FMO DATABASE

FMODB ID: RLN38

Calculation Name: 1JO0-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1JO0

Chain ID: A

ChEMBL ID:

UniProt ID: P71376

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	97
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-682726.494001
FMO2-HF: Nuclear repulsion	646105.131995
FMO2-HF: Total energy	-36621.362006
FMO2-MP2: Total energy	-36730.599802

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:THR)

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

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.
-37.917	-30.786	21.047	-12.651	-15.527	-0.12

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.812 / q_NPA : 0.895

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	LEU	0	0.024	0.027	3.002	3.401	5.301	0.054	-0.596	-1.359	-0.001
4	A	5	SER	0	0.058	0.028	5.174	2.069	2.066	-0.001	-0.002	0.006	0.000
67	A	68	VAL	0	-0.042	0.004	4.530	-2.455	-2.405	-0.001	-0.002	-0.047	0.000
71	A	72	LYS	1	0.860	0.932	3.111	34.121	35.196	0.015	-0.474	-0.615	-0.002
72	A	73	ALA	0	0.008	0.021	1.845	-59.257	-60.251	15.469	-8.068	-6.408	-0.093
73	A	74	ALA	0	-0.025	-0.015	2.346	-11.378	-9.990	3.742	-1.968	-3.162	-0.016
74	A	75	GLN	0	0.038	0.007	3.170	12.642	12.546	0.075	0.337	-0.317	0.000
85	A	86	TYR	0	0.040	0.004	2.888	1.552	2.136	0.116	-0.189	-0.511	-0.001
86	A	87	ARG	1	0.762	0.821	2.643	19.376	21.930	0.420	-1.224	-1.749	-0.005
87	A	88	PRO	0	-0.030	0.004	2.376	2.349	2.993	1.159	-0.464	-1.339	-0.002
88	A	89	SER	0	-0.035	-0.042	5.284	-0.628	-0.599	-0.001	-0.001	-0.026	0.000
5	A	6	THR	0	0.034	-0.006	8.833	-1.044	-1.044	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.971	0.988	11.348	17.319	17.319	0.000	0.000	0.000	0.000
7	A	8	GLN	0	0.053	0.034	7.048	-2.059	-2.059	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.899	0.959	7.691	30.924	30.924	0.000	0.000	0.000	0.000
9	A	10	GLN	0	0.021	0.000	8.812	0.314	0.314	0.000	0.000	0.000	0.000
10	A	11	PHE	0	0.019	0.009	10.782	0.936	0.936	0.000	0.000	0.000	0.000
11	A	12	LEU	0	0.042	0.021	6.265	0.791	0.791	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.879	0.941	10.561	18.740	18.740	0.000	0.000	0.000	0.000
13	A	14	GLY	0	-0.030	-0.019	12.950	0.997	0.997	0.000	0.000	0.000	0.000
14	A	15	LEU	0	0.013	0.009	11.871	0.906	0.906	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.034	-0.002	12.291	0.678	0.678	0.000	0.000	0.000	0.000
16	A	17	HIS	0	-0.080	-0.030	14.293	0.131	0.131	0.000	0.000	0.000	0.000
17	A	18	HIS	0	0.020	0.002	17.846	0.849	0.849	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.002	0.031	13.346	0.374	0.374	0.000	0.000	0.000	0.000
19	A	20	ASN	0	0.023	0.006	17.597	0.238	0.238	0.000	0.000	0.000	0.000
20	A	21	PRO	0	-0.065	-0.059	17.057	-0.811	-0.811	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.003	0.011	14.196	0.734	0.734	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.034	0.037	14.790	0.085	0.085	0.000	0.000	0.000	0.000
23	A	24	MET	0	-0.054	-0.041	17.387	-0.129	-0.129	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.019	0.027	16.206	0.151	0.151	0.000	0.000	0.000	0.000
25	A	26	GLY	0	0.026	0.005	20.263	0.473	0.473	0.000	0.000	0.000	0.000
26	A	27	GLY	0	-0.011	-0.015	23.280	-0.410	-0.410	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.005	0.004	24.175	0.269	0.269	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.002	0.010	20.812	-0.300	-0.300	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.030	-0.023	13.637	-0.138	-0.138	0.000	0.000	0.000	0.000
30	A	31	THR	0	0.022	0.011	17.897	-0.042	-0.042	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.905	-0.954	17.736	-17.037	-17.037	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.074	0.034	17.466	-0.657	-0.657	0.000	0.000	0.000	0.000
33	A	34	VAL	0	0.024	0.012	16.190	-0.515	-0.515	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.011	-0.010	11.144	-1.429	-1.429	0.000	0.000	0.000	0.000
35	A	36	ALA	0	0.037	0.020	13.175	-1.466	-1.466	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.912	-0.963	15.087	-15.929	-15.929	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.030	-0.029	9.832	-0.653	-0.653	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.776	-0.857	8.925	-31.773	-31.773	0.000	0.000	0.000	0.000
