FMO DATABASE

FMODB ID: 87YYY

Calculation Name: 6J9C-D-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6J9C

Chain ID: D

ChEMBL ID:

UniProt ID: Q1PFR7

Base Structure: X-ray

Registration Date: 2025-10-04

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	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-928892.109624
FMO2-HF: Nuclear repulsion	883080.699455
FMO2-HF: Total energy	-45811.410168
FMO2-MP2: Total energy	-45943.506106

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:160:SER)

Summations of interaction energy for fragment #1(A:160: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.
-77.924	-76.848	12.695	-6.851	-6.919	-0.073

Interaction energy analysis for fragmet #1(A:160:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.779 / q_NPA : 0.873

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	162	PHE	0	0.018	0.014	3.623	-6.075	-4.630	-0.003	-0.766	-0.676	-0.002
5	A	164	ASN	0	-0.041	-0.018	2.790	-4.694	-4.147	0.045	-0.189	-0.403	-0.001
6	A	165	LYS	1	0.909	0.967	3.635	39.289	39.995	0.008	-0.312	-0.402	-0.002
7	A	166	LYS	1	0.948	0.957	1.861	-2.407	-4.493	10.019	-4.553	-3.380	-0.058
8	A	167	LEU	0	0.039	0.010	2.171	3.041	3.310	2.628	-1.013	-1.884	-0.010
9	A	168	ARG	1	0.865	0.941	4.623	20.202	20.315	-0.001	-0.005	-0.106	0.000
54	A	213	VAL	0	-0.012	-0.015	4.430	-3.007	-2.925	-0.001	-0.013	-0.068	0.000
4	A	163	ASP	-1	-0.809	-0.883	6.089	-39.808	-39.808	0.000	0.000	0.000	0.000
10	A	169	VAL	0	0.043	0.013	7.305	0.186	0.186	0.000	0.000	0.000	0.000
11	A	170	LEU	0	-0.070	-0.025	9.029	1.522	1.522	0.000	0.000	0.000	0.000
12	A	171	CYS	0	-0.020	-0.017	12.370	1.711	1.711	0.000	0.000	0.000	0.000
13	A	172	GLU	-1	-0.835	-0.910	12.370	-23.304	-23.304	0.000	0.000	0.000	0.000
14	A	173	LYS	1	0.724	0.866	14.520	15.225	15.225	0.000	0.000	0.000	0.000
15	A	174	GLU	-1	-0.794	-0.852	17.079	-14.017	-14.017	0.000	0.000	0.000	0.000
16	A	175	LEU	0	-0.045	-0.037	18.178	0.886	0.886	0.000	0.000	0.000	0.000
17	A	176	LYS	1	0.852	0.904	20.968	13.296	13.296	0.000	0.000	0.000	0.000
18	A	177	ASN	0	0.045	0.006	24.752	-0.239	-0.239	0.000	0.000	0.000	0.000
19	A	178	SER	0	-0.022	-0.021	27.578	0.129	0.129	0.000	0.000	0.000	0.000
20	A	179	ASP	-1	-0.799	-0.882	22.219	-13.074	-13.074	0.000	0.000	0.000	0.000
21	A	180	VAL	0	0.043	0.027	22.363	-0.310	-0.310	0.000	0.000	0.000	0.000
22	A	181	GLY	0	0.037	0.037	24.778	0.322	0.322	0.000	0.000	0.000	0.000
23	A	182	SER	0	-0.013	-0.036	28.239	-0.243	-0.243	0.000	0.000	0.000	0.000
24	A	183	LEU	0	-0.066	-0.018	28.107	0.229	0.229	0.000	0.000	0.000	0.000
25	A	184	GLY	0	0.011	0.010	26.854	0.009	0.009	0.000	0.000	0.000	0.000
26	A	185	ARG	1	0.852	0.920	24.579	10.119	10.119	0.000	0.000	0.000	0.000
27	A	186	ILE	0	0.074	0.060	19.104	0.220	0.220	0.000	0.000	0.000	0.000
28	A	187	VAL	0	-0.035	-0.023	22.476	-0.055	-0.055	0.000	0.000	0.000	0.000
29	A	188	LEU	0	0.009	-0.010	17.866	-0.523	-0.523	0.000	0.000	0.000	0.000
30	A	189	PRO	0	0.026	0.009	18.371	0.886	0.886	0.000	0.000	0.000	0.000
