FMO DATABASE

FMODB ID: 4G1MN

Calculation Name: 1Q8C-A-Xray549

Preferred Name:

Target Type:

Ligand Name: chloride ion | iodide ion

Ligand 3-letter code: CL | IOD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1Q8C

Chain ID: A

ChEMBL ID:

UniProt ID: P47273

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	140
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1364925.608196
FMO2-HF: Nuclear repulsion	1308781.470403
FMO2-HF: Total energy	-56144.137793
FMO2-MP2: Total energy	-56311.44736

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:LEU)

Summations of interaction energy for fragment #1(A:12:LEU)

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.
-49.54	-36.814	11.206	-8.729	-15.202	-0.086

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.836 / q_NPA : 0.925

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	ARG	1	0.969	0.977	3.359	27.250	29.101	0.032	-0.916	-0.967	0.000
5	A	16	GLN	0	0.064	0.037	2.181	-16.917	-15.042	5.765	-3.236	-4.404	-0.030
6	A	17	ARG	1	0.790	0.894	2.722	50.024	52.432	1.186	-0.769	-2.825	-0.004
7	A	18	ARG	1	0.802	0.867	4.617	27.995	28.115	-0.001	-0.016	-0.103	0.000
39	A	50	GLU	-1	-0.920	-0.943	4.273	-33.295	-33.134	-0.001	-0.052	-0.107	0.000
40	A	51	ARG	1	0.847	0.929	2.509	10.312	12.913	2.182	-1.901	-2.882	-0.028
41	A	52	GLN	0	-0.030	-0.022	2.655	-19.889	-16.436	2.045	-1.820	-3.678	-0.024
42	A	53	LEU	0	0.019	0.021	4.351	-2.587	-2.463	-0.001	-0.014	-0.108	0.000
46	A	57	GLN	0	0.084	0.039	4.423	-1.846	-1.713	-0.001	-0.005	-0.128	0.000
4	A	15	THR	0	0.044	0.008	6.025	0.430	0.430	0.000	0.000	0.000	0.000
8	A	19	ILE	0	0.033	0.026	6.473	1.726	1.726	0.000	0.000	0.000	0.000
9	A	20	ALA	0	0.006	-0.001	4.818	2.238	2.238	0.000	0.000	0.000	0.000
10	A	21	VAL	0	0.007	0.003	6.850	1.859	1.859	0.000	0.000	0.000	0.000
11	A	22	VAL	0	0.004	0.000	9.577	1.655	1.655	0.000	0.000	0.000	0.000
12	A	23	GLU	-1	-0.871	-0.938	10.305	-17.348	-17.348	0.000	0.000	0.000	0.000
13	A	24	PHE	0	-0.025	0.003	10.936	1.115	1.115	0.000	0.000	0.000	0.000
14	A	25	ILE	0	0.013	0.001	12.685	1.266	1.266	0.000	0.000	0.000	0.000
15	A	26	PHE	0	0.008	-0.012	15.004	1.225	1.225	0.000	0.000	0.000	0.000
16	A	27	SER	0	-0.068	-0.038	15.272	0.864	0.864	0.000	0.000	0.000	0.000
17	A	28	LEU	0	0.018	0.001	16.414	0.832	0.832	0.000	0.000	0.000	0.000
18	A	29	LEU	0	-0.046	-0.025	18.995	0.777	0.777	0.000	0.000	0.000	0.000
19	A	30	PHE	0	-0.058	-0.010	19.684	0.695	0.695	0.000	0.000	0.000	0.000
