FMO DATABASE

FMODB ID: G5RM1

Calculation Name: 2F2F-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F2F

Chain ID: A

ChEMBL ID:

UniProt ID: O87120

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	153
LigandResidueName
LigandFragmentNumber	0
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1497170.788468
FMO2-HF: Nuclear repulsion	1436783.217015
FMO2-HF: Total energy	-60387.571453
FMO2-MP2: Total energy	-60562.876468

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:71:PRO)

Summations of interaction energy for fragment #1(A:71:PRO)

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.
-6.364	-0.994	4.933	-4.225	-6.079	-0.008

Interaction energy analysis for fragmet #1(A:71:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.020 / q_NPA : -0.015

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	73	GLU	-1	-0.886	-0.929	2.611	-4.159	0.215	0.188	-2.255	-2.307	-0.003
4	A	74	PRO	0	0.024	-0.003	2.147	-0.861	-1.066	4.637	-1.543	-2.890	-0.002
5	A	75	SER	0	0.025	0.018	4.815	0.083	0.270	-0.001	-0.048	-0.137	0.000
6	A	76	ASN	0	-0.106	-0.046	6.960	0.313	0.313	0.000	0.000	0.000	0.000
7	A	77	PHE	0	-0.032	-0.021	6.966	0.214	0.214	0.000	0.000	0.000	0.000
8	A	78	MET	0	-0.022	0.002	10.337	-0.096	-0.096	0.000	0.000	0.000	0.000
9	A	79	THR	0	-0.022	-0.038	13.150	0.061	0.061	0.000	0.000	0.000	0.000
10	A	80	LEU	0	0.008	0.012	16.268	0.005	0.005	0.000	0.000	0.000	0.000
11	A	81	MET	0	-0.034	-0.012	18.329	0.021	0.021	0.000	0.000	0.000	0.000
12	A	82	GLY	0	0.061	0.036	21.292	0.007	0.007	0.000	0.000	0.000	0.000
13	A	83	GLN	0	0.035	0.022	24.518	-0.014	-0.014	0.000	0.000	0.000	0.000
14	A	84	ASN	0	-0.031	0.003	26.365	-0.008	-0.008	0.000	0.000	0.000	0.000
15	A	85	GLY	0	-0.001	-0.012	22.582	0.002	0.002	0.000	0.000	0.000	0.000
16	A	86	ALA	0	-0.083	-0.049	21.850	-0.018	-0.018	0.000	0.000	0.000	0.000
17	A	87	LEU	0	0.027	0.004	17.035	-0.002	-0.002	0.000	0.000	0.000	0.000
18	A	88	LEU	0	0.008	0.015	20.873	0.017	0.017	0.000	0.000	0.000	0.000
19	A	89	THR	0	-0.010	-0.010	19.771	-0.032	-0.032	0.000	0.000	0.000	0.000
20	A	90	VAL	0	0.022	0.022	20.208	0.018	0.018	0.000	0.000	0.000	0.000
21	A	91	TRP	0	-0.009	0.003	21.677	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	92	ALA	0	0.007	0.001	23.832	0.002	0.002	0.000	0.000	0.000	0.000
23	A	93	LEU	0	0.060	0.003	20.558	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	94	ALA	0	-0.026	0.003	23.622	0.001	0.001	0.000	0.000	0.000	0.000
25	A	95	LYS	1	0.951	0.974	23.258	0.074	0.074	0.000	0.000	0.000	0.000
26	A	96	ARG	1	0.858	0.912	26.749	0.078	0.078	0.000	0.000	0.000	0.000
27	A	97	ASN	0	-0.032	-0.007	27.547	0.007	0.007	0.000	0.000	0.000	0.000
28	A	98	TRP	0	-0.024	-0.026	27.491	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	99	LEU	0	-0.027	0.004	23.262	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	100	TRP	0	-0.025	-0.009	24.914	0.010	0.010	0.000	0.000	0.000	0.000
31	A	101	ALA	0	0.054	0.014	23.893	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	102	TYR	0	0.038	0.024	22.381	0.017	0.017	0.000	0.000	0.000	0.000
