FMO DATABASE

FMODB ID: 169NZ

Calculation Name: 2BA2-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2BA2

Chain ID: A

ChEMBL ID:

UniProt ID: P75103

Base Structure: X-ray

Registration Date: 2025-07-08

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	158
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-363838.061768
FMO2-HF: Nuclear repulsion	331449.668412
FMO2-HF: Total energy	-32388.393356
FMO2-MP2: Total energy	-32483.668411

3D Structure Molmil

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:GLY)

Summations of interaction energy for fragment #1(A:5: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.
-18.407	-21.814	15.728	-6.373	-5.948	0.028

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.049 / q_NPA : 0.013

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	THR	0	0.005	0.079	3.315	1.238	1.668	0.009	-0.162	-0.277	0.000
4	A	7	ARG	0	0.096	-0.056	3.578	-1.143	0.798	-0.004	-0.899	-1.038	-0.001
5	A	7	ARG	1	0.837	1.020	1.955	-19.640	-26.043	13.745	-4.041	-3.301	0.037
6	A	8	TYR	0	0.058	-0.090	4.418	0.825	1.008	-0.001	-0.051	-0.131	0.000
7	A	8	TYR	0	-0.051	0.104	2.452	0.085	0.527	1.979	-1.220	-1.201	-0.008
8	A	9	VAL	0	0.091	-0.090	5.590	-0.572	-0.572	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.073	0.117	9.777	0.034	0.034	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.059	-0.084	8.523	0.037	0.037	0.000	0.000	0.000	0.000
11	A	10	THR	0	-0.064	0.045	6.971	0.104	0.104	0.000	0.000	0.000	0.000
12	A	11	HIS	0	0.091	-0.070	9.031	0.119	0.119	0.000	0.000	0.000	0.000
13	A	11	HIS	0	-0.046	0.100	11.209	-0.034	-0.034	0.000	0.000	0.000	0.000
14	A	12	LYS	0	0.167	-0.057	12.472	0.075	0.075	0.000	0.000	0.000	0.000
15	A	12	LYS	1	0.751	1.012	13.373	0.428	0.428	0.000	0.000	0.000	0.000
16	A	13	GLN	0	0.115	-0.094	12.165	0.119	0.119	0.000	0.000	0.000	0.000
17	A	13	GLN	0	-0.022	0.129	9.405	-0.182	-0.182	0.000	0.000	0.000	0.000
18	A	14	LEU	0	0.132	-0.056	13.243	0.060	0.060	0.000	0.000	0.000	0.000
19	A	14	LEU	0	-0.074	0.112	13.267	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	15	ASP	0	0.076	-0.111	14.717	0.056	0.056	0.000	0.000	0.000	0.000
21	A	15	ASP	-1	-0.857	-0.829	17.098	-0.410	-0.410	0.000	0.000	0.000	0.000
22	A	16	GLU	0	0.074	-0.110	16.849	0.056	0.056	0.000	0.000	0.000	0.000
23	A	16	GLU	-1	-0.989	-0.810	16.380	-0.443	-0.443	0.000	0.000	0.000	0.000
24	A	17	LYS	0	0.025	-0.105	17.323	0.032	0.032	0.000	0.000	0.000	0.000
