FMO DATABASE

FMODB ID: 25J9R

Calculation Name: 3K1H-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3K1H

Chain ID: A

ChEMBL ID:

UniProt ID: O25709

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-921899.396775
FMO2-HF: Nuclear repulsion	875848.090492
FMO2-HF: Total energy	-46051.306283
FMO2-MP2: Total energy	-46184.128106

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:33:PHE)

Summations of interaction energy for fragment #1(A:33:PHE)

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.
-217.306	-206.081	17.324	-10.234	-18.317	-0.114

Interaction energy analysis for fragmet #1(A:33:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.799 / q_NPA : 0.899

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	35	ARG	1	0.801	0.904	2.431	34.990	37.492	7.753	-2.547	-7.708	-0.013
4	A	36	ASP	-1	-0.824	-0.895	4.225	-31.451	-31.303	0.000	-0.041	-0.108	0.000
59	A	91	SER	0	0.034	0.023	2.568	-4.929	-3.859	0.905	-0.642	-1.334	-0.010
60	A	92	PRO	0	0.007	0.003	2.554	2.288	3.335	0.324	-0.263	-1.108	0.000
61	A	93	LEU	0	-0.016	-0.013	4.130	-2.755	-2.481	-0.001	-0.064	-0.210	0.000
63	A	95	ASP	-1	-0.836	-0.898	4.182	-49.582	-49.124	-0.001	-0.132	-0.325	0.000
64	A	96	THR	0	-0.085	-0.071	1.978	-54.617	-49.789	8.328	-6.377	-6.778	-0.090
65	A	97	GLN	0	-0.035	-0.017	3.476	9.842	10.529	0.017	-0.114	-0.590	-0.001
66	A	98	LEU	0	-0.013	-0.018	4.184	-4.434	-4.223	-0.001	-0.054	-0.156	0.000
5	A	37	MET	0	-0.079	-0.028	7.076	0.935	0.935	0.000	0.000	0.000	0.000
6	A	38	LYS	1	0.863	0.921	10.454	19.667	19.667	0.000	0.000	0.000	0.000
7	A	39	ASN	0	0.003	-0.015	13.383	0.853	0.853	0.000	0.000	0.000	0.000
8	A	40	ILE	0	0.128	0.076	14.886	-1.219	-1.219	0.000	0.000	0.000	0.000
9	A	41	ASN	0	-0.005	-0.001	16.879	-0.116	-0.116	0.000	0.000	0.000	0.000
10	A	42	GLU	-1	-0.860	-0.923	11.249	-21.298	-21.298	0.000	0.000	0.000	0.000
11	A	43	SER	0	0.013	-0.001	12.278	-1.549	-1.549	0.000	0.000	0.000	0.000
12	A	44	VAL	0	0.048	0.026	13.326	-0.628	-0.628	0.000	0.000	0.000	0.000
13	A	45	GLY	0	-0.021	-0.010	14.192	0.115	0.115	0.000	0.000	0.000	0.000
14	A	46	ALA	0	0.000	-0.007	9.402	-0.186	-0.186	0.000	0.000	0.000	0.000
15	A	47	LEU	0	0.043	0.019	11.119	-0.680	-0.680	0.000	0.000	0.000	0.000
16	A	48	GLN	0	0.020	0.018	13.425	0.540	0.540	0.000	0.000	0.000	0.000
17	A	49	VAL	0	-0.018	-0.014	11.902	0.650	0.650	0.000	0.000	0.000	0.000
18	A	50	LEU	0	0.043	0.026	9.473	0.491	0.491	0.000	0.000	0.000	0.000
19	A	51	GLN	0	0.017	0.010	12.666	0.996	0.996	0.000	0.000	0.000	0.000
20	A	52	ILE	0	-0.056	-0.035	16.384	0.904	0.904	0.000	0.000	0.000	0.000
21	A	53	ALA	0	-0.007	-0.005	13.596	0.794	0.794	0.000	0.000	0.000	0.000
22	A	54	CYS	0	0.024	0.005	13.823	0.367	0.367	0.000	0.000	0.000	0.000
23	A	55	LYS	1	0.953	0.983	16.506	15.289	15.289	0.000	0.000	0.000	0.000
24	A	56	LYS	1	0.889	0.952	18.229	16.291	16.291	0.000	0.000	0.000	0.000
25	A	57	LEU	0	0.003	0.005	14.616	0.690	0.690	0.000	0.000	0.000	0.000
26	A	58	PHE	0	0.031	0.027	19.258	0.630	0.630	0.000	0.000	0.000	0.000