20	A	31	PHE	0	-0.066	-0.028	21.410	0.529	0.529	0.000	0.000	0.000	0.000
21	A	32	LEU	0	-0.021	0.017	21.333	-0.054	-0.054	0.000	0.000	0.000	0.000
22	A	33	PRO	0	-0.027	-0.024	25.113	0.318	0.318	0.000	0.000	0.000	0.000
23	A	34	LYS	1	0.868	0.896	20.837	12.887	12.887	0.000	0.000	0.000	0.000
24	A	35	GLU	-1	-0.871	-0.936	24.102	-10.401	-10.401	0.000	0.000	0.000	0.000
25	A	36	ALA	0	0.008	0.003	22.096	-0.503	-0.503	0.000	0.000	0.000	0.000
26	A	37	GLU	-1	-0.890	-0.963	20.642	-12.225	-12.225	0.000	0.000	0.000	0.000
27	A	38	VAL	0	-0.022	-0.006	20.681	-0.383	-0.383	0.000	0.000	0.000	0.000
28	A	39	ILE	0	0.002	0.007	17.071	-0.561	-0.561	0.000	0.000	0.000	0.000
29	A	40	GLN	0	-0.058	-0.049	16.273	-1.145	-1.145	0.000	0.000	0.000	0.000
30	A	41	ALA	0	0.004	0.008	15.973	-0.862	-0.862	0.000	0.000	0.000	0.000
31	A	42	ASP	-1	-0.767	-0.867	16.581	-14.398	-14.398	0.000	0.000	0.000	0.000
32	A	43	PHE	0	-0.055	-0.041	8.361	-1.354	-1.354	0.000	0.000	0.000	0.000
33	A	44	LEU	0	-0.048	-0.031	11.630	-1.727	-1.727	0.000	0.000	0.000	0.000
34	A	45	GLU	-1	-0.939	-0.963	12.646	-15.118	-15.118	0.000	0.000	0.000	0.000
35	A	46	TYR	0	-0.042	-0.015	8.498	0.105	0.105	0.000	0.000	0.000	0.000
36	A	47	ASP	-1	-0.818	-0.896	6.804	-32.007	-32.007	0.000	0.000	0.000	0.000
37	A	48	THR	0	-0.052	-0.046	6.951	0.566	0.566	0.000	0.000	0.000	0.000
38	A	49	LYS	1	0.965	0.972	5.951	18.496	18.496	0.000	0.000	0.000	0.000
43	A	54	ASN	0	0.002	-0.006	5.701	2.691	2.691	0.000	0.000	0.000	0.000
44	A	55	GLU	-1	-0.773	-0.898	7.347	-20.282	-20.282	0.000	0.000	0.000	0.000
45	A	56	TRP	0	-0.067	-0.022	7.658	-0.466	-0.466	0.000	0.000	0.000	0.000
47	A	58	LYS	1	0.891	0.946	9.162	24.014	24.014	0.000	0.000	0.000	0.000
48	A	59	LEU	0	0.002	0.012	11.847	1.291	1.291	0.000	0.000	0.000	0.000
49	A	60	ILE	0	0.006	0.000	10.353	1.103	1.103	0.000	0.000	0.000	0.000
50	A	61	VAL	0	0.017	0.007	11.642	1.204	1.204	0.000	0.000	0.000	0.000
51	A	62	LYS	1	0.874	0.930	14.318	14.541	14.541	0.000	0.000	0.000	0.000
52	A	63	ALA	0	0.023	0.018	17.161	0.873	0.873	0.000	0.000	0.000	0.000
53	A	64	PHE	0	0.019	0.003	16.428	0.798	0.798	0.000	0.000	0.000	0.000
54	A	65	SER	0	-0.055	-0.024	18.216	0.875	0.875	0.000	0.000	0.000	0.000
55	A	66	GLU	-1	-0.804	-0.884	20.041	-12.536	-12.536	0.000	0.000	0.000	0.000
56	A	67	ASN	0	-0.097	-0.059	21.873	0.944	0.944	0.000	0.000	0.000	0.000
57	A	68	ILE	0	0.048	0.041	20.656	0.404	0.404	0.000	0.000	0.000	0.000
