FMO DATABASE

FMODB ID: VN851

Calculation Name: 2MAH-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2MAH

Chain ID: A

ChEMBL ID:

UniProt ID: P91682

Base Structure: SolutionNMR

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	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1141616.402291
FMO2-HF: Nuclear repulsion	1087518.000126
FMO2-HF: Total energy	-54098.402165
FMO2-MP2: Total energy	-54248.583817

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:12:SER)

Summations of interaction energy for fragment #1(A:12: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.
41.272	44.866	-0.027	-1.816	-1.748	-0.008

Interaction energy analysis for fragmet #1(A:12:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.852 / q_NPA : 0.905

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	14	LEU	0	0.011	0.014	3.710	6.988	10.456	-0.026	-1.799	-1.642	-0.008
13	A	24	ARG	1	0.841	0.915	4.361	43.545	43.671	-0.001	-0.017	-0.106	0.000
4	A	15	VAL	0	0.024	0.020	5.219	-3.284	-3.284	0.000	0.000	0.000	0.000
5	A	16	PRO	0	-0.015	-0.005	7.289	1.261	1.261	0.000	0.000	0.000	0.000
6	A	17	ARG	1	0.944	0.966	9.588	21.828	21.828	0.000	0.000	0.000	0.000
7	A	18	GLY	0	0.034	0.026	12.669	-0.803	-0.803	0.000	0.000	0.000	0.000
8	A	19	SER	0	0.041	-0.003	15.490	0.410	0.410	0.000	0.000	0.000	0.000
9	A	20	HIS	0	-0.007	0.010	14.397	-0.847	-0.847	0.000	0.000	0.000	0.000
10	A	21	MET	0	-0.044	-0.004	14.766	0.854	0.854	0.000	0.000	0.000	0.000
11	A	22	VAL	0	0.018	-0.009	11.870	0.405	0.405	0.000	0.000	0.000	0.000
12	A	23	ARG	1	0.857	0.943	8.550	25.069	25.069	0.000	0.000	0.000	0.000
14	A	25	ALA	0	0.027	0.030	6.897	-5.043	-5.043	0.000	0.000	0.000	0.000
15	A	26	ARG	1	0.972	0.971	9.665	26.618	26.618	0.000	0.000	0.000	0.000
16	A	27	CYS	0	-0.016	0.012	11.647	0.176	0.176	0.000	0.000	0.000	0.000
17	A	28	TYR	0	-0.003	0.004	14.663	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	29	PRO	0	0.039	0.020	17.730	0.273	0.273	0.000	0.000	0.000	0.000
19	A	30	THR	0	-0.019	-0.017	21.252	0.126	0.126	0.000	0.000	0.000	0.000
20	A	31	SER	0	-0.019	-0.032	23.827	0.610	0.610	0.000	0.000	0.000	0.000
21	A	32	ASN	0	-0.029	-0.015	26.422	-0.199	-0.199	0.000	0.000	0.000	0.000
22	A	33	ALA	0	0.024	0.025	28.087	0.172	0.172	0.000	0.000	0.000	0.000
23	A	34	THR	0	0.024	-0.013	26.317	-0.333	-0.333	0.000	0.000	0.000	0.000
24	A	35	ASN	0	-0.007	0.007	25.813	0.385	0.385	0.000	0.000	0.000	0.000
