FMO DATABASE

FMODB ID: ZZ7ZN

Calculation Name: 2F9F-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F9F

Chain ID: A

ChEMBL ID:

UniProt ID: O30192

Base Structure: X-ray

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1823225.480182
FMO2-HF: Nuclear repulsion	1756029.607604
FMO2-HF: Total energy	-67195.872578
FMO2-MP2: Total energy	-67391.196427

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:2:VAL)

Summations of interaction energy for fragment #1(A:2:VAL)

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.
-100.747	-98.08	27.277	-14.305	-15.64	-0.162

Interaction energy analysis for fragmet #1(A:2:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.762 / q_NPA : 0.864

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	4	THR	0	0.038	0.005	2.676	9.245	11.256	0.239	-0.652	-1.598	-0.001
4	A	5	SER	0	-0.027	-0.012	4.591	6.004	6.132	-0.001	-0.013	-0.114	0.000
101	A	102	LEU	0	0.023	0.000	2.355	-1.802	-2.040	2.566	-0.365	-1.963	-0.002
102	A	103	THR	0	0.043	0.029	4.644	-1.151	-1.107	-0.001	-0.002	-0.041	0.000
104	A	105	ILE	0	-0.005	0.016	2.536	-0.228	0.894	1.024	-0.381	-1.765	-0.003
105	A	106	GLU	-1	-0.826	-0.887	4.416	-31.542	-31.403	-0.001	-0.009	-0.129	0.000
164	A	165	LYS	1	0.891	0.939	4.848	19.982	19.976	-0.001	-0.004	0.011	0.000
166	A	167	PHE	-1	-0.801	-0.879	1.825	-145.732	-146.265	23.452	-12.879	-10.041	-0.156
5	A	6	LYS	1	0.882	0.933	6.943	32.009	32.009	0.000	0.000	0.000	0.000
6	A	7	PHE	0	-0.012	-0.002	4.972	3.276	3.276	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.929	0.968	9.370	20.549	20.549	0.000	0.000	0.000	0.000
8	A	9	PHE	0	0.038	0.016	12.548	0.444	0.444	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.822	0.907	15.272	15.538	15.538	0.000	0.000	0.000	0.000
10	A	11	CYS	0	-0.039	-0.020	18.650	0.563	0.563	0.000	0.000	0.000	0.000
11	A	12	TYR	0	0.000	-0.014	16.982	-0.427	-0.427	0.000	0.000	0.000	0.000
12	A	13	GLY	0	0.016	0.014	20.628	0.597	0.597	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.868	-0.933	22.629	-11.023	-11.023	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.046	-0.011	18.444	0.235	0.235	0.000	0.000	0.000	0.000
15	A	16	TRP	0	-0.011	-0.011	18.025	-0.847	-0.847	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.000	0.004	13.279	0.373	0.373	0.000	0.000	0.000	0.000
17	A	18	SER	0	0.014	-0.012	15.059	-0.245	-0.245	0.000	0.000	0.000	0.000
18	A	19	VAL	0	0.037	0.016	10.881	0.448	0.448	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.028	0.016	12.758	-0.945	-0.945	0.000	0.000	0.000	0.000
20	A	21	ARG	1	0.915	0.952	15.261	15.880	15.880	0.000	0.000	0.000	0.000
21	A	22	ILE	0	-0.006	0.004	17.798	0.169	0.169	0.000	0.000	0.000	0.000
22	A	23	TYR	0	0.014	-0.011	20.237	0.520	0.520	0.000	0.000	0.000	0.000
23	A	24	PRO	0	0.015	0.003	21.373	-0.270	-0.270	0.000	0.000	0.000	0.000
24	A	25	GLU	-1	-0.879	-0.928	18.720	-13.217	-13.217	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.779	0.849	14.023	17.088	17.088	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.765	0.865	18.831	13.423	13.423	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.038	0.022	19.306	0.085	0.085	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.807	-0.906	22.501	-10.779	-10.779	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.029	0.001	21.717	0.256	0.256	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.022	0.009	17.801	0.293	0.293	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.017	-0.008	23.089	0.233	0.233	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.883	-0.939	26.519	-8.979	-8.979	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.022	0.002	23.814	0.257	0.257	0.000	0.000	0.000	0.000