25	A	17	LYS	1	0.745	0.966	14.512	0.467	0.467	0.000	0.000	0.000	0.000
26	A	18	LEU	0	0.098	-0.092	18.742	0.034	0.034	0.000	0.000	0.000	0.000
27	A	18	LEU	0	-0.089	0.105	18.602	0.000	0.000	0.000	0.000	0.000	0.000
28	A	19	LYS	0	0.086	-0.074	20.870	0.024	0.024	0.000	0.000	0.000	0.000
29	A	19	LYS	1	0.838	1.030	21.137	0.247	0.247	0.000	0.000	0.000	0.000
30	A	20	ASN	0	0.034	-0.031	22.810	0.012	0.012	0.000	0.000	0.000	0.000
31	A	20	ASN	0	-0.120	0.041	21.153	0.009	0.009	0.000	0.000	0.000	0.000
32	A	21	PHE	0	0.092	-0.104	23.677	0.015	0.015	0.000	0.000	0.000	0.000
33	A	21	PHE	0	-0.139	0.071	21.002	0.003	0.003	0.000	0.000	0.000	0.000
34	A	22	VAL	0	0.132	-0.079	24.897	-0.010	-0.010	0.000	0.000	0.000	0.000
35	A	22	VAL	0	-0.084	0.106	29.069	0.002	0.002	0.000	0.000	0.000	0.000
36	A	23	THR	0	0.030	-0.101	27.576	0.002	0.002	0.000	0.000	0.000	0.000
37	A	23	THR	0	-0.089	0.021	26.760	0.003	0.003	0.000	0.000	0.000	0.000
38	A	24	LYS	0	0.079	-0.080	28.513	0.007	0.007	0.000	0.000	0.000	0.000
39	A	24	LYS	1	0.894	1.054	27.386	0.078	0.078	0.000	0.000	0.000	0.000
40	A	25	THR	0	-0.004	-0.062	30.781	0.009	0.009	0.000	0.000	0.000	0.000
41	A	25	THR	0	0.012	0.061	31.726	0.000	0.000	0.000	0.000	0.000	0.000
42	A	26	GLU	0	0.148	-0.083	32.105	0.007	0.007	0.000	0.000	0.000	0.000
43	A	26	GLU	-1	-0.823	-0.739	29.886	-0.116	-0.116	0.000	0.000	0.000	0.000
44	A	27	PHE	0	0.173	-0.019	32.732	0.005	0.005	0.000	0.000	0.000	0.000
45	A	27	PHE	0	-0.111	0.064	32.461	0.000	0.000	0.000	0.000	0.000	0.000
46	A	28	LYS	0	-0.076	-0.164	34.321	0.005	0.005	0.000	0.000	0.000	0.000
47	A	28	LYS	1	0.761	1.002	34.234	0.062	0.062	0.000	0.000	0.000	0.000
48	A	29	GLU	0	0.199	-0.046	36.704	0.006	0.006	0.000	0.000	0.000	0.000
49	A	29	GLU	-1	-1.010	-0.847	37.251	-0.076	-0.076	0.000	0.000	0.000	0.000
50	A	30	PHE	0	0.141	-0.061	37.455	0.004	0.004	0.000	0.000	0.000	0.000
51	A	30	PHE	0	-0.120	0.072	37.103	0.000	0.000	0.000	0.000	0.000	0.000
52	A	31	GLN	0	0.065	-0.080	38.476	0.003	0.003	0.000	0.000	0.000	0.000
53	A	31	GLN	0	-0.068	0.073	37.056	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	32	THR	0	-0.028	-0.082	40.238	0.004	0.004	0.000	0.000	0.000	0.000
55	A	32	THR	0	-0.048	0.067	41.438	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	33	VAL	0	0.188	-0.064	42.366	0.004	0.004	0.000	0.000	0.000	0.000
57	A	33	VAL	0	-0.074	0.114	42.469	0.000	0.000	0.000	0.000	0.000	0.000
58	A	34	VAL	0	0.111	-0.068	42.892	0.002	0.002	0.000	0.000	0.000	0.000
