FMO DATABASE

FMODB ID: 3KMZL

Calculation Name: 1B24-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1B24

Chain ID: A

ChEMBL ID:

UniProt ID: P21505

Base Structure: X-ray

Registration Date: 2025-09-02

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	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1888297.733615
FMO2-HF: Nuclear repulsion	1819035.334959
FMO2-HF: Total energy	-69262.398655
FMO2-MP2: Total energy	-69469.007038

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:7:VAL)

Summations of interaction energy for fragment #1(A:7:VAL)

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.
160.894	170.09	4.087	-4.907	-8.375	-0.038

Interaction energy analysis for fragmet #1(A:7:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.937 / q_NPA : 0.963

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	9	GLY	0	0.022	0.012	3.915	4.594	5.844	-0.007	-0.465	-0.778	0.001
4	A	10	ILE	0	0.016	0.007	2.206	2.009	3.604	0.764	-0.753	-1.605	-0.009
5	A	11	SER	0	0.037	0.024	3.423	9.329	10.348	0.017	-0.406	-0.629	0.001
52	A	58	PHE	0	0.025	0.015	2.324	-7.379	-5.997	1.934	-1.184	-2.132	-0.010
53	A	59	LEU	0	-0.008	0.000	3.143	-2.949	-2.320	0.081	-0.136	-0.574	-0.001
56	A	62	GLU	-1	-0.945	-0.965	2.431	-57.937	-55.211	1.290	-1.840	-2.176	-0.020
57	A	63	LEU	0	-0.075	-0.038	4.535	2.198	2.328	-0.001	-0.007	-0.122	0.000
84	A	90	TYR	0	-0.014	-0.007	3.599	0.402	0.752	0.010	-0.105	-0.256	0.000
98	A	104	ARG	1	0.985	0.988	3.959	44.672	44.787	-0.001	-0.011	-0.103	0.000
6	A	12	ALA	0	0.028	0.014	5.701	5.476	5.476	0.000	0.000	0.000	0.000
7	A	13	TYR	0	-0.039	-0.032	7.651	3.859	3.859	0.000	0.000	0.000	0.000
8	A	14	LEU	0	-0.006	-0.011	6.708	3.142	3.142	0.000	0.000	0.000	0.000
9	A	15	LEU	0	-0.004	0.002	9.634	2.560	2.560	0.000	0.000	0.000	0.000
10	A	16	GLY	0	0.029	0.005	11.657	2.043	2.043	0.000	0.000	0.000	0.000
11	A	17	LEU	0	-0.029	-0.023	11.845	1.583	1.583	0.000	0.000	0.000	0.000
12	A	18	ILE	0	-0.054	-0.026	11.949	1.286	1.286	0.000	0.000	0.000	0.000
13	A	19	ILE	0	-0.074	-0.037	15.517	1.163	1.163	0.000	0.000	0.000	0.000
14	A	20	GLY	0	-0.029	-0.005	17.362	0.906	0.906	0.000	0.000	0.000	0.000
15	A	21	ASP	-1	-0.832	-0.925	18.629	-12.897	-12.897	0.000	0.000	0.000	0.000
16	A	22	GLY	0	0.046	0.022	18.318	-0.775	-0.775	0.000	0.000	0.000	0.000
17	A	23	GLY	0	0.008	0.020	17.945	0.895	0.895	0.000	0.000	0.000	0.000
18	A	24	LEU	0	-0.025	-0.013	13.921	-0.760	-0.760	0.000	0.000	0.000	0.000
19	A	25	TYR	0	0.009	0.000	17.943	0.934	0.934	0.000	0.000	0.000	0.000
20	A	26	LYS	1	0.893	0.945	20.299	11.791	11.791	0.000	0.000	0.000	0.000
21	A	27	LEU	0	0.035	0.031	22.685	0.484	0.484	0.000	0.000	0.000	0.000
