FMO DATABASE

FMODB ID: 5G4QZ

Calculation Name: 1B4A-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1B4A

Chain ID: A

ChEMBL ID:

UniProt ID: O31408

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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1244481.217598
FMO2-HF: Nuclear repulsion	1186309.915065
FMO2-HF: Total energy	-58171.302533
FMO2-MP2: Total energy	-58338.672539

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:4:GLY)

Summations of interaction energy for fragment #1(A:4: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.
27.255	31.596	0.589	-2.241	-2.689	-0.022

Interaction energy analysis for fragmet #1(A:4:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.892 / q_NPA : 0.934

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	6	ARG	1	0.917	0.969	3.856	48.813	49.709	-0.004	-0.365	-0.526	-0.001
4	A	7	HIS	0	0.024	-0.005	2.579	-16.762	-13.657	0.591	-1.786	-1.911	-0.021
5	A	8	ILE	0	-0.015	-0.012	3.875	8.503	8.843	0.002	-0.090	-0.252	0.000
6	A	9	LYS	1	0.876	0.932	6.115	31.735	31.735	0.000	0.000	0.000	0.000
7	A	10	ILE	0	0.035	0.022	7.255	3.697	3.697	0.000	0.000	0.000	0.000
8	A	11	ARG	1	0.925	0.962	7.438	33.084	33.084	0.000	0.000	0.000	0.000
9	A	12	GLU	-1	-0.840	-0.901	10.166	-21.906	-21.906	0.000	0.000	0.000	0.000
10	A	13	ILE	0	0.000	0.006	11.748	2.120	2.120	0.000	0.000	0.000	0.000
11	A	14	ILE	0	-0.031	-0.022	11.810	1.496	1.496	0.000	0.000	0.000	0.000
12	A	15	MET	0	-0.051	-0.023	13.711	0.895	0.895	0.000	0.000	0.000	0.000
13	A	16	SER	0	-0.013	0.000	15.962	1.310	1.310	0.000	0.000	0.000	0.000
14	A	17	ASN	0	-0.066	-0.036	17.898	0.701	0.701	0.000	0.000	0.000	0.000
15	A	18	ASP	-1	-0.826	-0.929	18.707	-14.628	-14.628	0.000	0.000	0.000	0.000
16	A	19	ILE	0	-0.032	0.001	16.420	0.334	0.334	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.798	-0.893	19.249	-12.742	-12.742	0.000	0.000	0.000	0.000
18	A	21	THR	0	-0.039	-0.030	20.453	-0.167	-0.167	0.000	0.000	0.000	0.000
19	A	22	GLN	0	0.059	0.026	15.614	-1.083	-1.083	0.000	0.000	0.000	0.000
20	A	23	ASP	-1	-0.846	-0.929	16.522	-16.652	-16.652	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.765	-0.865	18.200	-15.603	-15.603	0.000	0.000	0.000	0.000
22	A	25	LEU	0	-0.007	-0.010	11.554	-0.596	-0.596	0.000	0.000	0.000	0.000
23	A	26	VAL	0	-0.059	-0.042	13.813	-1.470	-1.470	0.000	0.000	0.000	0.000
24	A	27	ASP	-1	-0.864	-0.929	14.872	-16.768	-16.768	0.000	0.000	0.000	0.000
25	A	28	ARG	1	0.871	0.918	15.689	16.401	16.401	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.072	-0.028	9.428	-1.726	-1.726	0.000	0.000	0.000	0.000
27	A	30	ARG	1	0.814	0.907	12.930	17.917	17.917	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.884	-0.942	15.448	-15.469	-15.469	0.000	0.000	0.000	0.000
29	A	32	ALA	0	-0.077	-0.029	13.227	0.238	0.238	0.000	0.000	0.000	0.000
30	A	33	GLY	0	0.017	0.012	13.335	-1.345	-1.345	0.000	0.000	0.000	0.000