25	A	36	THR	0	0.002	-0.016	27.721	0.275	0.275	0.000	0.000	0.000	0.000
26	A	37	CYS	0	-0.068	-0.031	26.940	-0.247	-0.247	0.000	0.000	0.000	0.000
27	A	38	PHE	0	0.022	-0.001	31.023	0.147	0.147	0.000	0.000	0.000	0.000
28	A	39	GLY	0	0.030	0.029	34.608	0.217	0.217	0.000	0.000	0.000	0.000
29	A	40	SER	0	0.027	0.012	33.026	0.120	0.120	0.000	0.000	0.000	0.000
30	A	41	LYS	1	0.946	0.975	30.899	9.584	9.584	0.000	0.000	0.000	0.000
31	A	42	LEU	0	0.021	0.026	25.832	0.085	0.085	0.000	0.000	0.000	0.000
32	A	43	PRO	0	-0.036	-0.003	25.275	0.057	0.057	0.000	0.000	0.000	0.000
33	A	44	TYR	0	-0.011	-0.034	21.405	-0.193	-0.193	0.000	0.000	0.000	0.000
34	A	45	GLU	-1	-0.897	-0.948	22.147	-13.178	-13.178	0.000	0.000	0.000	0.000
35	A	46	LEU	0	-0.045	0.000	16.820	0.008	0.008	0.000	0.000	0.000	0.000
36	A	47	SER	0	-0.011	0.004	19.303	0.044	0.044	0.000	0.000	0.000	0.000
37	A	48	SER	0	0.015	-0.030	13.575	-1.059	-1.059	0.000	0.000	0.000	0.000
38	A	49	LEU	0	-0.019	0.001	15.925	0.395	0.395	0.000	0.000	0.000	0.000
39	A	50	ASP	-1	-0.835	-0.912	9.885	-29.232	-29.232	0.000	0.000	0.000	0.000
40	A	51	LEU	0	-0.055	-0.024	13.290	-0.639	-0.639	0.000	0.000	0.000	0.000
41	A	52	THR	0	-0.068	-0.050	15.369	1.303	1.303	0.000	0.000	0.000	0.000
42	A	53	ASP	-1	-0.920	-0.960	16.251	-17.880	-17.880	0.000	0.000	0.000	0.000
43	A	54	PHE	0	0.003	-0.009	17.528	1.344	1.344	0.000	0.000	0.000	0.000
44	A	55	HIS	0	0.032	0.011	16.943	-1.418	-1.418	0.000	0.000	0.000	0.000
45	A	56	THR	0	-0.035	-0.026	19.089	0.229	0.229	0.000	0.000	0.000	0.000
46	A	57	GLU	-1	-0.846	-0.937	20.949	-14.027	-14.027	0.000	0.000	0.000	0.000
47	A	58	LYS	1	0.923	0.978	22.848	12.176	12.176	0.000	0.000	0.000	0.000
48	A	59	GLU	-1	-0.789	-0.898	22.240	-13.912	-13.912	0.000	0.000	0.000	0.000
49	A	60	LEU	0	-0.036	-0.004	20.529	0.309	0.309	0.000	0.000	0.000	0.000
50	A	61	ASN	0	-0.039	-0.041	23.904	0.245	0.245	0.000	0.000	0.000	0.000
51	A	62	ASP	-1	-0.881	-0.938	27.382	-10.477	-10.477	0.000	0.000	0.000	0.000
52	A	63	LYS	1	0.822	0.928	25.253	12.179	12.179	0.000	0.000	0.000	0.000
53	A	64	LEU	0	-0.045	-0.030	27.368	0.267	0.267	0.000	0.000	0.000	0.000
54	A	65	ASN	0	0.006	0.000	30.125	0.133	0.133	0.000	0.000	0.000	0.000
55	A	66	ASP	-1	-0.783	-0.874	30.289	-9.814	-9.814	0.000	0.000	0.000	0.000
56	A	67	TYR	0	-0.037	-0.017	30.041	0.246	0.246	0.000	0.000	0.000	0.000
57	A	68	TYR	0	0.048	0.018	32.158	0.463	0.463	0.000	0.000	0.000	0.000
58	A	69	ALA	0	0.016	0.012	35.149	0.272	0.272	0.000	0.000	0.000	0.000