27	A	59	ASN	0	0.005	-0.010	21.473	0.633	0.633	0.000	0.000	0.000	0.000
28	A	60	LYS	1	0.795	0.896	21.884	13.623	13.623	0.000	0.000	0.000	0.000
29	A	61	SER	0	-0.029	-0.019	21.926	0.324	0.324	0.000	0.000	0.000	0.000
30	A	62	MET	0	0.006	0.012	24.018	0.285	0.285	0.000	0.000	0.000	0.000
31	A	63	GLY	0	0.033	0.014	27.320	0.230	0.230	0.000	0.000	0.000	0.000
32	A	64	LEU	0	-0.094	-0.043	24.075	0.187	0.187	0.000	0.000	0.000	0.000
33	A	65	GLU	-1	-0.865	-0.948	28.104	-10.921	-10.921	0.000	0.000	0.000	0.000
34	A	66	ASP	-1	-0.921	-0.948	30.013	-9.081	-9.081	0.000	0.000	0.000	0.000
35	A	67	LYS	1	0.807	0.926	29.017	11.037	11.037	0.000	0.000	0.000	0.000
36	A	68	ASP	-1	-0.808	-0.905	32.091	-9.485	-9.485	0.000	0.000	0.000	0.000
37	A	69	ALA	0	0.032	-0.004	31.290	-0.303	-0.303	0.000	0.000	0.000	0.000
38	A	70	LEU	0	-0.033	0.008	30.496	-0.318	-0.318	0.000	0.000	0.000	0.000
39	A	71	GLN	0	0.022	0.001	30.142	-0.604	-0.604	0.000	0.000	0.000	0.000
40	A	72	ALA	0	0.040	0.016	27.858	-0.440	-0.440	0.000	0.000	0.000	0.000
41	A	73	SER	0	-0.091	-0.051	26.160	-0.546	-0.546	0.000	0.000	0.000	0.000
42	A	74	ILE	0	0.013	0.000	25.357	-0.514	-0.514	0.000	0.000	0.000	0.000
43	A	75	ILE	0	0.037	0.019	24.084	-0.507	-0.507	0.000	0.000	0.000	0.000
44	A	76	LYS	1	0.955	0.975	21.926	12.427	12.427	0.000	0.000	0.000	0.000
45	A	77	GLN	0	-0.026	-0.018	20.406	-1.057	-1.057	0.000	0.000	0.000	0.000
46	A	78	GLU	-1	-0.848	-0.918	20.438	-13.202	-13.202	0.000	0.000	0.000	0.000
47	A	79	LEU	0	-0.040	-0.021	18.674	-0.786	-0.786	0.000	0.000	0.000	0.000
48	A	80	ARG	1	0.821	0.895	16.277	16.545	16.545	0.000	0.000	0.000	0.000
49	A	81	GLU	-1	-0.848	-0.906	15.597	-15.956	-15.956	0.000	0.000	0.000	0.000
50	A	82	ILE	0	-0.082	-0.044	15.633	-0.471	-0.471	0.000	0.000	0.000	0.000
51	A	83	VAL	0	0.001	0.000	10.810	-1.084	-1.084	0.000	0.000	0.000	0.000
52	A	84	GLU	-1	-0.863	-0.922	11.075	-21.505	-21.505	0.000	0.000	0.000	0.000
53	A	85	ASN	0	-0.065	-0.027	11.480	-0.752	-0.752	0.000	0.000	0.000	0.000
54	A	86	CYS	0	-0.076	-0.015	10.026	0.480	0.480	0.000	0.000	0.000	0.000
55	A	87	GLN	0	-0.015	-0.013	7.780	-2.902	-2.902	0.000	0.000	0.000	0.000
56	A	88	PHE	0	0.036	0.014	7.701	2.748	2.748	0.000	0.000	0.000	0.000
57	A	89	LEU	0	-0.014	-0.011	7.316	-2.150	-2.150	0.000	0.000	0.000	0.000
58	A	90	ALA	0	0.003	0.007	6.945	-1.334	-1.334	0.000	0.000	0.000	0.000
62	A	94	PHE	0	0.087	0.047	6.346	0.534	0.534	0.000	0.000	0.000	0.000
67	A	99	ASN	0	0.004	0.015	6.565	3.779	3.779	0.000	0.000	0.000	0.000
68	A	100	ILE	0	0.021	-0.006	9.038	0.230	0.230	0.000	0.000	0.000	0.000
69	A	101	ALA	0	0.006	0.013	12.206	0.589	0.589	0.000	0.000	0.000	0.000
70	A	102	ILE	0	-0.023	-0.023	15.489	0.280	0.280	0.000	0.000	0.000	0.000
71	A	103	ASN	0	0.001	0.000	18.724	0.096	0.096	0.000	0.000	0.000	0.000
72	A	104	ASP	-1	-0.939	-0.963	20.848	-12.522	-12.522	0.000	0.000	0.000	0.000
73	A	105	GLU	-1	-0.956	-0.955	19.047	-14.278	-14.278	0.000	0.000	0.000	0.000
74	A	106	ILE	0	-0.064	-0.049	12.475	-0.609	-0.609	0.000	0.000	0.000	0.000
75	A	107	PHE	0	0.039	0.025	14.178	-0.265	-0.265	0.000	0.000	0.000	0.000
