FMO DATABASE

FMODB ID: Q1MNY

Calculation Name: 2AJ2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2AJ2

Chain ID: A

ChEMBL ID:

UniProt ID: Q9KUP8

Base Structure: X-ray

Registration Date: 2023-03-13

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	187
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1974056.980276
FMO2-HF: Nuclear repulsion	1900065.496922
FMO2-HF: Total energy	-73991.483354
FMO2-MP2: Total energy	-74204.156603

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:6:SER)

Summations of interaction energy for fragment #1(A:6:SER)

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.
-2.334	0.831	0.212	-1.571	-1.805	0

Interaction energy analysis for fragmet #1(A:6:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.081 / q_NPA : -0.058

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].
3	A	8	ILE	0	-0.046	-0.021	2.808	0.122	3.287	0.212	-1.571	-1.805
4	A	9	GLU	-1	-0.900	-0.946	5.530	-1.822	-1.822	0.000	0.000	0.000
5	A	10	VAL	0	-0.078	-0.042	8.423	0.567	0.567	0.000	0.000	0.000
6	A	11	GLY	0	0.013	0.018	10.497	0.104	0.104	0.000	0.000	0.000
7	A	12	HIS	0	-0.022	-0.037	13.605	0.103	0.103	0.000	0.000	0.000
8	A	13	SER	0	-0.045	-0.019	17.168	0.050	0.050	0.000	0.000	0.000
9	A	14	MET	0	0.044	0.042	19.404	0.019	0.019	0.000	0.000	0.000
10	A	15	ASN	0	-0.029	-0.019	22.625	0.055	0.055	0.000	0.000	0.000
11	A	16	LEU	0	0.044	0.012	25.191	0.013	0.013	0.000	0.000	0.000
12	A	17	THR	0	0.003	-0.002	28.476	0.027	0.027	0.000	0.000	0.000
13	A	18	ASN	0	-0.006	0.002	30.428	0.009	0.009	0.000	0.000	0.000
14	A	19	HIS	0	-0.013	-0.011	28.356	0.007	0.007	0.000	0.000	0.000
15	A	20	PHE	0	-0.065	-0.025	32.772	0.009	0.009	0.000	0.000	0.000
16	A	21	LEU	0	0.040	0.031	31.866	-0.009	-0.009	0.000	0.000	0.000
17	A	22	VAL	0	-0.015	-0.024	34.956	0.014	0.014	0.000	0.000	0.000
18	A	23	ALA	0	0.007	0.018	36.400	-0.005	-0.005	0.000	0.000	0.000
19	A	24	MET	0	0.022	0.022	35.163	0.010	0.010	0.000	0.000	0.000
20	A	25	PRO	0	-0.029	-0.032	38.367	0.005	0.005	0.000	0.000	0.000
21	A	26	SER	0	-0.063	-0.039	37.001	0.007	0.007	0.000	0.000	0.000
22	A	27	MET	0	-0.033	0.028	37.452	0.000	0.000	0.000	0.000	0.000
23	A	28	LYS	1	0.860	0.905	35.034	0.182	0.182	0.000	0.000	0.000
24	A	29	ASP	-1	-0.829	-0.921	40.864	-0.123	-0.123	0.000	0.000	0.000
25	A	30	PRO	0	-0.046	-0.036	42.660	0.000	0.000	0.000	0.000	0.000
26	A	31	TYR	0	-0.011	-0.006	43.964	0.002	0.002	0.000	0.000	0.000
27	A	32	PHE	0	0.062	0.025	40.629	-0.001	-0.001	0.000	0.000	0.000
28	A	33	LYS	1	0.812	0.911	42.117	0.109	0.109	0.000	0.000	0.000
29	A	34	ARG	1	0.896	0.952	43.407	0.102	0.102	0.000	0.000	0.000
30	A	35	SER	0	0.022	0.011	41.007	0.000	0.000	0.000	0.000	0.000