39	A	40	ASN	0	-0.011	0.000	11.292	-0.148	-0.148	0.000	0.000	0.000	0.000
40	A	41	ALA	0	-0.003	-0.006	12.833	0.176	0.176	0.000	0.000	0.000	0.000
41	A	42	LEU	0	-0.059	-0.037	6.177	-0.659	-0.659	0.000	0.000	0.000	0.000
42	A	43	ASN	0	0.039	0.026	9.507	-2.090	-2.090	0.000	0.000	0.000	0.000
43	A	44	HIS	0	-0.030	-0.001	11.363	0.709	0.709	0.000	0.000	0.000	0.000
44	A	45	HIS	0	0.035	0.016	11.945	0.659	0.659	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.715	-0.828	6.979	-24.954	-24.954	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.110	-0.064	6.973	-3.979	-3.979	0.000	0.000	0.000	0.000
47	A	48	ILE	0	0.031	0.011	8.895	2.292	2.292	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.829	0.923	11.209	15.334	15.334	0.000	0.000	0.000	0.000
49	A	50	VAL	0	0.039	0.021	12.279	0.634	0.634	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.895	0.938	14.880	13.620	13.620	0.000	0.000	0.000	0.000
51	A	52	VAL	0	0.025	0.002	16.094	-0.034	-0.034	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.018	-0.016	19.165	0.241	0.241	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.008	0.004	22.875	0.049	0.049	0.000	0.000	0.000	0.000
54	A	55	ALA	0	-0.005	0.014	21.017	0.210	0.210	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.795	-0.872	23.002	-13.483	-13.483	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.900	0.940	19.817	13.267	13.267	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.831	-0.928	19.159	-14.946	-14.946	0.000	0.000	0.000	0.000
58	A	59	THR	0	0.004	-0.017	19.272	-0.828	-0.828	0.000	0.000	0.000	0.000
59	A	60	LYS	1	0.888	0.934	16.411	16.596	16.596	0.000	0.000	0.000	0.000
60	A	61	GLN	0	-0.043	-0.023	12.732	-0.590	-0.590	0.000	0.000	0.000	0.000
61	A	62	LEU	0	0.009	0.007	14.365	-1.655	-1.655	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.013	0.011	14.720	-1.214	-1.214	0.000	0.000	0.000	0.000
63	A	64	ILE	0	-0.034	-0.015	10.252	-1.664	-1.664	0.000	0.000	0.000	0.000
64	A	65	ASN	0	-0.005	-0.004	10.024	-4.192	-4.192	0.000	0.000	0.000	0.000
65	A	66	ALA	0	0.019	0.017	10.226	-2.331	-2.331	0.000	0.000	0.000	0.000
66	A	67	ILE	0	0.060	0.024	8.887	-1.488	-1.488	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.898	0.962	6.151	17.624	17.624	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.857	-0.917	8.327	-26.164	-26.164	0.000	0.000	0.000	0.000
70	A	71	THR	0	0.004	-0.017	6.426	-3.922	-3.922	0.000	0.000	0.000	0.000
75	A	76	VAL	0	-0.020	0.003	6.856	1.386	1.386	0.000	0.000	0.000	0.000
76	A	77	GLN	0	0.031	-0.005	8.769	3.149	3.149	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.021	0.024	12.127	-0.574	-0.574	0.000	0.000	0.000	0.000
78	A	79	ILE	0	-0.018	-0.008	14.482	0.736	0.736	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.037	0.021	18.061	0.248	0.248	0.000	0.000	0.000	0.000
80	A	81	HIS	0	0.052	0.032	19.727	-0.441	-0.441	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.003	0.007	15.472	-0.021	-0.021	0.000	0.000	0.000	0.000
82	A	83	LEU	0	0.015	0.011	11.830	-0.292	-0.292	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.012	-0.013	10.229	0.831	0.831	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.008	-0.004	6.933	-2.226	-2.226	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.964	-0.981	8.925	-21.430	-21.430	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.951	-0.962	11.347	-14.556	-14.556	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.024	0.003	10.302	-0.432	-0.432	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.874	0.928	11.278	20.700	20.700	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.066	-0.034	9.533	1.030	1.030	0.000	0.000	0.000	0.000
94	A	95	GLN	0	0.007	0.001	10.846	-0.808	-0.808	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.024	-0.007	6.117	0.227	0.227	0.000	0.000	0.000	0.000
96	A	97	PRO	0	-0.038	-0.021	10.284	0.690	0.690	0.000	0.000	0.000	0.000
97	A	98	ARG	0	0.067	0.046	10.491	-5.513	-5.513	0.000	0.000	0.000	0.000

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