76	A	108	SER	0	-0.024	-0.035	9.984	-0.865	-0.865	0.000	0.000	0.000	0.000
77	A	109	MET	0	-0.012	0.021	9.803	1.482	1.482	0.000	0.000	0.000	0.000
78	A	110	ILE	0	-0.017	-0.022	5.645	-4.266	-4.266	0.000	0.000	0.000	0.000
79	A	111	VAL	0	-0.008	0.006	8.024	3.683	3.683	0.000	0.000	0.000	0.000
80	A	112	VAL	0	0.013	-0.001	7.528	-4.848	-4.848	0.000	0.000	0.000	0.000
81	A	113	ASN	0	0.045	-0.002	8.294	4.714	4.714	0.000	0.000	0.000	0.000
82	A	114	PRO	0	0.026	0.015	10.125	0.947	0.947	0.000	0.000	0.000	0.000
83	A	115	LEU	0	-0.047	-0.029	13.583	1.810	1.810	0.000	0.000	0.000	0.000
84	A	116	ASP	-1	-0.911	-0.949	13.371	-20.909	-20.909	0.000	0.000	0.000	0.000
85	A	117	LEU	0	0.006	0.002	15.791	0.995	0.995	0.000	0.000	0.000	0.000
86	A	118	LEU	0	-0.097	-0.041	18.295	1.084	1.084	0.000	0.000	0.000	0.000
87	A	119	GLU	-1	-1.023	-1.002	20.353	-11.947	-11.947	0.000	0.000	0.000	0.000
88	A	120	ASN	0	0.013	-0.001	22.232	0.938	0.938	0.000	0.000	0.000	0.000
89	A	121	VAL	0	0.026	-0.001	22.640	-0.540	-0.540	0.000	0.000	0.000	0.000
90	A	122	GLY	0	0.048	0.029	23.427	-0.240	-0.240	0.000	0.000	0.000	0.000
91	A	123	GLU	-1	-0.890	-0.939	20.476	-14.288	-14.288	0.000	0.000	0.000	0.000
92	A	124	PHE	0	-0.034	-0.026	16.959	-0.840	-0.840	0.000	0.000	0.000	0.000
93	A	125	GLN	0	-0.035	-0.025	19.054	-0.438	-0.438	0.000	0.000	0.000	0.000
94	A	126	ALA	0	0.050	0.023	20.952	-0.321	-0.321	0.000	0.000	0.000	0.000
95	A	127	TYR	0	0.053	0.032	11.612	-1.313	-1.313	0.000	0.000	0.000	0.000
96	A	128	LEU	0	-0.025	-0.020	15.402	-0.994	-0.994	0.000	0.000	0.000	0.000
97	A	129	GLU	-1	-0.961	-0.979	17.673	-13.091	-13.091	0.000	0.000	0.000	0.000
98	A	130	GLU	-1	-0.945	-0.974	17.987	-16.532	-16.532	0.000	0.000	0.000	0.000
99	A	131	LYS	1	0.804	0.884	12.287	22.856	22.856	0.000	0.000	0.000	0.000
100	A	132	LEU	0	-0.036	-0.023	15.988	-0.297	-0.297	0.000	0.000	0.000	0.000
101	A	133	ASN	0	-0.050	-0.021	18.391	0.803	0.803	0.000	0.000	0.000	0.000
102	A	134	GLU	-1	-0.794	-0.880	14.540	-21.273	-21.273	0.000	0.000	0.000	0.000
103	A	135	ILE	0	-0.004	-0.018	13.263	-0.038	-0.038	0.000	0.000	0.000	0.000
104	A	136	LYS	1	0.922	0.967	16.155	13.016	13.016	0.000	0.000	0.000	0.000
105	A	137	GLU	-1	-0.882	-0.925	19.427	-12.936	-12.936	0.000	0.000	0.000	0.000
106	A	138	LEU	0	0.007	0.009	13.599	0.176	0.176	0.000	0.000	0.000	0.000
107	A	139	LEU	0	-0.034	-0.027	16.967	0.321	0.321	0.000	0.000	0.000	0.000
108	A	140	GLY	0	-0.001	0.025	18.975	0.641	0.641	0.000	0.000	0.000	0.000
109	A	141	TYR	0	0.023	-0.010	19.517	0.186	0.186	0.000	0.000	0.000	0.000
110	A	142	LEU	0	-0.026	-0.016	15.485	0.153	0.153	0.000	0.000	0.000	0.000
111	A	143	SER	0	-0.052	-0.049	20.159	0.414	0.414	0.000	0.000	0.000	0.000
112	A	144	GLU	-1	-0.959	-0.975	23.357	-11.191	-11.191	0.000	0.000	0.000	0.000
113	A	145	SER	0	-0.042	-0.023	21.712	0.284	0.284	0.000	0.000	0.000	0.000
114	A	146	LEU	0	-0.129	-0.065	21.330	-0.053	-0.053	0.000	0.000	0.000	0.000
115	A	147	SER	-1	-1.004	-0.975	24.788	-9.912	-9.912	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:33:PHE)