59	A	34	VAL	0	-0.120	0.086	41.561	0.000	0.000	0.000	0.000	0.000	0.000
60	A	35	MET	0	0.088	-0.109	44.343	0.002	0.002	0.000	0.000	0.000	0.000
61	A	35	MET	0	-0.101	0.088	43.752	0.000	0.000	0.000	0.000	0.000	0.000
62	A	36	GLU	0	0.082	-0.116	46.238	0.003	0.003	0.000	0.000	0.000	0.000
63	A	36	GLU	-1	-0.978	-0.839	45.911	-0.044	-0.044	0.000	0.000	0.000	0.000
64	A	37	SER	0	0.017	-0.110	47.494	0.002	0.002	0.000	0.000	0.000	0.000
65	A	37	SER	0	-0.066	0.055	46.956	0.000	0.000	0.000	0.000	0.000	0.000
66	A	38	PHE	0	0.060	-0.071	48.458	0.001	0.001	0.000	0.000	0.000	0.000
67	A	38	PHE	0	-0.115	0.060	45.587	0.000	0.000	0.000	0.000	0.000	0.000
68	A	39	ALA	0	0.125	-0.092	50.210	0.002	0.002	0.000	0.000	0.000	0.000
69	A	39	ALA	0	-0.101	0.104	51.305	0.000	0.000	0.000	0.000	0.000	0.000
70	A	40	VAL	0	0.077	-0.095	52.199	0.002	0.002	0.000	0.000	0.000	0.000
71	A	40	VAL	0	-0.100	0.090	52.536	0.000	0.000	0.000	0.000	0.000	0.000
72	A	41	GLN	0	0.089	-0.094	52.936	0.001	0.001	0.000	0.000	0.000	0.000
73	A	41	GLN	0	-0.092	0.097	52.049	0.000	0.000	0.000	0.000	0.000	0.000
74	A	42	ASN	0	0.094	-0.068	54.271	0.001	0.001	0.000	0.000	0.000	0.000
75	A	42	ASN	0	-0.123	0.046	52.938	0.000	0.000	0.000	0.000	0.000	0.000
76	A	43	GLN	0	0.159	-0.063	56.137	0.002	0.002	0.000	0.000	0.000	0.000
77	A	43	GLN	0	-0.115	0.090	57.271	0.000	0.000	0.000	0.000	0.000	0.000
78	A	44	ASN	0	0.070	-0.075	57.687	0.001	0.001	0.000	0.000	0.000	0.000
79	A	44	ASN	0	-0.158	0.032	56.170	0.000	0.000	0.000	0.000	0.000	0.000
80	A	45	ILE	0	0.130	-0.063	58.409	0.001	0.001	0.000	0.000	0.000	0.000
81	A	45	ILE	0	-0.116	0.068	55.905	0.000	0.000	0.000	0.000	0.000	0.000
82	A	46	ASP	0	0.050	-0.121	59.922	0.001	0.001	0.000	0.000	0.000	0.000
83	A	46	ASP	-1	-0.984	-0.840	60.529	-0.018	-0.018	0.000	0.000	0.000	0.000
84	A	47	ALA	0	0.161	-0.074	62.028	0.001	0.001	0.000	0.000	0.000	0.000
85	A	47	ALA	0	-0.072	0.105	62.987	0.000	0.000	0.000	0.000	0.000	0.000
86	A	48	GLN	0	0.020	-0.124	63.161	0.001	0.001	0.000	0.000	0.000	0.000
87	A	48	GLN	0	-0.103	0.094	61.584	0.000	0.000	0.000	0.000	0.000	0.000
88	A	49	GLY	0	-0.004	-0.108	64.070	0.001	0.001	0.000	0.000	0.000	0.000
89	A	50	GLU	0	0.117	-0.026	65.698	0.001	0.001	0.000	0.000	0.000	0.000
90	A	50	GLU	-1	-1.024	-0.826	67.206	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	51	GLN	0	0.145	-0.083	67.947	0.001	0.001	0.000	0.000	0.000	0.000
92	A	51	GLN	0	-0.100	0.095	67.448	0.000	0.000	0.000	0.000	0.000	0.000