33	A	103	PRO	0	0.059	0.046	21.485	-0.021	-0.021	0.000	0.000	0.000	0.000
34	A	104	ASN	0	0.046	0.015	16.537	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	105	ILE	0	-0.022	-0.011	19.186	0.003	0.003	0.000	0.000	0.000	0.000
36	A	106	TYR	0	-0.016	0.002	21.489	0.014	0.014	0.000	0.000	0.000	0.000
37	A	107	SER	0	0.038	0.016	19.956	0.000	0.000	0.000	0.000	0.000	0.000
38	A	108	GLN	0	-0.045	-0.016	17.493	-0.014	-0.014	0.000	0.000	0.000	0.000
39	A	109	ASP	-1	-0.895	-0.939	16.894	-0.160	-0.160	0.000	0.000	0.000	0.000
40	A	110	PHE	0	-0.031	-0.024	18.267	0.007	0.007	0.000	0.000	0.000	0.000
41	A	111	GLY	0	0.014	0.018	14.024	0.003	0.003	0.000	0.000	0.000	0.000
42	A	112	ASN	0	0.025	-0.021	9.174	-0.038	-0.038	0.000	0.000	0.000	0.000
43	A	113	ILE	0	-0.030	0.010	12.967	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	114	ARG	1	0.860	0.924	14.550	0.307	0.307	0.000	0.000	0.000	0.000
45	A	115	ASN	0	-0.021	0.016	10.581	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	116	TRP	0	-0.014	-0.025	13.884	0.055	0.055	0.000	0.000	0.000	0.000
47	A	117	LYS	1	0.978	1.002	11.407	0.243	0.243	0.000	0.000	0.000	0.000
48	A	118	ILE	0	-0.018	-0.007	13.875	0.049	0.049	0.000	0.000	0.000	0.000
49	A	119	GLU	-1	-0.840	-0.910	15.834	-0.212	-0.212	0.000	0.000	0.000	0.000
50	A	120	PRO	0	0.015	-0.005	18.174	0.007	0.007	0.000	0.000	0.000	0.000
51	A	121	GLY	0	-0.009	-0.009	21.579	0.005	0.005	0.000	0.000	0.000	0.000
52	A	122	LYS	1	0.838	0.923	24.364	0.069	0.069	0.000	0.000	0.000	0.000
53	A	123	HIS	1	0.717	0.811	27.045	0.089	0.089	0.000	0.000	0.000	0.000
54	A	124	ARG	1	0.985	0.959	27.132	0.065	0.065	0.000	0.000	0.000	0.000
55	A	125	GLU	-1	-0.913	-0.940	26.323	-0.105	-0.105	0.000	0.000	0.000	0.000
56	A	126	TYR	0	-0.050	0.005	26.401	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	127	PHE	0	0.037	0.026	20.454	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	128	ARG	1	0.890	0.953	19.046	0.161	0.161	0.000	0.000	0.000	0.000
59	A	129	PHE	0	-0.005	-0.015	18.467	-0.019	-0.019	0.000	0.000	0.000	0.000
60	A	130	VAL	0	0.081	0.039	15.657	0.018	0.018	0.000	0.000	0.000	0.000
61	A	131	ASN	0	-0.045	-0.035	15.279	-0.040	-0.040	0.000	0.000	0.000	0.000
62	A	132	GLN	0	0.042	0.013	7.790	0.013	0.013	0.000	0.000	0.000	0.000
63	A	133	SER	0	-0.077	-0.030	12.533	0.034	0.034	0.000	0.000	0.000	0.000
64	A	134	LEU	0	0.006	-0.008	14.315	0.029	0.029	0.000	0.000	0.000	0.000
65	A	135	GLY	0	-0.011	0.011	16.221	0.021	0.021	0.000	0.000	0.000	0.000
66	A	136	THR	0	-0.097	-0.081	17.212	0.008	0.008	0.000	0.000	0.000	0.000
67	A	137	CYM	-1	-0.791	-0.871	19.256	-0.166	-0.166	0.000	0.000	0.000	0.000
68	A	138	ILE	0	-0.060	-0.007	20.887	0.014	0.014	0.000	0.000	0.000	0.000
69	A	139	GLU	-1	-0.898	-0.972	23.500	-0.083	-0.083	0.000	0.000	0.000	0.000
70	A	140	ALA	0	-0.032	-0.013	27.142	0.001	0.001	0.000	0.000	0.000	0.000
71	A	141	TYR	0	0.001	-0.010	30.204	0.008	0.008	0.000	0.000	0.000	0.000
72	A	142	GLY	0	0.050	0.023	32.722	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	143	ASN	0	0.012	0.001	35.632	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	144	GLY	0	0.068	0.043	31.955	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	145	LEU	0	-0.006	0.016	25.572	0.001	0.001	0.000	0.000	0.000	0.000
