FMO DATABASE

FMODB ID: 1VJ2Z

Calculation Name: 1BV8-A-Other547

Preferred Name: Alpha-2-macroglobulin

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1BV8

Chain ID: A

ChEMBL ID: CHEMBL4295690

UniProt ID: P01023

Base Structure: SolutionNMR

Registration Date: 2025-10-06

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1160803.289313
FMO2-HF: Nuclear repulsion	1106743.998008
FMO2-HF: Total energy	-54059.291305
FMO2-MP2: Total energy	-54216.293491

3D Structure

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:GLU)

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

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.
-37.087	-35.092	3.718	-2.688	-3.023	-0.03

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.207 / q_NPA : -0.122

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	PHE	0	-0.035	-0.022	2.205	-16.829	-14.897	3.719	-2.681	-2.969	-0.030
4	A	4	PRO	0	0.036	0.052	5.009	2.070	2.133	-0.001	-0.007	-0.054	0.000
5	A	5	PHE	0	0.005	-0.001	8.363	0.209	0.209	0.000	0.000	0.000	0.000
6	A	6	ALA	0	-0.018	-0.012	10.575	0.231	0.231	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.007	0.002	12.610	0.154	0.154	0.000	0.000	0.000	0.000
8	A	8	GLY	0	-0.034	-0.010	16.356	0.087	0.087	0.000	0.000	0.000	0.000
9	A	9	VAL	0	0.015	-0.001	19.032	0.075	0.075	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.025	-0.015	22.289	0.080	0.080	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.026	0.018	25.221	0.001	0.001	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.010	0.002	28.816	0.004	0.004	0.000	0.000	0.000	0.000
13	A	13	PRO	0	-0.020	-0.011	31.003	0.026	0.026	0.000	0.000	0.000	0.000
14	A	14	GLN	0	-0.026	-0.009	33.754	0.040	0.040	0.000	0.000	0.000	0.000
15	A	15	THR	0	0.018	-0.011	35.508	0.008	0.008	0.000	0.000	0.000	0.000
16	A	16	CYS	0	-0.069	-0.036	32.971	0.030	0.030	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.892	-0.947	38.697	-0.288	-0.288	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.826	-0.898	41.991	-0.318	-0.318	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.042	0.027	42.773	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.816	0.889	41.811	0.336	0.336	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.010	0.025	38.568	-0.018	-0.018	0.000	0.000	0.000	0.000
22	A	22	HIS	0	0.017	0.004	39.027	-0.021	-0.021	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.056	-0.036	40.931	-0.009	-0.009	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.067	-0.037	39.311	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.051	0.033	34.982	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	26	GLN	0	0.015	0.025	30.427	0.027	0.027	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.013	-0.014	27.526	0.004	0.004	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.035	-0.011	24.263	-0.008	-0.008	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.026	0.004	22.820	-0.008	-0.008	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.013	-0.005	17.886	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	31	VAL	0	0.056	0.043	15.967	0.006	0.006	0.000	0.000	0.000	0.000
32	A	32	SER	0	-0.002	0.009	10.934	0.194	0.194	0.000	0.000	0.000	0.000
33	A	33	TYR	-1	-0.848	-0.932	11.156	-5.326	-5.326	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.055	-0.027	6.401	-0.162	-0.162	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.135	0.091	7.841	-1.302	-1.302	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.105	-0.075	6.180	-1.405	-1.405	0.000	0.000	0.000	0.000
37	A	37	ARG	0	0.020	0.029	7.559	1.389	1.389	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.114	-0.071	11.123	0.031	0.031	0.000	0.000	0.000	0.000
39	A	39	ALA	0	0.028	-0.020	13.657	0.333	0.333	0.000	0.000	0.000	0.000
40	A	40	SER	-1	-0.707	-0.804	14.622	-2.401	-2.401	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.191	-0.082	16.874	-0.143	-0.143	0.000	0.000	0.000	0.000