93	A	52	ILE	0	0.060	-0.103	68.540	0.001	0.001	0.000	0.000	0.000	0.000
94	A	52	ILE	0	-0.110	0.084	66.125	0.000	0.000	0.000	0.000	0.000	0.000
95	A	53	LYS	0	0.023	-0.134	69.885	0.001	0.001	0.000	0.000	0.000	0.000
96	A	53	LYS	1	0.744	1.008	70.022	0.012	0.012	0.000	0.000	0.000	0.000
97	A	54	GLU	0	0.091	-0.123	71.678	0.001	0.001	0.000	0.000	0.000	0.000
98	A	54	GLU	-1	-0.935	-0.826	72.604	-0.015	-0.015	0.000	0.000	0.000	0.000
99	A	55	LEU	0	0.048	-0.106	73.369	0.001	0.001	0.000	0.000	0.000	0.000
100	A	55	LEU	0	-0.068	0.120	71.487	0.000	0.000	0.000	0.000	0.000	0.000
101	A	56	GLN	0	0.095	-0.097	74.141	0.000	0.000	0.000	0.000	0.000	0.000
102	A	56	GLN	0	-0.045	0.105	70.806	0.000	0.000	0.000	0.000	0.000	0.000
103	A	57	VAL	0	0.002	-0.119	75.723	0.001	0.001	0.000	0.000	0.000	0.000
104	A	57	VAL	0	-0.097	0.105	76.252	0.000	0.000	0.000	0.000	0.000	0.000
105	A	58	GLU	0	0.124	-0.101	78.172	0.001	0.001	0.000	0.000	0.000	0.000
106	A	58	GLU	-1	-0.927	-0.792	78.479	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	59	GLN	0	0.124	-0.097	78.638	0.000	0.000	0.000	0.000	0.000	0.000
108	A	59	GLN	0	-0.110	0.100	76.624	0.000	0.000	0.000	0.000	0.000	0.000
109	A	60	LYS	0	0.081	-0.074	79.963	0.000	0.000	0.000	0.000	0.000	0.000
110	A	60	LYS	1	0.849	1.048	80.093	0.009	0.009	0.000	0.000	0.000	0.000
111	A	61	ALA	0	0.034	-0.143	81.742	0.001	0.001	0.000	0.000	0.000	0.000
112	A	61	ALA	0	-0.040	0.141	83.230	0.000	0.000	0.000	0.000	0.000	0.000
113	A	62	GLN	0	0.072	-0.109	83.465	0.000	0.000	0.000	0.000	0.000	0.000
114	A	62	GLN	0	-0.094	0.094	81.628	0.000	0.000	0.000	0.000	0.000	0.000
115	A	63	GLY	0	0.016	-0.100	83.906	0.000	0.000	0.000	0.000	0.000	0.000
116	A	64	LYS	0	0.104	0.017	85.341	0.000	0.000	0.000	0.000	0.000	0.000
117	A	64	LYS	1	0.860	1.050	86.087	0.008	0.008	0.000	0.000	0.000	0.000
118	A	65	THR	0	0.039	-0.074	87.785	0.000	0.000	0.000	0.000	0.000	0.000
119	A	65	THR	0	-0.056	0.056	87.798	0.000	0.000	0.000	0.000	0.000	0.000
120	A	66	LEU	0	0.064	-0.106	88.510	0.000	0.000	0.000	0.000	0.000	0.000
121	A	66	LEU	0	-0.081	0.107	86.173	0.000	0.000	0.000	0.000	0.000	0.000
122	A	67	GLN	0	0.096	-0.074	89.581	0.000	0.000	0.000	0.000	0.000	0.000
123	A	67	GLN	0	-0.087	0.067	88.120	0.000	0.000	0.000	0.000	0.000	0.000
124	A	68	LEU	0	0.072	-0.096	91.319	0.000	0.000	0.000	0.000	0.000	0.000
125	A	68	LEU	0	-0.104	0.092	91.959	0.000	0.000	0.000	0.000	0.000	0.000
126	A	69	ILE	0	0.111	-0.067	93.205	0.000	0.000	0.000	0.000	0.000	0.000