31	A	34	PHE	0	-0.046	-0.040	6.784	-3.307	-3.307	0.000	0.000	0.000	0.000
32	A	35	ASN	0	0.019	0.010	11.466	1.040	1.040	0.000	0.000	0.000	0.000
33	A	36	VAL	0	-0.006	0.006	9.229	-1.009	-1.009	0.000	0.000	0.000	0.000
34	A	37	THR	0	0.058	0.032	12.429	1.277	1.277	0.000	0.000	0.000	0.000
35	A	38	GLN	0	0.098	0.027	13.593	-2.149	-2.149	0.000	0.000	0.000	0.000
36	A	39	ALA	0	0.004	0.003	14.973	-0.601	-0.601	0.000	0.000	0.000	0.000
37	A	40	THR	0	-0.063	-0.031	8.929	-0.905	-0.905	0.000	0.000	0.000	0.000
38	A	41	VAL	0	0.044	0.021	10.433	-1.629	-1.629	0.000	0.000	0.000	0.000
39	A	42	SER	0	-0.010	-0.017	11.474	-0.234	-0.234	0.000	0.000	0.000	0.000
40	A	43	ARG	1	0.818	0.911	8.306	31.648	31.648	0.000	0.000	0.000	0.000
41	A	44	ASP	-1	-0.791	-0.895	6.928	-42.792	-42.792	0.000	0.000	0.000	0.000
42	A	45	ILE	0	0.003	0.004	9.043	-0.802	-0.802	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.965	0.985	11.910	20.890	20.890	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.856	-0.923	6.934	-40.490	-40.490	0.000	0.000	0.000	0.000
45	A	48	MET	0	-0.064	-0.024	6.237	-2.460	-2.460	0.000	0.000	0.000	0.000
46	A	49	GLN	0	-0.044	-0.019	8.816	2.696	2.696	0.000	0.000	0.000	0.000
47	A	50	LEU	0	-0.021	-0.001	10.448	0.940	0.940	0.000	0.000	0.000	0.000
48	A	51	VAL	0	-0.020	-0.003	13.901	1.101	1.101	0.000	0.000	0.000	0.000
49	A	52	LYS	1	0.864	0.940	17.676	15.075	15.075	0.000	0.000	0.000	0.000
50	A	53	VAL	0	-0.013	-0.010	20.258	0.422	0.422	0.000	0.000	0.000	0.000
51	A	54	PRO	0	0.018	0.020	22.647	-0.098	-0.098	0.000	0.000	0.000	0.000
52	A	55	MET	0	-0.013	0.000	24.423	-0.303	-0.303	0.000	0.000	0.000	0.000
53	A	56	ALA	0	0.011	-0.005	26.552	0.316	0.316	0.000	0.000	0.000	0.000
54	A	57	ASN	0	0.013	0.003	29.018	0.117	0.117	0.000	0.000	0.000	0.000
55	A	58	GLY	0	0.030	0.028	30.003	0.289	0.289	0.000	0.000	0.000	0.000
56	A	59	ARG	1	0.850	0.924	26.925	11.438	11.438	0.000	0.000	0.000	0.000
57	A	60	TYR	0	0.004	-0.012	23.581	-0.278	-0.278	0.000	0.000	0.000	0.000
58	A	61	LYS	1	0.956	1.006	19.981	14.831	14.831	0.000	0.000	0.000	0.000
59	A	62	TYR	0	-0.018	-0.021	15.732	0.292	0.292	0.000	0.000	0.000	0.000
60	A	63	SER	0	-0.033	-0.060	16.296	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	64	LEU	0	0.025	0.016	10.995	-1.154	-1.154	0.000	0.000	0.000	0.000
62	A	65	PRO	0	0.057	0.035	12.486	1.484	1.484	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.008	-0.014	14.479	0.545	0.545	0.000	0.000	0.000	0.000
64	A	67	ASP	-1	-0.837	-0.884	16.206	-14.794	-14.794	0.000	0.000	0.000	0.000
65	A	68	GLN	0	0.033	0.000	18.771	0.513	0.513	0.000	0.000	0.000	0.000
66	A	69	ARG	1	0.873	0.960	22.182	13.686	13.686	0.000	0.000	0.000	0.000
67	A	70	PHE	0	0.032	0.011	22.543	0.531	0.531	0.000	0.000	0.000	0.000
68	A	71	ASN	0	-0.021	-0.027	21.246	-0.879	-0.879	0.000	0.000	0.000	0.000
69	A	72	PRO	0	0.106	0.063	23.731	-0.339	-0.339	0.000	0.000	0.000	0.000