42	A	42	MET	0	-0.023	-0.038	18.307	0.211	0.211	0.000	0.000	0.000	0.000
43	A	43	ALA	0	-0.007	0.002	17.565	-0.295	-0.295	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.014	0.019	19.073	0.231	0.231	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.017	-0.014	19.748	-0.105	-0.105	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.855	-0.914	22.187	-1.174	-1.174	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.044	0.027	24.511	-0.040	-0.040	0.000	0.000	0.000	0.000
48	A	48	LYS	1	0.951	0.970	26.450	0.862	0.862	0.000	0.000	0.000	0.000
49	A	49	MET	0	0.042	0.001	29.424	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	50	VAL	0	0.010	0.005	31.318	0.023	0.023	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.022	0.035	34.907	0.006	0.006	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.045	-0.039	36.518	0.027	0.027	0.000	0.000	0.000	0.000
53	A	53	PHE	0	-0.030	-0.018	33.898	0.025	0.025	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.005	-0.003	39.427	-0.012	-0.012	0.000	0.000	0.000	0.000
55	A	55	PRO	0	0.067	0.047	35.396	0.004	0.004	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.021	-0.007	37.507	0.024	0.024	0.000	0.000	0.000	0.000
57	A	57	LYS	1	1.022	1.006	37.017	0.521	0.521	0.000	0.000	0.000	0.000
58	A	58	PRO	0	-0.027	-0.022	37.280	-0.021	-0.021	0.000	0.000	0.000	0.000
59	A	59	THR	0	0.000	-0.008	34.489	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	60	VAL	0	0.025	0.012	31.953	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.962	0.997	32.452	0.578	0.578	0.000	0.000	0.000	0.000
62	A	62	MET	0	-0.059	-0.035	34.374	0.023	0.023	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.014	0.020	27.917	0.002	0.002	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.848	-0.905	30.281	-0.726	-0.726	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.909	0.938	31.840	0.584	0.584	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.071	-0.045	29.407	0.037	0.037	0.000	0.000	0.000	0.000
67	A	67	ASN	0	-0.079	-0.059	28.890	0.070	0.070	0.000	0.000	0.000	0.000
68	A	68	HIS	0	-0.040	-0.011	30.853	-0.024	-0.024	0.000	0.000	0.000	0.000
69	A	69	VAL	0	0.071	0.044	25.900	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	70	SER	0	0.004	-0.004	25.513	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	71	ARG	0	-0.042	0.012	26.445	0.122	0.122	0.000	0.000	0.000	0.000
72	A	72	THR	0	0.009	-0.001	26.426	-0.062	-0.062	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.919	-0.967	28.815	-0.739	-0.739	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.011	-0.008	30.792	-0.029	-0.029	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.020	0.004	33.431	0.051	0.051	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.059	-0.040	35.457	0.023	0.023	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.019	-0.025	35.423	0.013	0.013	0.000	0.000	0.000	0.000
78	A	78	HIS	0	0.007	-0.006	30.439	0.009	0.009	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.038	-0.015	27.555	0.048	0.048	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.004	0.005	26.899	-0.049	-0.049	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.035	-0.028	22.248	0.080	0.080	0.000	0.000	0.000	0.000
82	A	82	TYR	-1	-0.905	-0.956	24.107	-1.378	-1.378	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.012	-0.008	20.772	0.122	0.122	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.858	-0.939	21.204	-1.494	-1.494	0.000	0.000	0.000	0.000
85	A	85	LYS	0	-0.061	-0.035	20.466	0.143	0.143	0.000	0.000	0.000	0.000
86	A	86	VAL	0	-0.032	-0.018	14.739	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	87	SER	-1	-0.782	-0.860	15.890	-2.339	-2.339	0.000	0.000	0.000	0.000
88	A	88	ASN	0	0.036	-0.033	10.985	-0.335	-0.335	0.000	0.000	0.000	0.000
