FMO DATABASE

FMODB ID: 74Q7K

Calculation Name: 1CMI-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1CMI

Chain ID: A

ChEMBL ID:

UniProt ID: P63167

Base Structure: X-ray

Registration Date: 2025-10-11

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	85
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-615683.051161
FMO2-HF: Nuclear repulsion	580847.301921
FMO2-HF: Total energy	-34835.749241
FMO2-MP2: Total energy	-34936.416389

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:5:LYS)

Summations of interaction energy for fragment #1(A:5:LYS)

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.
-25.936	-23.401	0	-0.897	-1.64	-0.001

Interaction energy analysis for fragmet #1(A:5:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.829 / q_NPA : 1.895

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

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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	7	VAL	0	-0.034	-0.023	3.755	-1.828	-0.258	-0.010	-0.605	-0.956	0.000
74	A	78	LEU	0	0.028	0.008	3.304	-14.201	-13.752	0.012	-0.182	-0.280	-0.001
75	A	79	GLY	0	0.016	0.022	3.764	9.534	9.853	-0.001	-0.042	-0.276	0.000
76	A	80	GLN	0	-0.033	-0.018	4.143	-13.893	-13.696	-0.001	-0.068	-0.128	0.000
4	A	8	ILE	0	0.055	0.027	6.167	3.448	3.448	0.000	0.000	0.000	0.000
5	A	9	LYS	1	0.855	0.945	8.828	59.131	59.131	0.000	0.000	0.000	0.000
6	A	10	ASN	0	-0.011	-0.014	12.312	3.395	3.395	0.000	0.000	0.000	0.000
7	A	11	ALA	0	0.014	0.007	14.159	-1.530	-1.530	0.000	0.000	0.000	0.000
8	A	12	ASP	-1	-0.823	-0.898	16.231	-25.857	-25.857	0.000	0.000	0.000	0.000
9	A	13	MET	0	-0.071	-0.012	15.994	0.732	0.732	0.000	0.000	0.000	0.000
10	A	14	SER	0	0.047	0.016	17.515	-1.464	-1.464	0.000	0.000	0.000	0.000
11	A	15	GLU	-1	-0.892	-0.957	15.122	-33.347	-33.347	0.000	0.000	0.000	0.000
12	A	16	GLU	-1	-0.904	-0.945	14.373	-30.462	-30.462	0.000	0.000	0.000	0.000
13	A	17	MET	0	0.005	0.018	15.133	-1.332	-1.332	0.000	0.000	0.000	0.000
14	A	18	GLN	0	-0.018	-0.016	11.739	-4.011	-4.011	0.000	0.000	0.000	0.000
15	A	19	GLN	0	0.020	0.010	10.369	-3.921	-3.921	0.000	0.000	0.000	0.000
16	A	20	ASP	-1	-0.738	-0.830	10.588	-36.934	-36.934	0.000	0.000	0.000	0.000
17	A	21	SER	0	-0.049	-0.039	12.078	-0.069	-0.069	0.000	0.000	0.000	0.000
18	A	22	VAL	0	-0.029	-0.020	5.701	-3.319	-3.319	0.000	0.000	0.000	0.000
19	A	23	GLU	-1	-0.934	-0.945	7.894	-45.688	-45.688	0.000	0.000	0.000	0.000
20	A	24	CYS	0	-0.006	0.009	9.587	0.143	0.143	0.000	0.000	0.000	0.000
21	A	25	ALA	0	0.015	-0.008	9.099	0.794	0.794	0.000	0.000	0.000	0.000
22	A	26	THR	0	-0.087	-0.051	6.131	-6.426	-6.426	0.000	0.000	0.000	0.000
23	A	27	GLN	0	0.056	0.025	8.116	2.824	2.824	0.000	0.000	0.000	0.000
24	A	28	ALA	0	-0.050	-0.015	11.643	2.609	2.609	0.000	0.000	0.000	0.000
25	A	29	LEU	0	-0.034	-0.033	7.208	1.451	1.451	0.000	0.000	0.000	0.000
26	A	30	GLU	-1	-0.951	-0.970	9.245	-51.339	-51.339	0.000	0.000	0.000	0.000
27	A	31	LYS	1	0.879	0.961	11.554	33.181	33.181	0.000	0.000	0.000	0.000
28	A	32	TYR	0	-0.032	-0.023	14.380	3.429	3.429	0.000	0.000	0.000	0.000
29	A	33	ASN	0	0.024	0.005	14.434	-3.654	-3.654	0.000	0.000	0.000	0.000
30	A	34	ILE	0	0.001	0.012	16.307	-0.105	-0.105	0.000	0.000	0.000	0.000
31	A	35	GLU	-1	-0.851	-0.935	14.883	-37.390	-37.390	0.000	0.000	0.000	0.000
32	A	36	LYS	1	0.865	0.926	16.651	26.209	26.209	0.000	0.000	0.000	0.000
33	A	37	ASP	-1	-0.828	-0.915	18.957	-27.246	-27.246	0.000	0.000	0.000	0.000
34	A	38	ILE	0	0.003	0.008	12.368	0.131	0.131	0.000	0.000	0.000	0.000