76	A	146	ILE	0	0.014	0.022	27.523	0.001	0.001	0.000	0.000	0.000	0.000
77	A	147	HIS	0	0.044	0.063	22.683	-0.014	-0.014	0.000	0.000	0.000	0.000
78	A	148	ASP	-1	-0.788	-0.886	24.629	-0.067	-0.067	0.000	0.000	0.000	0.000
79	A	149	THR	0	-0.051	-0.039	23.857	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	150	CYS	0	0.016	0.000	20.775	0.001	0.001	0.000	0.000	0.000	0.000
81	A	151	SER	0	-0.054	-0.033	23.463	0.011	0.011	0.000	0.000	0.000	0.000
82	A	152	LEU	0	0.059	0.023	23.205	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	153	ASP	-1	-0.889	-0.940	26.544	-0.060	-0.060	0.000	0.000	0.000	0.000
84	A	154	LYS	1	0.864	0.942	27.461	0.082	0.082	0.000	0.000	0.000	0.000
85	A	155	LEU	0	0.045	0.020	28.811	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	156	ALA	0	-0.045	-0.028	29.875	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	157	GLN	0	-0.025	-0.022	25.130	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	158	GLU	-1	-0.729	-0.819	24.995	-0.109	-0.109	0.000	0.000	0.000	0.000
89	A	159	PHE	0	-0.034	-0.040	24.649	0.008	0.008	0.000	0.000	0.000	0.000
90	A	160	GLU	-1	-0.900	-0.956	25.996	-0.106	-0.106	0.000	0.000	0.000	0.000
91	A	161	LEU	0	-0.018	-0.010	21.224	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	162	LEU	0	-0.003	-0.005	25.888	0.002	0.002	0.000	0.000	0.000	0.000
93	A	163	PRO	0	0.039	0.023	27.566	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	164	THR	0	-0.018	-0.031	28.648	0.011	0.011	0.000	0.000	0.000	0.000
95	A	165	ASP	-1	-0.939	-0.978	29.825	-0.105	-0.105	0.000	0.000	0.000	0.000
96	A	166	SER	0	0.011	0.012	29.176	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	167	GLY	0	-0.022	-0.009	25.951	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	168	ALA	0	-0.040	0.003	24.709	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	169	VAL	0	-0.016	0.001	23.399	0.008	0.008	0.000	0.000	0.000	0.000
100	A	170	VAL	0	0.060	0.022	26.551	0.001	0.001	0.000	0.000	0.000	0.000
101	A	171	ILE	0	-0.016	-0.005	23.726	0.000	0.000	0.000	0.000	0.000	0.000
102	A	172	LYS	1	0.981	0.979	27.389	0.098	0.098	0.000	0.000	0.000	0.000
103	A	173	SER	0	-0.002	0.009	29.026	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	174	VAL	0	0.044	0.032	29.553	0.007	0.007	0.000	0.000	0.000	0.000
105	A	175	SER	0	-0.049	-0.028	31.814	0.005	0.005	0.000	0.000	0.000	0.000
106	A	176	GLN	0	0.021	-0.003	33.480	0.005	0.005	0.000	0.000	0.000	0.000
107	A	177	GLY	0	0.019	0.009	34.248	0.004	0.004	0.000	0.000	0.000	0.000
108	A	178	ARG	1	0.777	0.872	34.225	0.079	0.079	0.000	0.000	0.000	0.000
109	A	179	CYS	0	0.101	0.088	31.426	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	180	VAL	0	-0.011	0.005	26.582	0.007	0.007	0.000	0.000	0.000	0.000
111	A	181	THR	0	-0.036	-0.005	29.807	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	182	TYR	0	-0.013	-0.007	27.957	-0.002	-0.002	0.000	0.000	0.000	0.000
113	A	183	ASN	0	0.044	0.038	31.284	0.001	0.001	0.000	0.000	0.000	0.000
