FMO DATABASE

FMODB ID: MLRVZ

Calculation Name: 2EE2-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EE2

Chain ID: A

ChEMBL ID:

UniProt ID: Q12860

Base Structure: SolutionNMR

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	119
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-817994.880894
FMO2-HF: Nuclear repulsion	773390.73725
FMO2-HF: Total energy	-44604.143644
FMO2-MP2: Total energy	-44733.632642

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:1:GLY)

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

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.
-85.412	-82.929	0.068	-1.488	-1.063	-0.012

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.867 / q_NPA : 0.920

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	3	SER	0	-0.013	-0.014	2.914	-11.004	-8.521	0.068	-1.488	-1.063	-0.012
4	A	4	GLY	0	0.048	0.012	5.529	2.748	2.748	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.002	0.012	9.354	1.367	1.367	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.020	-0.029	12.134	1.131	1.131	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.021	0.033	15.172	1.193	1.193	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.005	-0.011	14.765	0.104	0.104	0.000	0.000	0.000	0.000
9	A	9	ALA	0	0.027	0.022	17.054	0.933	0.933	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.030	-0.008	18.005	-0.087	-0.087	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.002	0.002	20.594	0.555	0.555	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.006	-0.002	22.757	-0.429	-0.429	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.057	-0.044	25.920	0.400	0.400	0.000	0.000	0.000	0.000
14	A	14	ALA	0	0.024	0.021	29.655	-0.120	-0.120	0.000	0.000	0.000	0.000
15	A	15	GLN	0	-0.044	-0.012	31.664	0.277	0.277	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.853	-0.928	33.843	-8.921	-8.921	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.022	-0.011	29.904	-0.335	-0.335	0.000	0.000	0.000	0.000
18	A	18	PRO	0	-0.032	0.013	30.254	0.194	0.194	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.024	-0.023	31.063	-0.269	-0.269	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.892	-0.942	33.084	-8.904	-8.904	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.008	-0.001	31.817	-0.192	-0.192	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.050	-0.035	32.408	0.292	0.292	0.000	0.000	0.000	0.000
23	A	23	THR	0	0.040	0.019	34.912	-0.230	-0.230	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.944	-0.988	37.159	-7.448	-7.448	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.027	0.001	33.453	0.149	0.149	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.023	0.011	36.811	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.027	-0.009	34.303	0.046	0.046	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.882	0.940	37.659	7.467	7.467	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.023	0.012	37.722	0.005	0.005	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.072	-0.027	40.204	0.306	0.306	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.003	-0.017	41.070	0.223	0.223	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.019	-0.011	39.551	-0.091	-0.091	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.015	-0.019	36.833	-0.132	-0.132	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.897	-0.948	37.271	-8.000	-8.000	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.021	-0.018	34.521	0.152	0.152	0.000	0.000	0.000	0.000
36	A	36	SER	0	0.000	-0.010	37.938	-0.058	-0.058	0.000	0.000	0.000	0.000
37	A	37	VAL	0	0.010	0.005	34.056	-0.072	-0.072	0.000	0.000	0.000	0.000
38	A	38	HIS	0	0.038	0.021	37.371	0.080	0.080	0.000	0.000	0.000	0.000
39	A	39	TRP	0	0.023	0.007	36.432	-0.253	-0.253	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.909	-0.930	38.673	-7.443	-7.443	0.000	0.000	0.000	0.000
41	A	41	HIS	1	0.730	0.866	38.745	7.706	7.706	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.048	0.039	35.278	0.143	0.143	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.012	0.004	38.726	0.151	0.151	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.851	-0.926	35.615	-8.672	-8.672	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.897	0.934	37.871	7.258	7.258	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.027	0.019	34.560	0.118	0.118	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.043	-0.002	33.746	-0.222	-0.222	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.865	-0.930	33.871	-8.638	-8.638	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.093	-0.072	33.426	0.269	0.269	0.000	0.000	0.000	0.000
50	A	50	TYR	0	0.014	0.025	32.895	-0.185	-0.185	0.000	0.000	0.000	0.000
51	A	51	GLN	0	0.023	-0.001	26.883	0.184	0.184	0.000	0.000	0.000	0.000
52	A	52	ILE	0	-0.009	-0.001	29.533	-0.181	-0.181	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.947	0.974	22.847	12.988	12.988	0.000	0.000	0.000	0.000
54	A	54	TYR	0	0.035	0.004	27.060	0.317	0.317	0.000	0.000	0.000	0.000
55	A	55	TRP	0	0.003	0.000	22.546	-0.134	-0.134	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.033	0.021	25.618	0.378	0.378	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.010	-0.007	24.528	-0.556	-0.556	0.000	0.000	0.000	0.000