70	A	73	LEU	0	0.075	0.040	25.018	-0.107	-0.107	0.000	0.000	0.000	0.000
71	A	74	GLN	0	-0.015	-0.014	22.322	0.061	0.061	0.000	0.000	0.000	0.000
72	A	75	LYS	1	0.800	0.908	18.909	15.543	15.543	0.000	0.000	0.000	0.000
73	A	76	LEU	0	0.063	0.035	22.744	-0.159	-0.159	0.000	0.000	0.000	0.000
74	A	77	LYS	1	0.895	0.953	25.963	10.885	10.885	0.000	0.000	0.000	0.000
75	A	78	ARG	1	0.856	0.940	20.234	14.474	14.474	0.000	0.000	0.000	0.000
76	A	79	ALA	0	0.086	0.041	23.138	0.184	0.184	0.000	0.000	0.000	0.000
77	A	80	LEU	0	0.003	-0.008	24.193	0.245	0.245	0.000	0.000	0.000	0.000
78	A	81	VAL	0	-0.038	-0.021	25.208	0.316	0.316	0.000	0.000	0.000	0.000
79	A	82	ASP	-1	-0.933	-0.952	22.091	-14.079	-14.079	0.000	0.000	0.000	0.000
80	A	83	VAL	0	-0.068	-0.039	25.003	0.165	0.165	0.000	0.000	0.000	0.000
81	A	84	PHE	0	0.026	0.013	27.561	0.443	0.443	0.000	0.000	0.000	0.000
82	A	85	ILE	0	-0.046	-0.014	31.107	0.058	0.058	0.000	0.000	0.000	0.000
83	A	86	LYS	1	0.801	0.879	34.026	8.055	8.055	0.000	0.000	0.000	0.000
84	A	87	LEU	0	0.013	0.014	36.663	-0.170	-0.170	0.000	0.000	0.000	0.000
85	A	88	ASP	-1	-0.829	-0.897	38.653	-7.540	-7.540	0.000	0.000	0.000	0.000
86	A	89	GLY	0	0.035	0.002	41.574	-0.168	-0.168	0.000	0.000	0.000	0.000
87	A	90	THR	0	-0.053	-0.017	44.167	0.199	0.199	0.000	0.000	0.000	0.000
88	A	91	GLY	0	0.036	0.024	47.004	-0.055	-0.055	0.000	0.000	0.000	0.000
89	A	92	ASN	0	-0.057	-0.042	45.690	0.060	0.060	0.000	0.000	0.000	0.000
90	A	93	LEU	0	0.021	0.020	43.058	-0.155	-0.155	0.000	0.000	0.000	0.000
91	A	94	LEU	0	-0.024	-0.011	39.237	0.125	0.125	0.000	0.000	0.000	0.000
92	A	95	VAL	0	-0.011	-0.012	39.300	-0.088	-0.088	0.000	0.000	0.000	0.000
93	A	96	LEU	0	0.027	0.019	32.056	0.057	0.057	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.884	0.953	35.191	8.468	8.468	0.000	0.000	0.000	0.000
95	A	98	THR	0	0.031	-0.005	29.557	-0.046	-0.046	0.000	0.000	0.000	0.000
96	A	99	LEU	0	0.032	0.020	26.522	0.261	0.261	0.000	0.000	0.000	0.000
97	A	100	PRO	0	-0.001	-0.018	29.326	-0.121	-0.121	0.000	0.000	0.000	0.000
98	A	101	GLY	0	0.007	0.016	27.033	-0.405	-0.405	0.000	0.000	0.000	0.000
99	A	102	ASN	0	-0.038	-0.023	24.603	-0.884	-0.884	0.000	0.000	0.000	0.000
100	A	103	ALA	0	0.016	0.020	27.057	-0.128	-0.128	0.000	0.000	0.000	0.000
101	A	104	HIS	0	0.057	0.013	26.771	0.238	0.238	0.000	0.000	0.000	0.000
102	A	105	ALA	0	0.001	0.006	23.984	-0.026	-0.026	0.000	0.000	0.000	0.000
103	A	106	ILE	0	-0.005	-0.009	25.924	-0.105	-0.105	0.000	0.000	0.000	0.000
104	A	107	GLY	0	0.064	0.024	28.303	0.178	0.178	0.000	0.000	0.000	0.000
105	A	108	VAL	0	0.012	0.013	25.319	0.090	0.090	0.000	0.000	0.000	0.000
106	A	109	LEU	0	-0.079	-0.044	23.261	-0.127	-0.127	0.000	0.000	0.000	0.000
107	A	110	LEU	0	-0.030	-0.019	27.306	0.152	0.152	0.000	0.000	0.000	0.000
108	A	111	ASP	-1	-0.856	-0.913	30.639	-9.503	-9.503	0.000	0.000	0.000	0.000