59	A	70	LEU	0	-0.009	-0.009	34.015	0.255	0.255	0.000	0.000	0.000	0.000
60	A	71	LYS	1	0.865	0.937	37.100	8.444	8.444	0.000	0.000	0.000	0.000
61	A	72	HIS	0	0.022	0.019	39.186	0.184	0.184	0.000	0.000	0.000	0.000
62	A	73	VAL	0	-0.028	0.003	38.912	0.194	0.194	0.000	0.000	0.000	0.000
63	A	74	PRO	0	0.055	0.022	39.419	-0.235	-0.235	0.000	0.000	0.000	0.000
64	A	75	LYS	1	0.936	0.959	40.066	7.269	7.269	0.000	0.000	0.000	0.000
65	A	76	CYS	0	-0.007	-0.018	33.890	0.006	0.006	0.000	0.000	0.000	0.000
66	A	77	TRP	0	0.009	0.012	34.981	-0.353	-0.353	0.000	0.000	0.000	0.000
67	A	78	ALA	0	0.009	-0.010	35.489	-0.223	-0.223	0.000	0.000	0.000	0.000
68	A	79	ALA	0	-0.004	0.000	33.863	-0.122	-0.122	0.000	0.000	0.000	0.000
69	A	80	ILE	0	0.021	0.014	28.639	-0.289	-0.289	0.000	0.000	0.000	0.000
70	A	81	GLN	0	-0.046	-0.015	31.003	-0.144	-0.144	0.000	0.000	0.000	0.000
71	A	82	PRO	0	0.004	0.005	30.838	-0.173	-0.173	0.000	0.000	0.000	0.000
72	A	83	PHE	0	-0.003	-0.008	23.442	-0.392	-0.392	0.000	0.000	0.000	0.000
73	A	84	LEU	0	-0.003	-0.007	26.594	-0.489	-0.489	0.000	0.000	0.000	0.000
74	A	86	ALA	0	0.034	0.005	23.149	-0.435	-0.435	0.000	0.000	0.000	0.000
75	A	87	VAL	0	-0.008	0.017	22.081	-0.685	-0.685	0.000	0.000	0.000	0.000
76	A	88	PHE	0	-0.019	-0.028	22.496	-0.158	-0.158	0.000	0.000	0.000	0.000
77	A	89	LYS	1	0.902	0.965	22.184	11.884	11.884	0.000	0.000	0.000	0.000
78	A	90	PRO	0	0.045	0.040	17.879	0.467	0.467	0.000	0.000	0.000	0.000
79	A	91	LYS	1	0.905	0.952	19.877	14.855	14.855	0.000	0.000	0.000	0.000
80	A	93	GLU	-1	-0.778	-0.882	15.552	-15.433	-15.433	0.000	0.000	0.000	0.000
81	A	94	LYS	1	0.866	0.919	12.571	19.364	19.364	0.000	0.000	0.000	0.000
82	A	95	ILE	0	0.016	0.026	13.012	1.090	1.090	0.000	0.000	0.000	0.000
83	A	96	ASN	0	-0.019	-0.017	12.319	-0.548	-0.548	0.000	0.000	0.000	0.000
84	A	97	GLY	0	0.009	0.007	12.629	-0.524	-0.524	0.000	0.000	0.000	0.000
85	A	98	GLU	-1	-0.867	-0.928	7.463	-35.584	-35.584	0.000	0.000	0.000	0.000
86	A	99	ASP	-1	-0.848	-0.926	9.727	-21.404	-21.404	0.000	0.000	0.000	0.000
87	A	100	MET	0	-0.044	-0.015	9.586	-4.349	-4.349	0.000	0.000	0.000	0.000
88	A	101	VAL	0	0.019	0.011	11.830	2.096	2.096	0.000	0.000	0.000	0.000
89	A	102	TYR	0	-0.076	-0.053	14.401	-0.619	-0.619	0.000	0.000	0.000	0.000
90	A	103	LEU	0	-0.014	-0.002	13.701	0.297	0.297	0.000	0.000	0.000	0.000
91	A	104	PRO	0	-0.012	0.002	17.889	0.572	0.572	0.000	0.000	0.000	0.000
92	A	105	SER	0	0.049	0.001	21.674	-0.272	-0.272	0.000	0.000	0.000	0.000