31	A	36	VAL	0	-0.010	-0.005	39.015	-0.004	-0.004	0.000	0.000	0.000
32	A	37	ILE	0	-0.007	0.002	37.504	0.007	0.007	0.000	0.000	0.000
33	A	38	TYR	0	-0.010	-0.013	36.139	-0.008	-0.008	0.000	0.000	0.000
34	A	39	ILE	0	0.001	0.008	31.504	0.008	0.008	0.000	0.000	0.000
35	A	40	CYS	0	-0.053	-0.035	34.106	-0.001	-0.001	0.000	0.000	0.000
36	A	41	GLU	-1	-0.888	-0.964	31.439	-0.258	-0.258	0.000	0.000	0.000
37	A	42	HIS	0	-0.022	-0.017	26.227	0.007	0.007	0.000	0.000	0.000
38	A	43	ASN	0	-0.006	0.001	26.044	-0.025	-0.025	0.000	0.000	0.000
39	A	44	GLN	0	0.013	-0.006	20.203	0.017	0.017	0.000	0.000	0.000
40	A	45	ASP	-1	-0.900	-0.937	25.222	-0.303	-0.303	0.000	0.000	0.000
41	A	46	GLY	0	-0.039	-0.028	28.779	0.022	0.022	0.000	0.000	0.000
42	A	47	ALA	0	-0.020	-0.007	29.855	-0.018	-0.018	0.000	0.000	0.000
43	A	48	MET	0	0.001	0.012	32.210	0.016	0.016	0.000	0.000	0.000
44	A	49	GLY	0	0.031	0.006	35.443	-0.010	-0.010	0.000	0.000	0.000
45	A	50	LEU	0	-0.002	0.013	37.726	0.009	0.009	0.000	0.000	0.000
46	A	51	MET	0	-0.040	-0.012	40.861	-0.002	-0.002	0.000	0.000	0.000
47	A	52	ILE	0	-0.002	0.001	40.980	0.007	0.007	0.000	0.000	0.000
48	A	53	ASN	0	-0.047	-0.053	43.862	0.001	0.001	0.000	0.000	0.000
49	A	54	ALA	0	0.049	0.035	46.595	0.005	0.005	0.000	0.000	0.000
50	A	55	PRO	0	-0.040	-0.008	48.448	-0.001	-0.001	0.000	0.000	0.000
51	A	56	ILE	0	-0.018	-0.013	51.716	0.001	0.001	0.000	0.000	0.000
52	A	57	ASP	-1	-0.956	-0.981	54.268	-0.073	-0.073	0.000	0.000	0.000
53	A	58	ILE	0	0.009	0.016	56.553	0.002	0.002	0.000	0.000	0.000
54	A	59	THR	0	0.019	0.006	56.869	-0.003	-0.003	0.000	0.000	0.000
55	A	60	VAL	0	0.013	0.013	54.876	0.000	0.000	0.000	0.000	0.000
56	A	61	GLY	0	0.052	0.012	56.705	0.000	0.000	0.000	0.000	0.000
57	A	62	GLY	0	-0.019	-0.002	60.220	0.002	0.002	0.000	0.000	0.000
58	A	63	MET	0	0.005	0.000	53.591	0.001	0.001	0.000	0.000	0.000
59	A	64	LEU	0	0.031	0.014	56.431	0.000	0.000	0.000	0.000	0.000
60	A	65	LYS	1	0.800	0.892	59.241	0.068	0.068	0.000	0.000	0.000
61	A	66	GLN	0	-0.054	-0.021	59.753	0.003	0.003	0.000	0.000	0.000
62	A	67	VAL	0	-0.048	-0.028	56.157	0.001	0.001	0.000	0.000	0.000
63	A	68	ASP	-1	-0.906	-0.940	59.531	-0.066	-0.066	0.000	0.000	0.000
64	A	69	ILE	0	-0.036	-0.013	56.793	0.000	0.000	0.000	0.000	0.000
65	A	70	GLU	-1	-0.940	-0.962	60.553	-0.065	-0.065	0.000	0.000	0.000
66	A	71	PRO	0	-0.069	-0.026	60.716	-0.003	-0.003	0.000	0.000	0.000
67	A	72	ALA	0	0.008	-0.008	59.680	0.002	0.002	0.000	0.000	0.000
68	A	73	TYR	0	-0.022	-0.015	58.547	0.003	0.003	0.000	0.000	0.000
69	A	74	PRO	0	0.012	-0.009	63.176	0.000	0.000	0.000	0.000	0.000
70	A	75	GLN	0	0.035	0.021	62.196	-0.003	-0.003	0.000	0.000	0.000