34	A	35	PHE	0	0.000	-0.009	22.151	0.164	0.164	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.852	0.933	27.401	9.421	9.421	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.906	0.965	30.142	9.465	9.465	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.034	-0.016	26.105	0.205	0.205	0.000	0.000	0.000	0.000
38	A	39	GLN	0	0.000	-0.007	28.913	-0.110	-0.110	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.912	-0.951	30.585	-9.315	-9.315	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.850	-0.880	25.014	-11.453	-11.453	0.000	0.000	0.000	0.000
41	A	42	LYS	1	0.910	0.932	25.175	10.308	10.308	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.016	0.005	19.346	-0.455	-0.455	0.000	0.000	0.000	0.000
43	A	44	TYR	0	-0.036	-0.023	19.826	0.665	0.665	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.041	0.021	18.592	-0.692	-0.692	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.022	0.012	14.790	0.491	0.491	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.017	0.004	16.346	-0.722	-0.722	0.000	0.000	0.000	0.000
47	A	48	TRP	0	-0.019	-0.013	18.296	0.626	0.626	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.003	-0.005	20.658	-0.362	-0.362	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.010	-0.009	22.989	-0.087	-0.087	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.949	0.960	24.506	9.812	9.812	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.020	-0.018	28.042	0.103	0.103	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.820	-0.873	25.667	-10.932	-10.932	0.000	0.000	0.000	0.000
53	A	54	HIS	0	0.005	-0.010	28.582	0.228	0.228	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.026	0.011	24.679	0.131	0.131	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.778	-0.858	26.800	-9.587	-9.587	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.929	0.960	28.601	8.596	8.596	0.000	0.000	0.000	0.000
57	A	58	TYR	0	-0.083	-0.054	23.488	0.179	0.179	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.082	0.032	25.297	0.066	0.066	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.861	0.901	26.817	9.241	9.241	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.880	0.944	30.327	9.257	9.257	0.000	0.000	0.000	0.000
61	A	62	ILE	0	0.016	0.007	24.655	0.198	0.198	0.000	0.000	0.000	0.000
62	A	63	MET	0	-0.020	-0.011	26.868	0.056	0.056	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.921	0.975	28.864	8.441	8.441	0.000	0.000	0.000	0.000
64	A	65	ILE	0	-0.074	-0.029	29.701	0.275	0.275	0.000	0.000	0.000	0.000
65	A	66	ALA	0	0.018	0.005	28.029	-0.053	-0.053	0.000	0.000	0.000	0.000
66	A	67	PRO	0	-0.018	0.004	28.445	0.273	0.273	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.877	-0.951	29.520	-9.110	-9.110	0.000	0.000	0.000	0.000
68	A	69	ASN	0	-0.066	-0.027	28.366	-0.043	-0.043	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.031	-0.019	23.920	-0.472	-0.472	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.918	0.969	24.086	10.902	10.902	0.000	0.000	0.000	0.000
71	A	72	PHE	0	0.030	0.000	22.616	-0.486	-0.486	0.000	0.000	0.000	0.000