22	A	28	LYS	1	0.936	0.964	25.542	8.883	8.883	0.000	0.000	0.000	0.000
23	A	29	TYR	0	0.039	0.026	27.352	0.061	0.061	0.000	0.000	0.000	0.000
24	A	30	LYS	1	0.952	0.961	29.238	9.509	9.509	0.000	0.000	0.000	0.000
25	A	31	GLY	0	0.045	0.030	32.039	-0.122	-0.122	0.000	0.000	0.000	0.000
26	A	32	ASN	0	0.065	0.022	32.017	0.046	0.046	0.000	0.000	0.000	0.000
27	A	33	ARG	1	0.912	0.973	23.481	11.328	11.328	0.000	0.000	0.000	0.000
28	A	34	SER	0	0.035	0.004	24.847	-0.042	-0.042	0.000	0.000	0.000	0.000
29	A	35	GLU	-1	-0.819	-0.852	21.524	-13.192	-13.192	0.000	0.000	0.000	0.000
30	A	36	TYR	0	-0.016	-0.013	17.930	0.236	0.236	0.000	0.000	0.000	0.000
31	A	37	ARG	1	0.854	0.889	18.007	12.730	12.730	0.000	0.000	0.000	0.000
32	A	38	VAL	0	0.012	0.018	12.562	0.259	0.259	0.000	0.000	0.000	0.000
33	A	39	VAL	0	0.001	-0.011	15.854	0.215	0.215	0.000	0.000	0.000	0.000
34	A	40	ILE	0	0.007	0.008	12.548	-0.658	-0.658	0.000	0.000	0.000	0.000
35	A	41	THR	0	-0.008	0.000	17.234	0.275	0.275	0.000	0.000	0.000	0.000
36	A	42	GLN	0	-0.025	-0.017	18.329	-0.211	-0.211	0.000	0.000	0.000	0.000
37	A	43	LYS	1	0.934	0.959	21.361	11.514	11.514	0.000	0.000	0.000	0.000
38	A	44	SER	0	-0.030	-0.004	21.898	0.385	0.385	0.000	0.000	0.000	0.000
39	A	45	GLU	-1	-0.772	-0.877	21.369	-13.130	-13.130	0.000	0.000	0.000	0.000
40	A	46	ASN	0	0.046	0.007	20.643	-1.060	-1.060	0.000	0.000	0.000	0.000
41	A	47	LEU	0	-0.025	0.010	16.740	-0.826	-0.826	0.000	0.000	0.000	0.000
42	A	48	ILE	0	0.059	0.018	16.391	-1.424	-1.424	0.000	0.000	0.000	0.000
43	A	49	LYS	1	0.948	0.965	16.061	14.027	14.027	0.000	0.000	0.000	0.000
44	A	50	GLN	0	-0.037	-0.028	16.738	0.179	0.179	0.000	0.000	0.000	0.000
45	A	51	HIS	0	0.017	0.044	11.008	-0.425	-0.425	0.000	0.000	0.000	0.000
46	A	52	ILE	0	0.026	0.012	11.794	-2.056	-2.056	0.000	0.000	0.000	0.000
47	A	53	ALA	0	0.017	0.002	11.443	-1.800	-1.800	0.000	0.000	0.000	0.000
48	A	54	PRO	0	0.004	0.001	11.588	-1.200	-1.200	0.000	0.000	0.000	0.000
49	A	55	LEU	0	-0.005	0.003	6.394	-2.843	-2.843	0.000	0.000	0.000	0.000
50	A	56	MET	0	0.014	0.011	6.957	-4.842	-4.842	0.000	0.000	0.000	0.000
51	A	57	GLN	0	-0.072	-0.044	9.032	0.430	0.430	0.000	0.000	0.000	0.000
54	A	60	ILE	0	-0.039	-0.030	5.530	1.173	1.173	0.000	0.000	0.000	0.000
55	A	61	ASP	-1	-0.845	-0.911	8.490	-23.751	-23.751	0.000	0.000	0.000	0.000
58	A	64	ASN	0	-0.007	-0.001	6.878	5.167	5.167	0.000	0.000	0.000	0.000
59	A	65	VAL	0	-0.061	-0.034	9.811	2.919	2.919	0.000	0.000	0.000	0.000
60	A	66	LYS	1	0.937	0.963	11.865	18.563	18.563	0.000	0.000	0.000	0.000
61	A	67	SER	0	-0.065	-0.045	14.865	0.842	0.842	0.000	0.000	0.000	0.000
62	A	68	LYS	1	0.962	0.973	14.630	16.686	16.686	0.000	0.000	0.000	0.000