109	A	112	ASN	0	-0.059	-0.045	25.226	0.279	0.279	0.000	0.000	0.000	0.000
110	A	113	LEU	0	-0.085	-0.042	29.062	-0.206	-0.206	0.000	0.000	0.000	0.000
111	A	114	ASP	-1	-0.940	-0.957	31.058	-9.447	-9.447	0.000	0.000	0.000	0.000
112	A	115	TRP	0	-0.034	-0.016	32.725	0.213	0.213	0.000	0.000	0.000	0.000
113	A	116	ASP	-1	-0.839	-0.913	36.563	-7.853	-7.853	0.000	0.000	0.000	0.000
114	A	117	GLU	-1	-0.880	-0.923	38.959	-7.892	-7.892	0.000	0.000	0.000	0.000
115	A	118	ILE	0	-0.016	-0.010	35.340	0.185	0.185	0.000	0.000	0.000	0.000
116	A	119	VAL	0	-0.092	-0.050	39.175	0.026	0.026	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.050	0.026	36.999	-0.016	-0.016	0.000	0.000	0.000	0.000
118	A	121	THR	0	-0.069	-0.044	33.640	0.090	0.090	0.000	0.000	0.000	0.000
119	A	122	ILE	0	0.015	0.009	35.954	0.028	0.028	0.000	0.000	0.000	0.000
120	A	123	CYS	0	-0.078	-0.016	31.250	0.096	0.096	0.000	0.000	0.000	0.000
121	A	124	GLY	0	0.033	0.035	34.267	0.121	0.121	0.000	0.000	0.000	0.000
122	A	125	ASP	-1	-0.871	-0.943	31.064	-10.207	-10.207	0.000	0.000	0.000	0.000
123	A	126	ASP	-1	-0.910	-0.972	30.614	-9.547	-9.547	0.000	0.000	0.000	0.000
124	A	127	THR	0	-0.035	-0.015	32.869	0.213	0.213	0.000	0.000	0.000	0.000
125	A	128	CYS	0	-0.041	-0.025	32.949	-0.073	-0.073	0.000	0.000	0.000	0.000
126	A	129	LEU	0	-0.016	0.001	35.085	0.193	0.193	0.000	0.000	0.000	0.000
127	A	130	ILE	0	0.060	0.014	35.185	-0.123	-0.123	0.000	0.000	0.000	0.000
128	A	131	ILE	0	-0.008	0.003	38.359	0.265	0.265	0.000	0.000	0.000	0.000
129	A	132	CYS	0	0.012	0.019	40.601	-0.179	-0.179	0.000	0.000	0.000	0.000
130	A	133	ARG	1	0.871	0.933	41.560	7.718	7.718	0.000	0.000	0.000	0.000
131	A	134	THR	0	0.004	-0.029	44.978	0.220	0.220	0.000	0.000	0.000	0.000
132	A	135	PRO	0	0.039	0.000	46.015	-0.141	-0.141	0.000	0.000	0.000	0.000
133	A	136	LYS	1	0.920	0.969	46.994	6.581	6.581	0.000	0.000	0.000	0.000
134	A	137	ASP	-1	-0.773	-0.874	42.951	-7.265	-7.265	0.000	0.000	0.000	0.000
135	A	138	ALA	0	0.046	0.034	42.253	-0.194	-0.194	0.000	0.000	0.000	0.000
136	A	139	LYS	1	0.951	0.962	42.142	6.741	6.741	0.000	0.000	0.000	0.000
137	A	140	LYS	1	0.760	0.873	41.439	7.437	7.437	0.000	0.000	0.000	0.000
138	A	141	VAL	0	0.078	0.032	36.751	-0.168	-0.168	0.000	0.000	0.000	0.000
139	A	142	SER	0	0.010	0.006	37.529	-0.233	-0.233	0.000	0.000	0.000	0.000
140	A	143	ASN	0	-0.037	-0.033	38.313	-0.147	-0.147	0.000	0.000	0.000	0.000
141	A	144	GLN	0	0.008	0.023	34.151	0.024	0.024	0.000	0.000	0.000	0.000
142	A	145	LEU	0	0.001	-0.003	32.554	-0.282	-0.282	0.000	0.000	0.000	0.000
143	A	146	LEU	0	0.004	-0.006	33.748	-0.213	-0.213	0.000	0.000	0.000	0.000
144	A	147	SER	0	-0.088	-0.035	35.254	-0.107	-0.107	0.000	0.000	0.000	0.000
145	A	148	MET	0	-0.114	-0.063	29.913	-0.362	-0.362	0.000	0.000	0.000	0.000
146	A	149	LEU	-1	-0.896	-0.932	30.125	-10.135	-10.135	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:4:GLY)