31	A	190	LYS	1	0.824	0.900	20.748	10.830	10.830	0.000	0.000	0.000	0.000
32	A	191	ARG	1	0.937	0.970	20.530	13.398	13.398	0.000	0.000	0.000	0.000
33	A	192	ASP	-1	-0.849	-0.927	16.653	-16.298	-16.298	0.000	0.000	0.000	0.000
34	A	193	ALA	0	0.010	-0.001	18.398	-0.400	-0.400	0.000	0.000	0.000	0.000
35	A	194	GLU	-1	-0.792	-0.880	19.985	-11.407	-11.407	0.000	0.000	0.000	0.000
36	A	195	ALA	0	-0.055	-0.026	19.226	0.170	0.170	0.000	0.000	0.000	0.000
37	A	196	ASN	0	-0.096	-0.060	15.150	-0.472	-0.472	0.000	0.000	0.000	0.000
38	A	197	LEU	0	0.049	0.057	15.159	-0.678	-0.678	0.000	0.000	0.000	0.000
39	A	198	PRO	0	-0.005	-0.006	17.497	0.703	0.703	0.000	0.000	0.000	0.000
40	A	199	LYS	1	0.940	0.969	20.449	13.599	13.599	0.000	0.000	0.000	0.000
41	A	200	LEU	0	0.029	0.039	23.213	0.284	0.284	0.000	0.000	0.000	0.000
42	A	201	SER	0	0.012	-0.004	26.340	0.137	0.137	0.000	0.000	0.000	0.000
43	A	202	ASP	-1	-0.819	-0.896	29.639	-9.099	-9.099	0.000	0.000	0.000	0.000
44	A	203	LYS	1	0.944	0.964	29.821	8.299	8.299	0.000	0.000	0.000	0.000
45	A	204	GLU	-1	-0.960	-0.981	30.292	-10.195	-10.195	0.000	0.000	0.000	0.000
46	A	205	GLY	0	-0.040	-0.024	27.000	-0.208	-0.208	0.000	0.000	0.000	0.000
47	A	206	ILE	0	-0.006	-0.005	20.974	0.135	0.135	0.000	0.000	0.000	0.000
48	A	207	VAL	0	0.013	0.007	23.032	-0.142	-0.142	0.000	0.000	0.000	0.000
49	A	208	VAL	0	-0.026	-0.015	17.374	-0.265	-0.265	0.000	0.000	0.000	0.000
50	A	209	GLN	0	-0.007	-0.002	16.975	0.759	0.759	0.000	0.000	0.000	0.000
51	A	210	MET	0	-0.018	-0.004	13.182	-0.963	-0.963	0.000	0.000	0.000	0.000
52	A	211	ARG	1	0.890	0.957	8.033	34.667	34.667	0.000	0.000	0.000	0.000
53	A	212	ASP	-1	-0.726	-0.827	10.593	-28.707	-28.707	0.000	0.000	0.000	0.000
55	A	214	PHE	0	-0.025	-0.016	6.788	-5.993	-5.993	0.000	0.000	0.000	0.000
56	A	215	SER	0	-0.002	-0.026	8.869	1.601	1.601	0.000	0.000	0.000	0.000
57	A	216	MET	0	-0.025	-0.028	11.203	-1.281	-1.281	0.000	0.000	0.000	0.000
58	A	217	GLN	0	0.031	0.051	14.141	2.464	2.464	0.000	0.000	0.000	0.000
59	A	218	SER	0	-0.056	-0.037	14.298	-1.198	-1.198	0.000	0.000	0.000	0.000
60	A	219	TRP	0	0.014	-0.001	16.411	1.527	1.527	0.000	0.000	0.000	0.000
61	A	220	SER	0	-0.013	-0.009	17.922	-0.679	-0.679	0.000	0.000	0.000	0.000
62	A	221	PHE	0	0.028	0.014	16.961	0.579	0.579	0.000	0.000	0.000	0.000
63	A	222	LYS	1	0.870	0.935	21.955	10.928	10.928	0.000	0.000	0.000	0.000
64	A	223	TYR	0	0.024	0.022	20.713	0.069	0.069	0.000	0.000	0.000	0.000
65	A	224	LYS	1	0.855	0.913	22.824	10.902	10.902	0.000	0.000	0.000	0.000
66	A	225	PHE	0	-0.034	-0.016	25.439	-0.210	-0.210	0.000	0.000	0.000	0.000
67	A	226	TRP	0	0.017	0.016	28.028	0.319	0.319	0.000	0.000	0.000	0.000
68	A	227	SER	0	0.008	-0.012	31.143	-0.132	-0.132	0.000	0.000	0.000	0.000
69	A	228	ASN	0	-0.001	-0.014	31.541	0.283	0.283	0.000	0.000	0.000	0.000
70	A	229	ASN	0	0.036	0.024	34.165	0.080	0.080	0.000	0.000	0.000	0.000
71	A	230	LYS	1	0.950	0.971	36.977	7.543	7.543	0.000	0.000	0.000	0.000
72	A	231	SER	0	-0.003	0.001	31.670	-0.201	-0.201	0.000	0.000	0.000	0.000