63	A	69	ILE	0	0.018	0.019	12.391	0.303	0.303	0.000	0.000	0.000	0.000
64	A	70	GLN	0	-0.008	0.001	16.481	0.631	0.631	0.000	0.000	0.000	0.000
65	A	71	ILE	0	-0.010	-0.009	17.452	-0.486	-0.486	0.000	0.000	0.000	0.000
66	A	72	VAL	0	-0.018	-0.014	21.069	0.602	0.602	0.000	0.000	0.000	0.000
67	A	73	LYS	1	0.916	0.973	24.261	10.810	10.810	0.000	0.000	0.000	0.000
68	A	74	GLY	0	0.049	0.035	26.783	0.284	0.284	0.000	0.000	0.000	0.000
69	A	75	ASP	-1	-0.843	-0.922	28.577	-9.694	-9.694	0.000	0.000	0.000	0.000
70	A	76	THR	0	-0.059	-0.040	30.069	-0.354	-0.354	0.000	0.000	0.000	0.000
71	A	77	ARG	1	0.917	0.946	25.389	11.511	11.511	0.000	0.000	0.000	0.000
72	A	78	TYR	0	-0.015	-0.018	22.546	0.484	0.484	0.000	0.000	0.000	0.000
73	A	79	GLU	-1	-0.796	-0.871	20.914	-13.493	-13.493	0.000	0.000	0.000	0.000
74	A	80	LEU	0	-0.023	-0.008	14.086	0.095	0.095	0.000	0.000	0.000	0.000
75	A	81	ARG	1	0.842	0.896	17.944	12.904	12.904	0.000	0.000	0.000	0.000
76	A	82	VAL	0	0.066	0.024	12.777	-0.301	-0.301	0.000	0.000	0.000	0.000
77	A	83	SER	0	-0.009	-0.022	15.866	-0.262	-0.262	0.000	0.000	0.000	0.000
78	A	84	SER	0	0.019	0.021	12.774	0.282	0.282	0.000	0.000	0.000	0.000
79	A	85	LYS	1	0.973	0.984	14.867	14.824	14.824	0.000	0.000	0.000	0.000
80	A	86	LYS	1	0.947	0.974	11.595	18.422	18.422	0.000	0.000	0.000	0.000
81	A	87	LEU	0	0.062	0.035	8.410	-0.588	-0.588	0.000	0.000	0.000	0.000
82	A	88	TYR	0	0.030	0.006	11.137	-0.645	-0.645	0.000	0.000	0.000	0.000
83	A	89	TYR	0	-0.002	-0.009	13.834	-0.207	-0.207	0.000	0.000	0.000	0.000
85	A	91	PHE	0	0.035	-0.003	8.252	-0.747	-0.747	0.000	0.000	0.000	0.000
86	A	92	ALA	0	0.012	0.010	10.920	0.494	0.494	0.000	0.000	0.000	0.000
87	A	93	ASN	0	0.075	0.050	9.894	1.605	1.605	0.000	0.000	0.000	0.000
88	A	94	MET	0	-0.075	-0.036	7.020	-1.137	-1.137	0.000	0.000	0.000	0.000
89	A	95	LEU	0	-0.006	0.002	10.825	0.363	0.363	0.000	0.000	0.000	0.000
90	A	96	GLU	-1	-0.941	-0.968	14.307	-15.490	-15.490	0.000	0.000	0.000	0.000
91	A	97	ARG	1	0.872	0.913	12.545	19.255	19.255	0.000	0.000	0.000	0.000
92	A	98	ILE	0	0.034	0.035	13.298	-0.447	-0.447	0.000	0.000	0.000	0.000
93	A	99	ARG	1	0.917	0.939	14.324	14.404	14.404	0.000	0.000	0.000	0.000
94	A	100	LEU	0	-0.012	0.001	13.159	0.593	0.593	0.000	0.000	0.000	0.000
95	A	101	PHE	0	-0.024	0.010	10.514	-1.542	-1.542	0.000	0.000	0.000	0.000
96	A	102	ASN	0	0.062	0.036	8.157	1.694	1.694	0.000	0.000	0.000	0.000
97	A	103	MET	0	0.078	0.024	12.011	-0.628	-0.628	0.000	0.000	0.000	0.000
99	A	105	GLU	-1	-0.865	-0.925	6.864	-37.908	-37.908	0.000	0.000	0.000	0.000
100	A	106	GLN	0	-0.023	-0.022	9.718	1.455	1.455	0.000	0.000	0.000	0.000
101	A	107	ILE	0	0.031	0.023	11.943	0.447	0.447	0.000	0.000	0.000	0.000