58	A	69	PHE	0	0.032	0.015	23.043	0.154	0.154	0.000	0.000	0.000	0.000
59	A	70	SER	0	0.012	-0.004	26.371	0.380	0.380	0.000	0.000	0.000	0.000
60	A	71	PHE	0	-0.065	-0.035	20.081	0.279	0.279	0.000	0.000	0.000	0.000
61	A	72	GLN	0	0.064	0.026	23.979	-0.057	-0.057	0.000	0.000	0.000	0.000
62	A	73	LYS	1	0.869	0.925	25.871	9.370	9.370	0.000	0.000	0.000	0.000
63	A	74	LYS	1	0.984	0.994	26.488	11.000	11.000	0.000	0.000	0.000	0.000
64	A	75	ILE	0	0.042	0.021	22.353	0.139	0.139	0.000	0.000	0.000	0.000
65	A	76	GLU	-1	-0.860	-0.903	26.944	-9.058	-9.058	0.000	0.000	0.000	0.000
66	A	77	GLU	-1	-0.926	-0.977	30.093	-8.798	-8.798	0.000	0.000	0.000	0.000
67	A	78	GLN	0	-0.032	-0.029	28.663	0.398	0.398	0.000	0.000	0.000	0.000
68	A	79	GLN	0	0.070	0.029	28.440	0.252	0.252	0.000	0.000	0.000	0.000
69	A	80	LEU	0	-0.007	0.010	31.128	0.232	0.232	0.000	0.000	0.000	0.000
70	A	81	LYS	1	0.955	0.981	33.904	8.707	8.707	0.000	0.000	0.000	0.000
71	A	82	ASN	0	-0.090	-0.042	31.027	-0.112	-0.112	0.000	0.000	0.000	0.000
72	A	83	GLN	0	0.011	-0.011	34.686	0.156	0.156	0.000	0.000	0.000	0.000
73	A	84	LEU	0	-0.033	-0.009	35.512	0.193	0.193	0.000	0.000	0.000	0.000
74	A	85	GLU	0	0.059	0.017	39.460	0.055	0.055	0.000	0.000	0.000	0.000
75	A	86	ILE	0	0.084	0.039	41.116	-0.071	-0.071	0.000	0.000	0.000	0.000
76	A	87	GLN	0	0.027	0.009	35.850	-0.337	-0.337	0.000	0.000	0.000	0.000
77	A	88	THR	0	0.018	-0.009	35.840	-0.279	-0.279	0.000	0.000	0.000	0.000
78	A	89	LYS	0	-0.079	-0.024	35.896	-0.156	-0.156	0.000	0.000	0.000	0.000
79	A	90	TYR	0	-0.021	-0.003	30.938	-0.103	-0.103	0.000	0.000	0.000	0.000
80	A	91	ASN	0	-0.028	-0.022	31.771	-0.325	-0.325	0.000	0.000	0.000	0.000
81	A	92	LYS	1	0.903	0.966	31.008	9.121	9.121	0.000	0.000	0.000	0.000
82	A	93	ILE	0	0.041	0.027	27.419	-0.016	-0.016	0.000	0.000	0.000	0.000
83	A	94	SER	0	-0.017	-0.012	30.796	0.357	0.357	0.000	0.000	0.000	0.000
84	A	95	GLY	0	0.007	0.024	31.173	-0.233	-0.233	0.000	0.000	0.000	0.000
85	A	96	LYS	1	0.930	0.961	32.642	7.913	7.913	0.000	0.000	0.000	0.000
86	A	97	LYS	1	0.857	0.915	29.871	9.441	9.441	0.000	0.000	0.000	0.000
87	A	98	ILE	0	0.085	0.046	24.553	-0.174	-0.174	0.000	0.000	0.000	0.000
88	A	99	ASP	-1	-0.801	-0.861	22.556	-12.367	-12.367	0.000	0.000	0.000	0.000
89	A	100	LEU	0	0.066	0.047	21.768	-0.178	-0.178	0.000	0.000	0.000	0.000
90	A	101	LEU	0	0.015	0.025	15.349	-0.417	-0.417	0.000	0.000	0.000	0.000
91	A	102	THR	0	-0.003	-0.050	18.007	-0.684	-0.684	0.000	0.000	0.000	0.000
