FMO DATABASE

FMODB ID: 5R13Z

Calculation Name: 1W2I-A-Xray547

Preferred Name:

Target Type:

Ligand Name: formic acid

Ligand 3-letter code: FMT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1W2I

Chain ID: A

ChEMBL ID:

UniProt ID: P84142

Base Structure: X-ray

Registration Date: 2025-10-03

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-651212.401176
FMO2-HF: Nuclear repulsion	616421.50244
FMO2-HF: Total energy	-34790.898736
FMO2-MP2: Total energy	-34894.928343

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:ALA)

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

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.
-103.115	-96.421	17.643	-14.057	-10.278	-0.161

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.783 / q_NPA : 0.885

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	VAL	0	0.026	0.019	3.517	4.958	6.215	-0.003	-0.478	-0.776	0.001
50	A	51	ASP	-1	-0.858	-0.933	2.594	-86.319	-82.324	0.311	-2.410	-1.896	-0.030
51	A	52	GLU	-1	-0.821	-0.911	1.748	-115.682	-114.420	17.336	-11.159	-7.438	-0.132
52	A	53	GLU	-1	-0.864	-0.925	4.562	-27.663	-27.483	-0.001	-0.010	-0.168	0.000
4	A	5	ARG	1	0.774	0.858	6.137	23.648	23.648	0.000	0.000	0.000	0.000
5	A	6	ALA	0	0.024	0.027	9.916	0.626	0.626	0.000	0.000	0.000	0.000
6	A	7	HIS	1	0.716	0.819	12.035	17.786	17.786	0.000	0.000	0.000	0.000
7	A	8	LEU	0	0.010	0.001	14.659	0.293	0.293	0.000	0.000	0.000	0.000
8	A	9	LYS	1	0.820	0.903	18.105	12.969	12.969	0.000	0.000	0.000	0.000
9	A	10	ILE	0	0.031	0.021	20.090	-0.301	-0.301	0.000	0.000	0.000	0.000
10	A	11	TYR	0	0.012	-0.026	23.280	0.779	0.779	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.059	0.037	26.819	-0.155	-0.155	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.877	0.956	29.816	9.603	9.603	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.038	0.015	26.213	-0.082	-0.082	0.000	0.000	0.000	0.000
14	A	15	GLN	0	-0.038	-0.027	28.389	0.070	0.070	0.000	0.000	0.000	0.000
15	A	16	GLY	0	-0.012	-0.017	31.013	0.214	0.214	0.000	0.000	0.000	0.000
16	A	17	VAL	0	-0.019	-0.004	28.672	0.186	0.186	0.000	0.000	0.000	0.000
17	A	18	GLY	0	0.021	0.012	29.164	-0.174	-0.174	0.000	0.000	0.000	0.000
18	A	19	PHE	0	0.035	0.028	21.713	-0.261	-0.261	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.875	0.925	23.957	10.575	10.575	0.000	0.000	0.000	0.000
20	A	21	TRP	0	0.059	0.011	23.596	-0.638	-0.638	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.070	-0.044	23.879	-0.238	-0.238	0.000	0.000	0.000	0.000
22	A	23	MET	0	0.062	0.041	18.600	-0.567	-0.567	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.029	-0.009	18.963	-0.412	-0.412	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.929	0.966	19.797	12.348	12.348	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.809	-0.897	17.597	-16.456	-16.456	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.019	0.014	14.895	-1.122	-1.122	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.866	0.932	14.540	13.679	13.679	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.856	0.927	16.006	16.164	16.164	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.002	0.004	11.847	-0.431	-0.431	0.000	0.000	0.000	0.000
30	A	31	GLY	0	-0.001	0.016	10.949	-2.611	-2.611	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.058	-0.014	9.970	-1.611	-1.611	0.000	0.000	0.000	0.000
32	A	33	ASN	0	-0.008	-0.011	11.422	4.118	4.118	0.000	0.000	0.000	0.000
33	A	34	GLY	0	0.038	0.009	13.961	-0.956	-0.956	0.000	0.000	0.000	0.000
34	A	35	TRP	0	-0.102	-0.049	16.443	1.264	1.264	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.011	0.015	19.381	-0.439	-0.439	0.000	0.000	0.000	0.000
36	A	37	ARG	1	0.843	0.900	21.940	13.306	13.306	0.000	0.000	0.000	0.000
37	A	38	ASN	0	0.004	-0.006	25.429	-0.580	-0.580	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.005	0.011	25.572	-0.016	-0.016	0.000	0.000	0.000	0.000
