
113	A	144	ALA	0	0.009	0.012	13.568	-0.027	-0.027	0.000	0.000	0.000	0.000
114	A	145	LEU	0	-0.035	-0.006	15.479	0.058	0.058	0.000	0.000	0.000	0.000
115	A	146	ILE	0	-0.014	-0.003	9.730	-0.094	-0.094	0.000	0.000	0.000	0.000
116	A	147	GLY	0	0.078	0.039	12.522	0.143	0.143	0.000	0.000	0.000	0.000
117	A	148	LYS	1	0.809	0.896	12.455	0.197	0.197	0.000	0.000	0.000	0.000
118	A	149	ASP	-1	-0.857	-0.907	11.194	-0.262	-0.262	0.000	0.000	0.000	0.000
119	A	150	GLY	0	-0.059	-0.032	7.912	-0.035	-0.035	0.000	0.000	0.000	0.000
120	A	151	ASP	-1	-0.806	-0.901	7.744	-1.365	-1.365	0.000	0.000	0.000	0.000
121	A	152	VAL	0	0.020	-0.012	8.595	0.152	0.152	0.000	0.000	0.000	0.000
122	A	153	GLN	0	-0.053	-0.029	11.184	0.136	0.136	0.000	0.000	0.000	0.000
123	A	154	ARG	1	0.814	0.889	14.870	0.444	0.444	0.000	0.000	0.000	0.000
124	A	155	ILE	0	0.020	0.008	12.880	-0.057	-0.057	0.000	0.000	0.000	0.000
125	A	156	VAL	0	-0.035	-0.018	17.093	0.050	0.050	0.000	0.000	0.000	0.000
126	A	157	LYS	1	0.941	0.974	20.338	0.333	0.333	0.000	0.000	0.000	0.000
127	A	158	GLY	0	0.033	0.015	21.748	0.023	0.023	0.000	0.000	0.000	0.000
128	A	159	SER	0	-0.026	-0.053	23.542	-0.018	-0.018	0.000	0.000	0.000	0.000
129	A	160	ILE	0	-0.039	-0.008	22.915	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	161	ASN	0	0.032	0.010	26.764	0.002	0.002	0.000	0.000	0.000	0.000
131	A	162	GLU	-1	-0.727	-0.854	27.919	-0.150	-0.150	0.000	0.000	0.000	0.000
132	A	163	ALA	0	0.021	0.010	28.486	-0.007	-0.007	0.000	0.000	0.000	0.000
133	A	164	GLN	0	0.005	-0.006	26.806	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	165	ALA	0	0.034	0.019	24.087	-0.019	-0.019	0.000	0.000	0.000	0.000
135	A	166	LEU	0	-0.004	-0.008	24.039	-0.014	-0.014	0.000	0.000	0.000	0.000
136	A	167	ALA	0	-0.080	-0.037	26.494	0.003	0.003	0.000	0.000	0.000	0.000
137	A	168	LEU	0	0.005	0.001	20.883	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	169	ILE	0	-0.028	-0.011	20.206	-0.020	-0.020	0.000	0.000	0.000	0.000
139	A	170	ARG	1	0.922	0.981	21.907	0.190	0.190	0.000	0.000	0.000	0.000
140	A	171	ASN	0	0.028	0.003	22.817	-0.010	-0.010	0.000	0.000	0.000	0.000
141	A	172	PRO	0	0.071	0.055	18.335	0.011	0.011	0.000	0.000	0.000	0.000
142	A	173	ASN	0	-0.015	-0.009	20.327	-0.036	-0.036	0.000	0.000	0.000	0.000
143	A	174	ALA	0	-0.037	0.001	22.606	0.023	0.023	0.000	0.000	0.000	0.000
144	A	175	ASP	-1	-0.722	-0.841	25.259	-0.216	-0.216	0.000	0.000	0.000	0.000
145	A	176	LEU	0	-0.027	-0.013	23.908	0.005	0.005	0.000	0.000	0.000	0.000
146	A	177	GLY	0	-0.014	-0.006	28.377	0.009	0.009	0.000	0.000	0.000	0.000
147	A	178	SER	0	-0.020	-0.043	30.962	0.014	0.014	0.000	0.000	0.000	0.000
148	A	179	LEU	0	-0.021	-0.006	29.931	0.008	0.008	0.000	0.000	0.000	0.000
149	A	180	LYS	1	0.933	0.988	30.997	0.174	0.174	0.000	0.000	0.000	0.000
150	A	181	HIS	0	0.016	0.012	32.696	0.001	0.001	0.000	0.000	0.000	0.000
151	A	182	SER	0	-0.049	-0.030	33.840	0.005	0.005	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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