93	A	106	TYR	0	0.040	0.007	23.729	0.341	0.341	0.000	0.000	0.000	0.000
94	A	107	GLU	-1	-0.967	-0.969	25.402	-10.060	-10.060	0.000	0.000	0.000	0.000
95	A	108	MET	0	0.023	0.004	25.616	0.132	0.132	0.000	0.000	0.000	0.000
96	A	109	CYS	0	0.068	0.058	21.843	-0.494	-0.494	0.000	0.000	0.000	0.000
97	A	110	ARG	1	0.945	0.976	27.029	10.399	10.399	0.000	0.000	0.000	0.000
98	A	111	ILE	0	0.002	0.013	30.127	0.378	0.378	0.000	0.000	0.000	0.000
99	A	112	THR	0	-0.012	-0.026	29.571	0.328	0.328	0.000	0.000	0.000	0.000
100	A	113	MET	0	-0.025	-0.011	28.674	0.252	0.252	0.000	0.000	0.000	0.000
101	A	114	GLU	-1	-0.922	-0.950	32.712	-8.256	-8.256	0.000	0.000	0.000	0.000
102	A	115	PRO	0	-0.067	-0.021	35.267	0.216	0.216	0.000	0.000	0.000	0.000
103	A	117	ARG	1	0.988	1.010	32.497	9.100	9.100	0.000	0.000	0.000	0.000
104	A	118	ILE	0	-0.001	-0.021	34.545	-0.162	-0.162	0.000	0.000	0.000	0.000
105	A	119	LEU	0	-0.013	-0.018	30.678	-0.053	-0.053	0.000	0.000	0.000	0.000
106	A	120	TYR	0	-0.048	-0.019	30.011	-0.291	-0.291	0.000	0.000	0.000	0.000
107	A	121	ASN	0	0.029	0.011	27.212	-0.154	-0.154	0.000	0.000	0.000	0.000
108	A	122	THR	0	-0.016	0.015	28.428	-0.105	-0.105	0.000	0.000	0.000	0.000
109	A	123	THR	0	0.040	0.016	27.332	-0.233	-0.233	0.000	0.000	0.000	0.000
110	A	124	PHE	0	-0.028	-0.003	28.853	0.129	0.129	0.000	0.000	0.000	0.000
111	A	125	PHE	0	0.033	0.004	30.769	0.147	0.147	0.000	0.000	0.000	0.000
112	A	126	PRO	0	0.059	0.035	25.344	-0.136	-0.136	0.000	0.000	0.000	0.000
113	A	127	LYS	1	0.856	0.906	25.889	9.436	9.436	0.000	0.000	0.000	0.000
114	A	128	PHE	0	-0.008	-0.019	27.440	-0.137	-0.137	0.000	0.000	0.000	0.000
115	A	129	LEU	0	-0.001	-0.001	26.355	-0.159	-0.159	0.000	0.000	0.000	0.000
116	A	130	ARG	1	0.831	0.929	20.353	14.010	14.010	0.000	0.000	0.000	0.000
117	A	132	ASN	0	-0.037	-0.017	18.739	-0.728	-0.728	0.000	0.000	0.000	0.000
118	A	133	GLU	-1	-0.862	-0.941	21.721	-12.439	-12.439	0.000	0.000	0.000	0.000
119	A	134	THR	0	-0.022	-0.017	21.437	0.193	0.193	0.000	0.000	0.000	0.000
120	A	135	LEU	0	-0.038	-0.009	17.707	-0.142	-0.142	0.000	0.000	0.000	0.000
121	A	136	PHE	0	0.029	0.004	21.689	0.407	0.407	0.000	0.000	0.000	0.000
122	A	137	PRO	0	-0.010	0.017	19.203	-0.355	-0.355	0.000	0.000	0.000	0.000
123	A	138	THR	0	-0.097	-0.065	19.757	-0.247	-0.247	0.000	0.000	0.000	0.000
124	A	139	LYS	0	0.103	0.065	20.417	-0.806	-0.806	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:12:SER)