71	A	76	SER	0	-0.020	-0.049	62.115	0.001	0.001	0.000	0.000	0.000
72	A	77	HIS	1	0.792	0.891	56.808	0.083	0.083	0.000	0.000	0.000
73	A	78	GLN	0	0.018	-0.007	60.295	-0.002	-0.002	0.000	0.000	0.000
74	A	79	GLU	-1	-0.813	-0.900	61.091	-0.066	-0.066	0.000	0.000	0.000
75	A	80	ASN	0	-0.065	-0.054	55.895	-0.001	-0.001	0.000	0.000	0.000
76	A	81	LEU	0	0.040	0.024	57.321	-0.002	-0.002	0.000	0.000	0.000
77	A	82	LYS	1	0.801	0.872	59.559	0.067	0.067	0.000	0.000	0.000
78	A	83	LYS	1	0.909	0.979	54.011	0.088	0.088	0.000	0.000	0.000
79	A	84	PRO	0	-0.006	0.005	53.564	0.001	0.001	0.000	0.000	0.000
80	A	85	VAL	0	-0.005	0.010	51.455	-0.003	-0.003	0.000	0.000	0.000
81	A	86	PHE	0	-0.024	-0.033	48.046	0.003	0.003	0.000	0.000	0.000
82	A	87	ASN	0	-0.039	-0.025	47.007	-0.004	-0.004	0.000	0.000	0.000
83	A	88	GLY	0	0.024	0.000	44.470	-0.002	-0.002	0.000	0.000	0.000
84	A	89	GLY	0	0.030	0.004	42.704	-0.010	-0.010	0.000	0.000	0.000
85	A	90	PRO	0	0.000	0.012	42.321	0.003	0.003	0.000	0.000	0.000
86	A	91	VAL	0	-0.044	-0.010	39.885	0.004	0.004	0.000	0.000	0.000
87	A	92	SER	0	0.022	-0.005	43.327	-0.003	-0.003	0.000	0.000	0.000
88	A	93	GLU	-1	-0.820	-0.900	45.973	-0.113	-0.113	0.000	0.000	0.000
89	A	94	ASP	-1	-0.932	-0.960	48.611	-0.112	-0.112	0.000	0.000	0.000
90	A	95	ARG	1	0.856	0.919	44.700	0.132	0.132	0.000	0.000	0.000
91	A	96	GLY	0	0.002	0.008	47.908	-0.001	-0.001	0.000	0.000	0.000
92	A	97	PHE	0	-0.020	-0.026	42.122	-0.006	-0.006	0.000	0.000	0.000
93	A	98	ILE	0	-0.007	-0.002	46.153	0.003	0.003	0.000	0.000	0.000
94	A	99	LEU	0	0.022	0.030	40.751	-0.005	-0.005	0.000	0.000	0.000
95	A	100	HIS	0	-0.019	-0.037	43.901	0.005	0.005	0.000	0.000	0.000
96	A	101	ARG	1	0.804	0.867	43.620	0.119	0.119	0.000	0.000	0.000
97	A	102	PRO	0	-0.068	-0.022	41.951	0.005	0.005	0.000	0.000	0.000
98	A	103	ARG	1	0.819	0.910	45.035	0.098	0.098	0.000	0.000	0.000
99	A	104	ASP	-1	-0.831	-0.888	48.648	-0.099	-0.099	0.000	0.000	0.000
100	A	105	HIS	0	-0.077	-0.032	45.154	-0.002	-0.002	0.000	0.000	0.000
101	A	106	TYR	0	-0.009	-0.048	46.701	0.003	0.003	0.000	0.000	0.000
102	A	107	GLU	-1	-0.863	-0.941	46.200	-0.110	-0.110	0.000	0.000	0.000
103	A	108	SER	0	-0.024	-0.021	43.471	-0.005	-0.005	0.000	0.000	0.000
104	A	109	SER	0	-0.031	-0.024	43.162	-0.001	-0.001	0.000	0.000	0.000
105	A	110	MET	0	0.007	0.011	35.603	-0.004	-0.004	0.000	0.000	0.000
106	A	111	LYS	1	0.826	0.896	37.864	0.172	0.172	0.000	0.000	0.000
107	A	112	MET	0	-0.014	0.010	33.761	-0.013	-0.013	0.000	0.000	0.000
108	A	113	THR	0	0.038	0.013	34.515	-0.007	-0.007	0.000	0.000	0.000
109	A	114	ASP	-1	-0.918	-0.955	36.736	-0.166	-0.166	0.000	0.000	0.000
110	A	115	ASP	-1	-0.796	-0.882	39.484	-0.127	-0.127	0.000	0.000	0.000