89	A	89	GLN	0	-0.188	-0.044	11.945	-0.203	-0.203	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.059	-0.057	13.582	0.117	0.117	0.000	0.000	0.000	0.000
91	A	91	LEU	0	0.004	0.013	14.936	0.271	0.271	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.026	-0.022	18.703	-0.027	-0.027	0.000	0.000	0.000	0.000
93	A	93	LEU	0	0.000	0.011	21.411	0.095	0.095	0.000	0.000	0.000	0.000
94	A	94	PHE	0	-0.002	-0.014	24.623	0.009	0.009	0.000	0.000	0.000	0.000
95	A	95	PHE	0	0.014	0.006	27.156	0.051	0.051	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.035	-0.030	31.213	0.028	0.028	0.000	0.000	0.000	0.000
97	A	97	VAL	0	-0.033	-0.020	34.285	-0.010	-0.010	0.000	0.000	0.000	0.000
98	A	98	LEU	0	0.050	0.019	36.453	0.016	0.016	0.000	0.000	0.000	0.000
99	A	99	GLN	0	-0.051	-0.019	39.934	-0.018	-0.018	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.918	-0.959	41.783	-0.358	-0.358	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.006	0.006	45.473	0.014	0.014	0.000	0.000	0.000	0.000
102	A	102	PRO	0	-0.023	0.010	45.039	-0.018	-0.018	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.033	0.007	42.621	0.018	0.018	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.865	0.916	44.288	0.331	0.331	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.792	-0.894	40.376	-0.454	-0.454	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.022	0.010	38.763	-0.011	-0.011	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.822	0.881	35.091	0.497	0.497	0.000	0.000	0.000	0.000
108	A	108	PRO	0	0.029	0.030	30.641	0.000	0.000	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.049	-0.015	29.197	0.010	0.010	0.000	0.000	0.000	0.000
110	A	110	ILE	0	-0.010	0.000	25.052	-0.019	-0.019	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.026	-0.022	22.342	0.045	0.045	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.848	0.909	20.915	1.301	1.301	0.000	0.000	0.000	0.000
113	A	113	VAL	0	-0.015	-0.016	15.780	0.117	0.117	0.000	0.000	0.000	0.000
114	A	114	TYR	0	-0.012	-0.007	17.254	-0.144	-0.144	0.000	0.000	0.000	0.000
115	A	115	ASP	0	-0.041	-0.016	14.741	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	116	TYR	-1	-0.859	-0.963	17.195	-1.477	-1.477	0.000	0.000	0.000	0.000
117	A	117	TYR	0	-0.052	-0.032	16.171	-0.102	-0.102	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.845	-0.891	17.572	-1.766	-1.766	0.000	0.000	0.000	0.000
119	A	119	THR	0	-0.092	-0.061	15.586	0.064	0.064	0.000	0.000	0.000	0.000
120	A	120	ASP	-1	-0.915	-0.943	13.551	-2.478	-2.478	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.938	-0.963	11.275	-4.971	-4.971	0.000	0.000	0.000	0.000
122	A	122	PHE	0	-0.038	-0.022	13.772	0.380	0.380	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.026	0.009	14.094	-0.050	-0.050	0.000	0.000	0.000	0.000
124	A	124	ILE	0	-0.018	-0.031	15.714	0.300	0.300	0.000	0.000	0.000	0.000
125	A	125	ALA	0	-0.029	-0.007	18.719	-0.036	-0.036	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.949	-0.977	20.866	-0.809	-0.809	0.000	0.000	0.000	0.000
127	A	127	TYR	0	-0.018	-0.022	24.166	-0.026	-0.026	0.000	0.000	0.000	0.000
128	A	128	ASN	0	0.029	-0.005	26.798	0.059	0.059	0.000	0.000	0.000	0.000
129	A	129	ALA	0	0.045	0.008	30.441	-0.018	-0.018	0.000	0.000	0.000	0.000
130	A	130	PRO	0	-0.044	0.005	30.956	0.035	0.035	0.000	0.000	0.000	0.000
131	A	132	SER	0	0.010	0.002	36.324	0.007	0.007	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.908	0.957	38.252	0.353	0.353	0.000	0.000	0.000	0.000
133	A	134	ASP	0	0.059	0.032	41.704	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	135	LEU	0	-0.078	-0.063	44.231	0.009	0.009	0.000	0.000	0.000	0.000
135	A	136	GLY	0	0.017	0.018	47.334	0.001	0.001	0.000	0.000	0.000	0.000
136	A	137	ASN	0	-0.086	-0.063	49.386	0.011	0.011	0.000	0.000	0.000	0.000
137	A	138	ALA	-1	-0.855	-0.891	51.182	-0.254	-0.254	0.000	0.000	0.000	0.000

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