73	A	232	ARG	1	0.838	0.928	27.420	10.965	10.965	0.000	0.000	0.000	0.000
74	A	233	MET	0	-0.008	-0.008	27.748	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	234	TYR	0	0.004	0.000	23.103	0.272	0.272	0.000	0.000	0.000	0.000
76	A	235	VAL	0	-0.023	-0.006	23.666	-0.075	-0.075	0.000	0.000	0.000	0.000
77	A	236	LEU	0	0.038	0.031	18.110	-0.013	-0.013	0.000	0.000	0.000	0.000
78	A	237	GLU	-1	-0.804	-0.921	22.327	-10.453	-10.453	0.000	0.000	0.000	0.000
79	A	238	ASN	0	-0.003	-0.012	23.997	-0.093	-0.093	0.000	0.000	0.000	0.000
80	A	239	THR	0	0.023	0.013	20.683	-0.151	-0.151	0.000	0.000	0.000	0.000
81	A	240	GLY	0	0.027	0.012	22.864	-0.137	-0.137	0.000	0.000	0.000	0.000
82	A	241	GLU	-1	-0.825	-0.919	24.829	-11.767	-11.767	0.000	0.000	0.000	0.000
83	A	242	PHE	0	-0.020	0.007	15.169	0.013	0.013	0.000	0.000	0.000	0.000
84	A	243	VAL	0	0.042	0.026	20.194	-0.587	-0.587	0.000	0.000	0.000	0.000
85	A	244	LYS	1	0.847	0.916	21.698	11.261	11.261	0.000	0.000	0.000	0.000
86	A	245	GLN	0	-0.064	-0.036	20.966	-0.231	-0.231	0.000	0.000	0.000	0.000
87	A	246	ASN	0	-0.062	-0.046	16.337	-1.173	-1.173	0.000	0.000	0.000	0.000
88	A	247	GLY	0	-0.009	0.018	19.206	-0.279	-0.279	0.000	0.000	0.000	0.000
89	A	248	ALA	0	-0.010	0.003	18.933	0.102	0.102	0.000	0.000	0.000	0.000
90	A	249	GLU	-1	-0.930	-0.967	20.607	-12.214	-12.214	0.000	0.000	0.000	0.000
91	A	250	ILE	0	-0.110	-0.066	21.999	-0.208	-0.208	0.000	0.000	0.000	0.000
92	A	251	GLY	0	0.003	-0.005	21.731	0.175	0.175	0.000	0.000	0.000	0.000
93	A	252	ASP	-1	-0.775	-0.875	17.681	-16.272	-16.272	0.000	0.000	0.000	0.000
94	A	253	PHE	0	-0.011	-0.015	13.757	0.542	0.542	0.000	0.000	0.000	0.000
95	A	254	LEU	0	-0.028	-0.011	13.596	-1.064	-1.064	0.000	0.000	0.000	0.000
96	A	255	THR	0	-0.019	-0.028	9.400	0.790	0.790	0.000	0.000	0.000	0.000
97	A	256	ILE	0	-0.005	-0.016	10.699	-1.067	-1.067	0.000	0.000	0.000	0.000
98	A	257	TYR	0	0.008	-0.015	5.667	-0.769	-0.769	0.000	0.000	0.000	0.000
99	A	258	GLU	-1	-0.879	-0.933	8.607	-20.961	-20.961	0.000	0.000	0.000	0.000
100	A	259	ASP	-1	-0.816	-0.920	7.108	-37.079	-37.079	0.000	0.000	0.000	0.000
101	A	260	GLU	-1	-0.926	-0.962	7.966	-24.447	-24.447	0.000	0.000	0.000	0.000
102	A	261	SER	0	-0.093	-0.054	10.029	2.974	2.974	0.000	0.000	0.000	0.000
103	A	262	LYS	1	0.934	0.972	12.035	18.895	18.895	0.000	0.000	0.000	0.000
104	A	263	ASN	0	-0.016	0.017	10.935	2.585	2.585	0.000	0.000	0.000	0.000
105	A	264	LEU	0	0.035	0.007	10.720	-2.213	-2.213	0.000	0.000	0.000	0.000
106	A	265	TYR	0	-0.088	-0.056	7.791	-1.050	-1.050	0.000	0.000	0.000	0.000
107	A	266	PHE	0	0.009	-0.007	9.826	0.987	0.987	0.000	0.000	0.000	0.000
108	A	267	ALA	0	-0.004	-0.007	8.055	-2.075	-2.075	0.000	0.000	0.000	0.000
109	A	268	MET	0	-0.063	-0.018	9.762	0.719	0.719	0.000	0.000	0.000	0.000
110	A	269	ASN	0	0.020	0.006	10.036	0.669	0.669	0.000	0.000	0.000	0.000
111	A	270	GLY	0	0.018	0.010	13.508	0.204	0.204	0.000	0.000	0.000	0.000
112	A	271	ASN	-1	-0.937	-0.944	15.267	-14.952	-14.952	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:160:SER)