111	A	116	ILE	0	-0.009	-0.010	37.856	0.006	0.006	0.000	0.000	0.000
112	A	117	ALA	0	-0.007	0.010	39.343	-0.009	-0.009	0.000	0.000	0.000
113	A	118	VAL	0	0.037	0.018	39.894	0.007	0.007	0.000	0.000	0.000
114	A	119	THR	0	0.011	0.002	42.206	-0.004	-0.004	0.000	0.000	0.000
115	A	120	THR	0	-0.041	-0.006	43.269	0.004	0.004	0.000	0.000	0.000
116	A	121	SER	0	-0.003	-0.003	46.161	0.000	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.861	0.903	48.613	0.099	0.099	0.000	0.000	0.000
118	A	123	ASP	-1	-0.771	-0.850	50.333	-0.109	-0.109	0.000	0.000	0.000
119	A	124	ILE	0	0.035	0.036	48.494	0.004	0.004	0.000	0.000	0.000
120	A	125	LEU	0	0.010	-0.003	52.132	0.002	0.002	0.000	0.000	0.000
121	A	126	THR	0	-0.048	-0.032	54.644	0.003	0.003	0.000	0.000	0.000
122	A	127	VAL	0	0.032	0.024	53.864	0.004	0.004	0.000	0.000	0.000
123	A	128	LEU	0	0.032	0.035	52.342	0.001	0.001	0.000	0.000	0.000
124	A	129	GLY	0	0.008	0.002	56.341	0.003	0.003	0.000	0.000	0.000
125	A	130	THR	0	-0.089	-0.058	58.367	0.004	0.004	0.000	0.000	0.000
126	A	131	GLU	-1	-0.830	-0.878	58.150	-0.076	-0.076	0.000	0.000	0.000
127	A	132	ALA	0	-0.014	-0.007	56.347	-0.001	-0.001	0.000	0.000	0.000
128	A	133	GLU	-1	-0.767	-0.814	54.021	-0.091	-0.091	0.000	0.000	0.000
129	A	134	PRO	0	0.013	-0.001	49.090	0.001	0.001	0.000	0.000	0.000
130	A	135	GLU	-1	-0.857	-0.937	50.695	-0.094	-0.094	0.000	0.000	0.000
131	A	136	GLY	0	-0.023	-0.008	48.625	0.002	0.002	0.000	0.000	0.000
132	A	137	TYR	0	-0.092	-0.060	47.515	-0.005	-0.005	0.000	0.000	0.000
133	A	138	ILE	0	-0.042	-0.006	44.746	0.004	0.004	0.000	0.000	0.000
134	A	139	VAL	0	0.027	0.019	47.381	-0.005	-0.005	0.000	0.000	0.000
135	A	140	ALA	0	-0.006	-0.008	46.165	0.003	0.003	0.000	0.000	0.000
136	A	141	LEU	0	0.004	0.002	48.296	0.001	0.001	0.000	0.000	0.000
137	A	142	GLY	0	0.058	0.038	45.720	0.000	0.000	0.000	0.000	0.000
138	A	143	TYR	0	-0.036	-0.033	38.394	-0.005	-0.005	0.000	0.000	0.000
139	A	144	SER	0	-0.013	-0.016	38.932	0.005	0.005	0.000	0.000	0.000
140	A	145	GLY	0	0.005	-0.004	36.359	-0.007	-0.007	0.000	0.000	0.000
141	A	146	TRP	0	-0.064	-0.024	32.578	0.007	0.007	0.000	0.000	0.000
142	A	147	SER	0	0.030	0.003	31.963	-0.003	-0.003	0.000	0.000	0.000
143	A	148	ALA	0	0.061	0.036	26.927	-0.007	-0.007	0.000	0.000	0.000
144	A	149	GLY	0	0.011	0.019	26.002	0.006	0.006	0.000	0.000	0.000
145	A	150	GLN	0	-0.040	-0.037	26.628	-0.007	-0.007	0.000	0.000	0.000
146	A	151	LEU	0	0.011	0.020	29.630	0.016	0.016	0.000	0.000	0.000
147	A	152	GLU	-1	-0.825	-0.928	24.076	-0.379	-0.379	0.000	0.000	0.000
148	A	153	VAL	0	-0.015	-0.003	26.267	-0.002	-0.002	0.000	0.000	0.000
149	A	154	GLU	-1	-0.758	-0.834	27.745	-0.182	-0.182	0.000	0.000	0.000