102	A	108	ALA	0	-0.006	-0.003	8.284	0.589	0.589	0.000	0.000	0.000	0.000
103	A	109	PHE	0	0.026	0.010	10.221	0.929	0.929	0.000	0.000	0.000	0.000
104	A	110	ILE	0	-0.015	-0.004	12.591	1.363	1.363	0.000	0.000	0.000	0.000
105	A	111	LYS	1	0.927	0.985	10.990	23.731	23.731	0.000	0.000	0.000	0.000
106	A	112	GLY	0	0.009	-0.009	13.028	0.588	0.588	0.000	0.000	0.000	0.000
107	A	113	LEU	0	-0.004	-0.001	13.729	1.146	1.146	0.000	0.000	0.000	0.000
108	A	114	TYR	0	-0.070	-0.043	17.111	1.145	1.145	0.000	0.000	0.000	0.000
109	A	115	VAL	0	-0.107	-0.057	14.835	0.921	0.921	0.000	0.000	0.000	0.000
110	A	116	ALA	0	-0.026	0.012	17.415	0.518	0.518	0.000	0.000	0.000	0.000
111	A	117	GLU	-1	-0.877	-0.947	18.901	-12.415	-12.415	0.000	0.000	0.000	0.000
112	A	118	GLY	0	-0.006	0.011	21.041	0.656	0.656	0.000	0.000	0.000	0.000
113	A	119	ASP	-1	-0.811	-0.912	22.524	-11.332	-11.332	0.000	0.000	0.000	0.000
114	A	120	LYS	1	0.954	0.968	19.122	15.011	15.011	0.000	0.000	0.000	0.000
115	A	121	THR	0	-0.002	0.005	24.075	0.063	0.063	0.000	0.000	0.000	0.000
116	A	122	LEU	0	-0.017	0.008	22.531	0.190	0.190	0.000	0.000	0.000	0.000
117	A	123	LYS	1	0.990	1.001	26.482	9.502	9.502	0.000	0.000	0.000	0.000
118	A	124	ARG	1	0.779	0.873	28.782	10.410	10.410	0.000	0.000	0.000	0.000
119	A	125	LEU	0	0.042	0.028	23.943	-0.286	-0.286	0.000	0.000	0.000	0.000
120	A	126	ARG	1	0.917	0.970	25.268	10.747	10.747	0.000	0.000	0.000	0.000
121	A	127	ILE	0	0.026	0.012	19.779	-0.417	-0.417	0.000	0.000	0.000	0.000
122	A	128	TRP	0	0.034	0.019	23.515	0.705	0.705	0.000	0.000	0.000	0.000
123	A	129	ASN	0	0.019	-0.002	21.733	-0.392	-0.392	0.000	0.000	0.000	0.000
124	A	130	LYS	1	0.931	0.963	25.130	10.862	10.862	0.000	0.000	0.000	0.000
125	A	131	ASN	0	-0.016	0.000	22.145	0.669	0.669	0.000	0.000	0.000	0.000
126	A	132	LYS	1	0.906	0.940	24.611	9.981	9.981	0.000	0.000	0.000	0.000
127	A	133	ALA	0	0.038	0.011	24.594	-0.256	-0.256	0.000	0.000	0.000	0.000
128	A	134	LEU	0	-0.033	-0.009	17.904	-0.408	-0.408	0.000	0.000	0.000	0.000
129	A	135	LEU	0	0.026	0.010	21.037	-0.629	-0.629	0.000	0.000	0.000	0.000
130	A	136	GLU	-1	-0.817	-0.903	23.486	-11.027	-11.027	0.000	0.000	0.000	0.000
131	A	137	ILE	0	-0.044	-0.005	17.803	0.143	0.143	0.000	0.000	0.000	0.000
132	A	138	VAL	0	0.031	0.016	18.142	-0.378	-0.378	0.000	0.000	0.000	0.000
133	A	139	SER	0	-0.007	-0.024	20.419	-0.030	-0.030	0.000	0.000	0.000	0.000
134	A	140	ARG	1	0.948	0.972	22.667	12.508	12.508	0.000	0.000	0.000	0.000
135	A	141	TRP	0	0.040	0.011	14.684	-0.297	-0.297	0.000	0.000	0.000	0.000
136	A	142	LEU	0	-0.006	0.000	19.521	-0.115	-0.115	0.000	0.000	0.000	0.000
137	A	143	ASN	0	-0.040	-0.022	21.689	0.464	0.464	0.000	0.000	0.000	0.000