72	A	73	LEU	0	0.009	-0.006	19.210	0.355	0.355	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.022	0.022	21.477	0.065	0.065	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.066	-0.046	17.857	-0.800	-0.800	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.015	0.026	15.409	0.459	0.459	0.000	0.000	0.000	0.000
76	A	77	SER	0	-0.003	-0.037	15.894	-0.821	-0.821	0.000	0.000	0.000	0.000
77	A	78	GLU	-1	-0.790	-0.895	9.088	-27.100	-27.100	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.877	-0.951	12.728	-17.718	-17.718	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.839	-0.887	15.192	-14.159	-14.159	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.006	0.009	9.850	0.307	0.307	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.013	-0.004	9.759	-0.124	-0.124	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.829	-0.869	12.116	-14.351	-14.351	0.000	0.000	0.000	0.000
83	A	84	LEU	0	0.007	0.011	15.255	0.511	0.511	0.000	0.000	0.000	0.000
84	A	85	TYR	0	0.012	-0.037	8.215	1.335	1.335	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.038	-0.027	13.147	0.684	0.684	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.828	0.876	14.837	14.468	14.468	0.000	0.000	0.000	0.000
87	A	88	CYS	0	-0.020	0.028	15.223	0.469	0.469	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.841	0.895	18.039	11.256	11.256	0.000	0.000	0.000	0.000
89	A	90	GLY	0	0.038	0.004	15.861	-0.222	-0.222	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.047	-0.009	10.420	0.455	0.455	0.000	0.000	0.000	0.000
91	A	92	LEU	0	-0.009	-0.001	14.551	0.179	0.179	0.000	0.000	0.000	0.000
92	A	93	CYS	0	-0.015	-0.002	12.137	-0.469	-0.469	0.000	0.000	0.000	0.000
93	A	94	THR	0	0.030	-0.008	15.002	0.282	0.282	0.000	0.000	0.000	0.000
94	A	95	ALA	0	-0.018	0.006	14.694	0.712	0.712	0.000	0.000	0.000	0.000
95	A	96	LYS	1	0.932	0.959	16.595	12.448	12.448	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.780	-0.879	15.537	-16.579	-16.579	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.821	-0.900	10.746	-21.254	-21.254	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.887	-0.942	10.936	-19.852	-19.852	0.000	0.000	0.000	0.000
99	A	100	PHE	0	-0.018	-0.023	5.673	-0.838	-0.838	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.007	0.012	5.323	-3.258	-3.258	0.000	0.000	0.000	0.000
103	A	104	PRO	0	0.031	-0.007	7.577	0.532	0.532	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.001	0.005	6.220	2.323	2.323	0.000	0.000	0.000	0.000
107	A	108	MET	0	-0.037	0.001	7.647	2.317	2.317	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.025	0.005	5.947	1.309	1.309	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.052	-0.030	8.107	1.957	1.957	0.000	0.000	0.000	0.000
110	A	111	GLY	0	-0.017	-0.015	11.115	2.058	2.058	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.705	0.838	12.378	18.697	18.697	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.029	0.019	12.717	-1.216	-1.216	0.000	0.000	0.000	0.000
113	A	114	VAL	0	-0.010	-0.011	10.560	0.196	0.196	0.000	0.000	0.000	0.000
114	A	115	ILE	0	-0.023	0.001	14.040	0.444	0.444	0.000	0.000	0.000	0.000
115	A	116	ALA	0	0.015	-0.001	13.868	-0.188	-0.188	0.000	0.000	0.000	0.000
116	A	117	VAL	0	0.014	0.020	15.983	0.568	0.568	0.000	0.000	0.000	0.000
117	A	118	ASN	0	-0.003	0.002	16.032	-1.638	-1.638	0.000	0.000	0.000	0.000
118	A	119	GLU	-1	-0.837	-0.906	15.955	-13.552	-13.552	0.000	0.000	0.000	0.000
119	A	120	GLY	0	0.028	0.012	13.137	-0.838	-0.838	0.000	0.000	0.000	0.000
120	A	121	GLY	0	0.065	0.020	8.893	-0.026	-0.026	0.000	0.000	0.000	0.000