150	A	155	LEU	0	-0.038	-0.015	26.133	0.014	0.014	0.000	0.000	0.000
151	A	156	THR	0	-0.110	-0.058	24.469	-0.003	-0.003	0.000	0.000	0.000
152	A	157	GLU	-1	-0.849	-0.903	27.410	-0.166	-0.166	0.000	0.000	0.000
153	A	158	ASN	0	-0.025	-0.017	31.172	-0.008	-0.008	0.000	0.000	0.000
154	A	159	SER	0	-0.027	-0.030	33.588	0.017	0.017	0.000	0.000	0.000
155	A	160	TRP	0	-0.011	-0.032	32.451	0.014	0.014	0.000	0.000	0.000
156	A	161	LEU	0	-0.004	0.005	30.788	-0.004	-0.004	0.000	0.000	0.000
157	A	162	THR	0	0.022	0.007	29.219	0.002	0.002	0.000	0.000	0.000
158	A	163	ILE	0	-0.051	-0.023	30.973	-0.002	-0.002	0.000	0.000	0.000
159	A	164	GLU	-1	-0.851	-0.904	30.692	-0.255	-0.255	0.000	0.000	0.000
160	A	165	ALA	0	-0.039	-0.019	32.482	0.015	0.015	0.000	0.000	0.000
161	A	166	ASP	-1	-0.829	-0.922	36.106	-0.150	-0.150	0.000	0.000	0.000
162	A	167	PRO	0	0.063	0.024	39.065	0.002	0.002	0.000	0.000	0.000
163	A	168	GLU	-1	-0.792	-0.883	41.996	-0.123	-0.123	0.000	0.000	0.000
164	A	169	LEU	0	-0.067	-0.025	40.990	0.008	0.008	0.000	0.000	0.000
165	A	170	ILE	0	0.005	0.005	39.685	0.003	0.003	0.000	0.000	0.000
166	A	171	PHE	0	-0.024	-0.004	43.091	0.006	0.006	0.000	0.000	0.000
167	A	172	ASN	0	-0.029	-0.016	47.076	0.001	0.001	0.000	0.000	0.000
168	A	173	THR	0	-0.031	-0.005	45.979	0.005	0.005	0.000	0.000	0.000
169	A	174	PRO	0	-0.001	-0.007	48.665	-0.002	-0.002	0.000	0.000	0.000
170	A	175	VAL	0	0.051	0.015	49.110	-0.003	-0.003	0.000	0.000	0.000
171	A	176	HIS	0	-0.005	-0.011	48.596	-0.006	-0.006	0.000	0.000	0.000
172	A	177	GLU	-1	-0.814	-0.897	47.800	-0.098	-0.098	0.000	0.000	0.000
173	A	178	LYS	1	0.762	0.901	44.537	0.117	0.117	0.000	0.000	0.000
174	A	179	TRP	0	0.022	-0.003	41.092	0.002	0.002	0.000	0.000	0.000
175	A	180	GLN	0	-0.011	-0.024	42.463	-0.005	-0.005	0.000	0.000	0.000
176	A	181	LYS	1	0.866	0.913	43.482	0.105	0.105	0.000	0.000	0.000
177	A	182	ALA	0	0.026	0.024	39.043	-0.004	-0.004	0.000	0.000	0.000
178	A	183	ILE	0	0.013	-0.003	38.579	-0.006	-0.006	0.000	0.000	0.000
179	A	184	GLN	0	-0.001	0.005	39.029	0.002	0.002	0.000	0.000	0.000
180	A	185	LYS	1	0.863	0.941	36.783	0.163	0.163	0.000	0.000	0.000
181	A	186	LEU	0	-0.018	-0.003	33.212	-0.006	-0.006	0.000	0.000	0.000
182	A	187	GLY	0	-0.019	0.003	35.415	-0.002	-0.002	0.000	0.000	0.000
183	A	188	ILE	0	-0.029	-0.004	36.332	0.007	0.007	0.000	0.000	0.000
184	A	189	SER	0	-0.026	-0.038	39.285	0.005	0.005	0.000	0.000	0.000
185	A	190	PRO	0	-0.017	-0.014	42.294	-0.001	-0.001	0.000	0.000	0.000
186	A	191	ALA	0	0.015	0.010	43.632	0.003	0.003	0.000	0.000	0.000
187	A	192	GLN	0	-0.030	0.007	44.791	0.005	0.005	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:SER)