114	A	184	PRO	0	-0.006	0.018	30.134	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	185	VAL	0	0.024	0.007	30.900	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	186	SER	0	-0.007	-0.018	31.781	0.006	0.006	0.000	0.000	0.000	0.000
117	A	187	PRO	0	-0.030	0.008	33.840	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	188	THR	0	-0.054	-0.015	31.331	0.002	0.002	0.000	0.000	0.000	0.000
119	A	189	TYR	0	0.003	-0.011	27.285	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	190	TYR	0	-0.020	-0.010	27.084	-0.009	-0.009	0.000	0.000	0.000	0.000
121	A	191	SER	0	0.016	-0.018	27.658	0.006	0.006	0.000	0.000	0.000	0.000
122	A	192	THR	0	-0.029	-0.037	28.803	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	193	VAL	0	-0.012	-0.003	26.662	-0.002	-0.002	0.000	0.000	0.000	0.000
124	A	194	THR	0	-0.026	-0.032	30.097	0.005	0.005	0.000	0.000	0.000	0.000
125	A	195	LEU	0	-0.035	0.000	30.419	-0.006	-0.006	0.000	0.000	0.000	0.000
126	A	196	SER	0	-0.046	-0.042	33.713	0.007	0.007	0.000	0.000	0.000	0.000
127	A	197	THR	0	0.037	0.008	35.876	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	198	CYS	0	-0.112	-0.071	34.781	-0.006	-0.006	0.000	0.000	0.000	0.000
129	A	199	ASP	-1	-0.838	-0.895	36.194	-0.079	-0.079	0.000	0.000	0.000	0.000
130	A	200	GLY	0	0.004	0.013	34.014	0.001	0.001	0.000	0.000	0.000	0.000
131	A	201	ALA	0	-0.006	0.009	35.064	0.000	0.000	0.000	0.000	0.000	0.000
132	A	202	THR	0	-0.017	-0.007	32.484	-0.007	-0.007	0.000	0.000	0.000	0.000
133	A	203	GLU	-1	-0.937	-0.971	34.827	-0.074	-0.074	0.000	0.000	0.000	0.000
134	A	204	PRO	0	0.036	-0.006	35.030	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	205	LEU	0	-0.021	-0.015	35.044	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	206	ARG	1	0.807	0.881	35.330	0.084	0.084	0.000	0.000	0.000	0.000
137	A	207	ASP	-1	-0.753	-0.874	31.215	-0.120	-0.120	0.000	0.000	0.000	0.000
138	A	208	GLN	0	-0.006	-0.032	30.959	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	209	THR	0	-0.037	0.007	28.698	-0.008	-0.008	0.000	0.000	0.000	0.000
140	A	210	TRP	0	-0.011	0.000	23.414	-0.004	-0.004	0.000	0.000	0.000	0.000
141	A	211	TYR	0	-0.007	-0.048	21.170	0.002	0.002	0.000	0.000	0.000	0.000
142	A	212	LEU	0	-0.022	-0.007	18.428	-0.013	-0.013	0.000	0.000	0.000	0.000
143	A	213	ALA	0	0.015	0.005	16.570	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	214	PRO	0	0.039	0.008	11.385	-0.032	-0.032	0.000	0.000	0.000	0.000
145	A	215	PRO	0	0.011	0.048	9.099	0.096	0.096	0.000	0.000	0.000	0.000
146	A	216	VAL	0	-0.033	-0.021	11.248	-0.026	-0.026	0.000	0.000	0.000	0.000
147	A	217	LEU	0	-0.052	-0.034	6.295	0.028	0.028	0.000	0.000	0.000	0.000
148	A	218	GLU	-1	-0.932	-0.949	6.661	-0.517	-0.517	0.000	0.000	0.000	0.000
149	A	219	ALA	0	-0.018	-0.010	5.278	-0.498	-0.498	0.000	0.000	0.000	0.000
150	A	220	THR	0	-0.013	-0.013	3.262	-1.223	-0.192	0.110	-0.378	-0.764	-0.003
151	A	221	ALA	0	-0.011	-0.001	5.222	-0.089	-0.106	-0.001	-0.001	0.019	0.000
152	A	222	VAL	0	0.006	-0.001	5.800	0.289	0.289	0.000	0.000	0.000	0.000
153	A	223	ASN	0	-0.002	0.005	8.290	0.005	0.005	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:71:PRO)