121	A	122	PHE	0	-0.025	-0.008	9.141	-1.793	-1.793	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.858	0.934	11.290	18.093	18.093	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.857	-0.906	9.112	-21.379	-21.379	0.000	0.000	0.000	0.000
124	A	125	THR	0	-0.050	-0.033	5.945	-0.921	-0.921	0.000	0.000	0.000	0.000
125	A	126	VAL	0	-0.007	-0.005	8.796	-0.331	-0.331	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.019	0.013	12.029	1.104	1.104	0.000	0.000	0.000	0.000
127	A	128	ASN	0	0.076	0.024	14.746	0.464	0.464	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.958	-0.989	18.024	-12.153	-12.153	0.000	0.000	0.000	0.000
129	A	130	LYS	1	0.893	0.943	17.080	15.437	15.437	0.000	0.000	0.000	0.000
130	A	131	THR	0	0.005	-0.018	12.106	-0.006	-0.006	0.000	0.000	0.000	0.000
131	A	132	GLY	0	0.037	0.016	14.227	-0.580	-0.580	0.000	0.000	0.000	0.000
132	A	133	TYR	0	-0.060	-0.040	16.666	0.791	0.791	0.000	0.000	0.000	0.000
133	A	134	LEU	0	-0.005	0.014	14.287	-0.377	-0.377	0.000	0.000	0.000	0.000
134	A	135	VAL	0	-0.033	-0.004	18.247	0.639	0.639	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.027	-0.049	20.367	-0.739	-0.739	0.000	0.000	0.000	0.000
136	A	137	ALA	0	-0.030	-0.017	21.906	-0.179	-0.179	0.000	0.000	0.000	0.000
137	A	138	ASP	-1	-0.830	-0.915	23.077	-9.865	-9.865	0.000	0.000	0.000	0.000
138	A	139	VAL	0	-0.004	-0.022	25.021	-0.244	-0.244	0.000	0.000	0.000	0.000
139	A	140	ASN	0	-0.049	-0.023	27.112	0.175	0.175	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.762	-0.866	24.584	-11.639	-11.639	0.000	0.000	0.000	0.000
141	A	142	ILE	0	0.019	0.010	21.141	-0.350	-0.350	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.026	0.011	23.378	-0.162	-0.162	0.000	0.000	0.000	0.000
143	A	144	ASP	-1	-0.887	-0.946	26.237	-10.053	-10.053	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.038	-0.020	21.293	-0.077	-0.077	0.000	0.000	0.000	0.000
145	A	146	MET	0	0.019	0.000	21.729	-0.242	-0.242	0.000	0.000	0.000	0.000
146	A	147	LYS	1	0.935	0.983	23.355	9.784	9.784	0.000	0.000	0.000	0.000
147	A	148	LYS	1	0.892	0.956	23.777	11.965	11.965	0.000	0.000	0.000	0.000
148	A	149	VAL	0	-0.012	-0.002	19.501	0.006	0.006	0.000	0.000	0.000	0.000
149	A	150	SER	0	-0.021	-0.025	22.631	0.018	0.018	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.909	0.963	25.348	9.692	9.692	0.000	0.000	0.000	0.000
151	A	152	ASN	0	-0.051	-0.026	24.416	-0.065	-0.065	0.000	0.000	0.000	0.000
152	A	153	PRO	0	0.049	0.040	21.434	-0.401	-0.401	0.000	0.000	0.000	0.000
153	A	154	ASP	-1	-0.906	-0.961	19.787	-13.718	-13.718	0.000	0.000	0.000	0.000
154	A	155	LYS	1	0.895	0.967	20.513	12.120	12.120	0.000	0.000	0.000	0.000
155	A	156	PHE	0	0.025	0.010	16.720	0.119	0.119	0.000	0.000	0.000	0.000
156	A	157	LYS	1	0.916	0.992	16.201	14.315	14.315	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.943	0.958	15.024	13.626	13.626	0.000	0.000	0.000	0.000
158	A	159	ASP	-1	-0.796	-0.881	14.570	-18.408	-18.408	0.000	0.000	0.000	0.000
159	A	160	CYS	0	-0.063	-0.003	11.912	-1.365	-1.365	0.000	0.000	0.000	0.000
160	A	161	PHE	0	-0.004	-0.005	10.304	-1.583	-1.583	0.000	0.000	0.000	0.000
161	A	162	ARG	1	0.774	0.883	10.322	18.468	18.468	0.000	0.000	0.000	0.000
162	A	163	ARG	1	0.867	0.920	8.783	25.418	25.418	0.000	0.000	0.000	0.000
163	A	164	ALA	0	-0.001	-0.003	5.931	-3.329	-3.329	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.902	-0.941	6.230	-27.909	-27.909	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:VAL)