127	A	69	ILE	0	-0.084	0.088	91.718	0.000	0.000	0.000	0.000	0.000	0.000
128	A	70	LEU	0	0.053	-0.109	93.829	0.000	0.000	0.000	0.000	0.000	0.000
129	A	70	LEU	0	-0.105	0.092	91.670	0.000	0.000	0.000	0.000	0.000	0.000
130	A	71	GLU	0	0.121	-0.099	95.300	0.000	0.000	0.000	0.000	0.000	0.000
131	A	71	GLU	-1	-1.015	-0.866	95.400	-0.006	-0.006	0.000	0.000	0.000	0.000
132	A	72	ALA	0	0.114	-0.083	97.565	0.000	0.000	0.000	0.000	0.000	0.000
133	A	72	ALA	0	-0.104	0.092	98.142	0.000	0.000	0.000	0.000	0.000	0.000
134	A	73	LEU	0	0.034	-0.127	98.440	0.000	0.000	0.000	0.000	0.000	0.000
135	A	73	LEU	0	-0.078	0.109	96.317	0.000	0.000	0.000	0.000	0.000	0.000
136	A	74	GLN	0	0.098	-0.090	99.478	0.000	0.000	0.000	0.000	0.000	0.000
137	A	74	GLN	0	-0.042	0.134	99.440	0.000	0.000	0.000	0.000	0.000	0.000
138	A	75	GLY	0	-0.026	-0.123	101.194	0.000	0.000	0.000	0.000	0.000	0.000
139	A	76	ILE	0	0.055	0.004	103.061	0.000	0.000	0.000	0.000	0.000	0.000
140	A	76	ILE	0	-0.087	0.082	101.466	0.000	0.000	0.000	0.000	0.000	0.000
141	A	77	ASN	0	0.125	-0.069	103.708	0.000	0.000	0.000	0.000	0.000	0.000
142	A	77	ASN	0	-0.130	0.062	102.299	0.000	0.000	0.000	0.000	0.000	0.000
143	A	78	LYS	0	0.193	-0.025	105.262	0.000	0.000	0.000	0.000	0.000	0.000
144	A	78	LYS	1	0.781	1.014	103.581	0.005	0.005	0.000	0.000	0.000	0.000
145	A	79	ARG	0	0.075	-0.081	107.496	0.000	0.000	0.000	0.000	0.000	0.000
146	A	79	ARG	1	0.809	1.026	106.833	0.006	0.006	0.000	0.000	0.000	0.000
147	A	80	LEU	0	0.042	-0.099	108.451	0.000	0.000	0.000	0.000	0.000	0.000
148	A	80	LEU	0	-0.070	0.097	106.376	0.000	0.000	0.000	0.000	0.000	0.000
149	A	81	ASP	0	0.132	-0.084	109.219	0.000	0.000	0.000	0.000	0.000	0.000
150	A	81	ASP	-1	-0.981	-0.873	107.794	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	82	ASN	0	0.046	-0.069	110.899	0.000	0.000	0.000	0.000	0.000	0.000
152	A	82	ASN	0	-0.159	0.039	112.507	0.000	0.000	0.000	0.000	0.000	0.000
153	A	83	LEU	0	0.055	-0.099	113.143	0.000	0.000	0.000	0.000	0.000	0.000
154	A	83	LEU	0	-0.108	0.068	112.256	0.000	0.000	0.000	0.000	0.000	0.000
155	A	84	GLU	0	0.042	-0.124	113.714	0.000	0.000	0.000	0.000	0.000	0.000
156	A	84	GLU	-1	-1.007	-0.844	111.120	-0.006	-0.006	0.000	0.000	0.000	0.000
157	A	85	SER	0	-0.120	-0.175	114.719	0.000	0.000	0.000	0.000	0.000	0.000
158	A	85	SER	0	0.004	0.034	117.867	0.000	0.000	0.000	0.000	0.000	0.000

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