39	A	40	PRO	0	0.027	0.009	29.366	0.148	0.148	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.755	-0.832	28.825	-10.939	-10.939	0.000	0.000	0.000	0.000
41	A	42	GLY	0	0.002	0.010	31.803	0.049	0.049	0.000	0.000	0.000	0.000
42	A	43	SER	0	-0.095	-0.074	26.263	-0.348	-0.348	0.000	0.000	0.000	0.000
43	A	44	VAL	0	-0.009	-0.010	23.006	0.213	0.213	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.747	-0.836	21.293	-14.128	-14.128	0.000	0.000	0.000	0.000
45	A	46	ALA	0	-0.025	-0.027	18.546	0.234	0.234	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.030	0.004	14.853	-0.357	-0.357	0.000	0.000	0.000	0.000
47	A	48	LEU	0	0.019	0.005	12.441	0.692	0.692	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.730	-0.852	10.021	-26.160	-26.160	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.036	0.014	7.747	3.301	3.301	0.000	0.000	0.000	0.000
53	A	54	ARG	1	0.881	0.928	6.683	37.193	37.193	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.018	-0.012	7.727	4.993	4.993	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.911	-0.961	8.184	-31.603	-31.603	0.000	0.000	0.000	0.000
56	A	57	ALA	0	0.002	0.009	10.291	3.207	3.207	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.042	-0.018	12.162	2.489	2.489	0.000	0.000	0.000	0.000
58	A	59	ILE	0	0.011	-0.006	11.481	2.054	2.054	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.022	0.025	14.292	1.509	1.509	0.000	0.000	0.000	0.000
60	A	61	TRP	0	0.005	0.002	16.199	1.302	1.302	0.000	0.000	0.000	0.000
61	A	62	ALA	0	-0.017	-0.014	17.593	1.209	1.209	0.000	0.000	0.000	0.000
62	A	63	HIS	0	-0.029	-0.037	17.507	1.110	1.110	0.000	0.000	0.000	0.000
63	A	64	GLN	0	-0.045	-0.007	21.086	0.993	0.993	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.023	0.002	22.239	0.587	0.587	0.000	0.000	0.000	0.000
65	A	66	PRO	0	-0.078	-0.034	23.754	0.013	0.013	0.000	0.000	0.000	0.000
66	A	67	PRO	0	0.055	0.003	26.512	0.183	0.183	0.000	0.000	0.000	0.000
67	A	68	LEU	0	0.006	0.014	29.341	0.244	0.244	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.051	-0.020	27.246	0.287	0.287	0.000	0.000	0.000	0.000
69	A	70	ARG	1	0.944	0.967	29.151	9.506	9.506	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.019	0.022	23.165	0.302	0.302	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.062	-0.042	26.610	0.246	0.246	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.881	0.921	23.808	11.958	11.958	0.000	0.000	0.000	0.000
73	A	74	VAL	0	0.005	0.003	18.213	0.210	0.210	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.786	-0.839	19.802	-13.006	-13.006	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.015	-0.004	13.025	-0.058	-0.058	0.000	0.000	0.000	0.000
76	A	77	LYS	1	0.949	0.987	15.453	16.561	16.561	0.000	0.000	0.000	0.000
77	A	78	TRP	0	0.072	0.025	8.157	-0.995	-0.995	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.873	-0.932	11.017	-16.719	-16.719	0.000	0.000	0.000	0.000
79	A	80	GLN	0	0.036	0.017	9.730	-1.562	-1.562	0.000	0.000	0.000	0.000
80	A	81	PRO	0	-0.025	-0.023	6.781	1.982	1.982	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.921	0.951	10.077	18.542	18.542	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.018	0.025	12.626	1.180	1.180	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.841	-0.918	13.775	-16.366	-16.366	0.000	0.000	0.000	0.000
84	A	85	LYS	1	0.962	0.978	14.525	14.435	14.435	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.015	0.010	16.017	1.233	1.233	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.023	0.008	15.634	0.087	0.087	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.891	0.940	18.300	16.255	16.255	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.008	-0.003	21.761	-0.362	-0.362	0.000	0.000	0.000	0.000
89	A	90	VAL	0	-0.048	-0.033	23.334	0.243	0.243	0.000	0.000	0.000	0.000
90	A	91	GLY	-1	-0.774	-0.846	26.052	-11.134	-11.134	0.000	0.000	0.000	0.000

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