35	A	39	ALA	0	0.007	-0.006	15.790	-0.211	-0.211	0.000	0.000	0.000	0.000
36	A	40	ALA	0	-0.043	-0.019	17.504	1.017	1.017	0.000	0.000	0.000	0.000
37	A	41	HIS	0	0.010	0.002	15.391	2.120	2.120	0.000	0.000	0.000	0.000
38	A	42	ILE	0	0.057	0.008	12.629	0.680	0.680	0.000	0.000	0.000	0.000
39	A	43	LYS	1	0.777	0.865	16.533	25.663	25.663	0.000	0.000	0.000	0.000
40	A	44	LYS	1	0.946	0.964	20.021	26.365	26.365	0.000	0.000	0.000	0.000
41	A	45	GLU	-1	-0.836	-0.892	17.197	-27.750	-27.750	0.000	0.000	0.000	0.000
42	A	46	PHE	0	-0.002	-0.009	14.973	0.734	0.734	0.000	0.000	0.000	0.000
43	A	47	ASP	-1	-0.776	-0.882	20.035	-23.567	-23.567	0.000	0.000	0.000	0.000
44	A	48	LYS	1	0.772	0.873	21.939	27.165	27.165	0.000	0.000	0.000	0.000
45	A	49	LYS	1	0.857	0.918	17.121	32.185	32.185	0.000	0.000	0.000	0.000
46	A	50	TYR	0	-0.025	-0.052	17.969	0.786	0.786	0.000	0.000	0.000	0.000
47	A	51	ASN	0	0.004	0.009	23.308	0.430	0.430	0.000	0.000	0.000	0.000
48	A	52	PRO	0	-0.005	0.008	25.443	-0.729	-0.729	0.000	0.000	0.000	0.000
49	A	53	THR	0	-0.076	-0.050	26.695	0.404	0.404	0.000	0.000	0.000	0.000
50	A	54	TRP	0	-0.027	-0.017	19.293	-1.020	-1.020	0.000	0.000	0.000	0.000
51	A	55	HIS	0	-0.021	0.000	21.989	0.334	0.334	0.000	0.000	0.000	0.000
52	A	56	CYS	0	-0.070	-0.041	16.457	-1.825	-1.825	0.000	0.000	0.000	0.000
53	A	57	ILE	0	-0.005	0.009	17.757	1.426	1.426	0.000	0.000	0.000	0.000
54	A	58	VAL	0	0.016	0.006	12.960	-2.373	-2.373	0.000	0.000	0.000	0.000
55	A	59	GLY	0	0.055	0.029	14.104	2.657	2.657	0.000	0.000	0.000	0.000
56	A	60	ARG	1	0.907	0.925	8.947	47.521	47.521	0.000	0.000	0.000	0.000
57	A	61	ASN	0	-0.057	-0.027	13.491	0.623	0.623	0.000	0.000	0.000	0.000
58	A	62	PHE	0	0.031	0.024	15.251	1.264	1.264	0.000	0.000	0.000	0.000
59	A	63	GLY	0	0.029	0.022	18.708	-1.045	-1.045	0.000	0.000	0.000	0.000
60	A	64	SER	0	-0.041	-0.025	20.779	0.599	0.599	0.000	0.000	0.000	0.000
61	A	65	TYR	0	0.020	0.010	22.944	-0.278	-0.278	0.000	0.000	0.000	0.000
62	A	66	VAL	0	-0.011	0.001	22.899	0.579	0.579	0.000	0.000	0.000	0.000
63	A	67	THR	0	0.018	0.015	26.096	0.029	0.029	0.000	0.000	0.000	0.000
64	A	68	HIS	1	0.827	0.900	23.505	26.029	26.029	0.000	0.000	0.000	0.000
65	A	69	GLU	-1	-0.845	-0.925	25.429	-22.070	-22.070	0.000	0.000	0.000	0.000
66	A	70	THR	0	-0.004	0.012	24.338	-1.160	-1.160	0.000	0.000	0.000	0.000
67	A	71	LYS	1	0.937	0.956	22.130	23.439	23.439	0.000	0.000	0.000	0.000
68	A	72	HIS	1	0.876	0.939	20.737	24.393	24.393	0.000	0.000	0.000	0.000
69	A	73	PHE	0	0.036	0.010	18.484	0.362	0.362	0.000	0.000	0.000	0.000
70	A	74	ILE	0	0.026	0.010	11.773	-0.645	-0.645	0.000	0.000	0.000	0.000
71	A	75	TYR	0	0.027	0.014	13.040	-0.512	-0.512	0.000	0.000	0.000	0.000
72	A	76	PHE	0	0.010	0.001	7.870	-1.393	-1.393	0.000	0.000	0.000	0.000
73	A	77	TYR	0	0.004	-0.002	6.423	2.194	2.194	0.000	0.000	0.000	0.000
77	A	81	VAL	0	0.014	0.022	6.512	8.522	8.522	0.000	0.000	0.000	0.000
78	A	82	ALA	0	-0.011	-0.004	8.679	-6.398	-6.398	0.000	0.000	0.000	0.000
79	A	83	ILE	0	0.032	0.004	9.685	3.235	3.235	0.000	0.000	0.000	0.000
80	A	84	LEU	0	-0.006	0.003	12.931	-1.012	-1.012	0.000	0.000	0.000	0.000
81	A	85	LEU	0	-0.001	0.007	15.235	0.904	0.904	0.000	0.000	0.000	0.000
82	A	86	PHE	0	-0.014	-0.020	17.292	-0.340	-0.340	0.000	0.000	0.000	0.000
83	A	87	LYS	1	0.864	0.954	20.573	23.035	23.035	0.000	0.000	0.000	0.000
84	A	88	SER	0	-0.037	-0.039	23.746	-0.051	-0.051	0.000	0.000	0.000	0.000
85	A	89	GLY	-1	-0.723	-0.816	27.303	-21.246	-21.246	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LYS)