58	A	58	HIS	0	-0.050	-0.016	22.635	-0.214	-0.214	0.000	0.000	0.000	0.000
59	A	59	ASP	-1	-0.899	-0.938	20.807	-14.224	-14.224	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.918	0.946	14.144	19.856	19.856	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.887	-0.948	17.699	-17.034	-17.034	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.965	-0.991	13.606	-22.297	-22.297	0.000	0.000	0.000	0.000
63	A	63	ALA	0	-0.059	-0.033	17.636	0.283	0.283	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.016	0.021	19.793	0.802	0.802	0.000	0.000	0.000	0.000
65	A	65	ASN	0	-0.049	-0.023	22.940	-0.014	-0.014	0.000	0.000	0.000	0.000
66	A	66	ARG	1	0.893	0.932	21.142	14.084	14.084	0.000	0.000	0.000	0.000
67	A	67	VAL	0	0.008	0.017	27.636	0.168	0.168	0.000	0.000	0.000	0.000
68	A	68	GLN	0	0.008	0.011	30.633	-0.215	-0.215	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.004	0.003	32.375	0.225	0.225	0.000	0.000	0.000	0.000
70	A	70	THR	0	0.033	0.004	36.017	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	71	SER	0	-0.014	-0.015	37.993	0.114	0.114	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.037	-0.024	38.921	0.208	0.208	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.921	-0.950	39.753	-7.506	-7.506	0.000	0.000	0.000	0.000
74	A	74	TYR	0	-0.020	-0.026	39.922	-0.178	-0.178	0.000	0.000	0.000	0.000
75	A	75	SER	0	0.000	-0.003	39.253	0.004	0.004	0.000	0.000	0.000	0.000
76	A	76	ALA	0	0.003	0.020	35.961	0.053	0.053	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.805	0.889	38.028	7.886	7.886	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.023	-0.004	32.200	-0.215	-0.215	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.777	-0.876	35.017	-7.989	-7.989	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.057	-0.040	33.214	-0.136	-0.136	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.007	0.032	31.697	-0.269	-0.269	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.010	0.015	29.750	0.291	0.291	0.000	0.000	0.000	0.000
83	A	83	PRO	0	0.040	0.028	33.696	0.047	0.047	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.907	-0.934	35.158	-8.625	-8.625	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.013	-0.008	30.269	-0.245	-0.245	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.003	0.003	28.989	-0.031	-0.031	0.000	0.000	0.000	0.000
87	A	87	TYR	0	0.004	-0.019	28.699	-0.444	-0.444	0.000	0.000	0.000	0.000
88	A	88	PHE	0	0.008	0.016	25.394	0.292	0.292	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.026	-0.032	27.841	-0.117	-0.117	0.000	0.000	0.000	0.000
90	A	90	GLU	-1	-0.895	-0.943	25.256	-12.744	-12.744	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.004	0.006	29.090	-0.050	-0.050	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.060	0.049	28.665	-0.043	-0.043	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.002	0.004	29.715	0.133	0.133	0.000	0.000	0.000	0.000
94	A	94	CYS	0	-0.057	-0.033	28.808	-0.346	-0.346	0.000	0.000	0.000	0.000
95	A	95	ASN	0	0.062	0.011	30.597	-0.041	-0.041	0.000	0.000	0.000	0.000
96	A	96	SER	0	-0.038	-0.020	29.785	-0.336	-0.336	0.000	0.000	0.000	0.000
97	A	97	ALA	0	-0.064	-0.005	29.960	-0.140	-0.140	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.029	0.003	27.870	-0.368	-0.368	0.000	0.000	0.000	0.000
99	A	99	CYS	0	-0.068	-0.040	23.383	0.249	0.249	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.060	0.031	26.568	0.046	0.046	0.000	0.000	0.000	0.000
101	A	101	PRO	0	-0.040	-0.015	26.099	-0.503	-0.503	0.000	0.000	0.000	0.000
102	A	102	PRO	0	-0.046	-0.015	24.243	0.373	0.373	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.054	-0.046	27.414	0.174	0.174	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.889	-0.955	28.660	-10.712	-10.712	0.000	0.000	0.000	0.000
105	A	105	MET	0	-0.048	-0.011	23.098	0.018	0.018	0.000	0.000	0.000	0.000
106	A	106	ILE	0	0.020	0.014	28.646	0.229	0.229	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.949	-0.967	30.283	-10.446	-10.446	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.031	-0.016	31.593	0.432	0.432	0.000	0.000	0.000	0.000
109	A	109	PHE	0	0.020	0.002	32.874	-0.242	-0.242	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.023	-0.023	34.881	0.313	0.313	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.920	0.958	37.141	7.536	7.536	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.898	0.922	39.388	7.789	7.789	0.000	0.000	0.000	0.000
113	A	113	ALA	0	0.026	0.017	40.226	0.151	0.151	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.020	-0.012	41.858	0.026	0.026	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.032	0.008	44.925	-0.117	-0.117	0.000	0.000	0.000	0.000
116	A	116	PRO	0	-0.033	-0.018	46.811	0.094	0.094	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.036	-0.021	46.701	0.103	0.103	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.026	-0.008	49.789	0.040	0.040	0.000	0.000	0.000	0.000
119	A	119	GLY	-1	-0.934	-0.948	51.999	-6.142	-6.142	0.000	0.000	0.000	0.000

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