138	A	144	ASN	0	-0.025	-0.006	19.357	0.768	0.768	0.000	0.000	0.000	0.000
139	A	145	LEU	0	-0.015	0.002	16.981	-0.222	-0.222	0.000	0.000	0.000	0.000
140	A	146	GLY	0	0.031	0.030	21.421	0.183	0.183	0.000	0.000	0.000	0.000
141	A	147	VAL	0	-0.066	-0.030	21.871	0.542	0.542	0.000	0.000	0.000	0.000
142	A	148	ARG	1	0.890	0.904	24.879	10.257	10.257	0.000	0.000	0.000	0.000
143	A	149	ASN	0	-0.043	-0.012	25.325	-0.041	-0.041	0.000	0.000	0.000	0.000
144	A	150	THR	0	0.013	0.009	27.535	0.171	0.171	0.000	0.000	0.000	0.000
145	A	151	ILE	0	0.022	0.006	26.054	-0.355	-0.355	0.000	0.000	0.000	0.000
146	A	152	HIS	0	-0.038	-0.014	29.748	0.235	0.235	0.000	0.000	0.000	0.000
147	A	153	LEU	0	-0.015	-0.008	31.633	-0.317	-0.317	0.000	0.000	0.000	0.000
148	A	154	ASP	-1	-0.912	-0.951	32.072	-9.468	-9.468	0.000	0.000	0.000	0.000
149	A	155	ASP	-1	-0.775	-0.873	33.348	-8.675	-8.675	0.000	0.000	0.000	0.000
150	A	156	HIS	0	0.063	0.000	34.661	-0.138	-0.138	0.000	0.000	0.000	0.000
151	A	157	ARG	1	0.920	0.989	37.244	7.834	7.834	0.000	0.000	0.000	0.000
152	A	158	HIS	0	-0.072	-0.066	33.403	0.112	0.112	0.000	0.000	0.000	0.000
153	A	159	GLY	0	0.035	0.037	32.394	-0.309	-0.309	0.000	0.000	0.000	0.000
154	A	160	VAL	0	-0.031	-0.018	28.497	-0.435	-0.435	0.000	0.000	0.000	0.000
155	A	161	TYR	0	0.028	0.006	28.117	0.415	0.415	0.000	0.000	0.000	0.000
156	A	162	VAL	0	-0.014	-0.004	27.628	-0.474	-0.474	0.000	0.000	0.000	0.000
157	A	163	LEU	0	0.003	0.008	23.220	0.277	0.277	0.000	0.000	0.000	0.000
158	A	164	ASN	0	0.028	0.012	26.247	-0.055	-0.055	0.000	0.000	0.000	0.000
159	A	165	ILE	0	0.029	0.010	22.442	0.021	0.021	0.000	0.000	0.000	0.000
160	A	166	SER	0	-0.020	-0.008	26.528	0.497	0.497	0.000	0.000	0.000	0.000
161	A	167	LEU	0	0.021	-0.014	28.762	-0.238	-0.238	0.000	0.000	0.000	0.000
162	A	168	ARG	1	0.938	0.962	30.798	8.747	8.747	0.000	0.000	0.000	0.000
163	A	169	ASP	-1	-0.705	-0.801	26.325	-11.027	-11.027	0.000	0.000	0.000	0.000
164	A	170	ARG	1	0.893	0.943	25.550	10.230	10.230	0.000	0.000	0.000	0.000
165	A	171	ILE	0	0.029	0.010	24.389	-0.481	-0.481	0.000	0.000	0.000	0.000
166	A	172	LYS	1	0.890	0.940	23.483	11.020	11.020	0.000	0.000	0.000	0.000
167	A	173	PHE	0	0.010	0.012	19.351	-0.676	-0.676	0.000	0.000	0.000	0.000
168	A	174	VAL	0	-0.005	-0.020	19.484	-0.766	-0.766	0.000	0.000	0.000	0.000
169	A	175	HIS	0	0.005	0.007	18.808	-0.643	-0.643	0.000	0.000	0.000	0.000
170	A	176	THR	0	-0.022	-0.014	17.216	-0.305	-0.305	0.000	0.000	0.000	0.000
171	A	177	ILE	0	-0.101	-0.050	14.846	-1.132	-1.132	0.000	0.000	0.000	0.000
172	A	178	LEU	-1	-0.945	-0.964	14.053	-21.524	-21.524	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:VAL)