92	A	103	THR	0	-0.035	-0.036	19.757	-0.223	-0.223	0.000	0.000	0.000	0.000
93	A	104	ALA	0	-0.001	0.000	15.986	-0.179	-0.179	0.000	0.000	0.000	0.000
94	A	105	VAL	0	-0.008	0.001	14.867	-0.902	-0.902	0.000	0.000	0.000	0.000
95	A	106	VAL	0	-0.005	-0.007	16.341	-0.387	-0.387	0.000	0.000	0.000	0.000
96	A	107	LEU	0	-0.007	-0.006	18.150	-0.065	-0.065	0.000	0.000	0.000	0.000
97	A	108	CYS	0	-0.046	0.013	11.621	-0.434	-0.434	0.000	0.000	0.000	0.000
98	A	109	ALA	0	0.038	0.021	14.968	-0.356	-0.356	0.000	0.000	0.000	0.000
99	A	110	LEU	0	0.022	0.005	16.338	0.191	0.191	0.000	0.000	0.000	0.000
100	A	111	SER	0	-0.031	-0.033	15.796	0.622	0.622	0.000	0.000	0.000	0.000
101	A	112	GLU	-1	-0.733	-0.822	11.973	-22.946	-22.946	0.000	0.000	0.000	0.000
102	A	113	GLN	0	-0.069	-0.034	15.361	0.622	0.622	0.000	0.000	0.000	0.000
103	A	114	LYS	1	0.857	0.936	18.594	12.959	12.959	0.000	0.000	0.000	0.000
104	A	115	ALA	0	-0.022	0.000	15.726	0.427	0.427	0.000	0.000	0.000	0.000
105	A	116	HIS	0	-0.040	-0.045	12.503	0.518	0.518	0.000	0.000	0.000	0.000
106	A	117	ASN	0	-0.036	-0.004	16.629	0.557	0.557	0.000	0.000	0.000	0.000
107	A	118	THR	0	-0.020	-0.027	14.064	0.399	0.399	0.000	0.000	0.000	0.000
108	A	119	ASP	-1	-0.743	-0.880	17.191	-12.955	-12.955	0.000	0.000	0.000	0.000
109	A	120	LYS	1	0.886	0.944	18.619	10.954	10.954	0.000	0.000	0.000	0.000
110	A	121	PRO	0	-0.008	-0.004	20.068	-0.265	-0.265	0.000	0.000	0.000	0.000
111	A	122	LEU	0	-0.013	0.014	13.256	-0.363	-0.363	0.000	0.000	0.000	0.000
112	A	123	LEU	0	-0.002	0.002	15.070	-0.831	-0.831	0.000	0.000	0.000	0.000
113	A	124	ILE	0	-0.011	-0.013	16.466	-0.203	-0.203	0.000	0.000	0.000	0.000
114	A	125	SER	0	-0.030	-0.021	16.879	-0.444	-0.444	0.000	0.000	0.000	0.000
115	A	126	GLU	-1	-0.809	-0.901	10.366	-26.694	-26.694	0.000	0.000	0.000	0.000
116	A	127	ALA	0	0.005	0.002	13.340	-0.770	-0.770	0.000	0.000	0.000	0.000
117	A	128	LEU	0	-0.031	-0.012	15.454	0.010	0.010	0.000	0.000	0.000	0.000
118	A	129	LEU	0	0.033	0.022	11.626	-0.195	-0.195	0.000	0.000	0.000	0.000
119	A	130	ILE	0	-0.037	-0.026	10.063	-1.171	-1.171	0.000	0.000	0.000	0.000
120	A	131	MET	0	-0.044	-0.017	13.155	0.266	0.266	0.000	0.000	0.000	0.000
121	A	132	ASP	-1	-0.874	-0.926	15.837	-15.511	-15.511	0.000	0.000	0.000	0.000
122	A	133	HIS	0	-0.091	-0.036	9.239	-1.540	-1.540	0.000	0.000	0.000	0.000
123	A	134	TYR	0	-0.042	-0.028	10.654	-0.309	-0.309	0.000	0.000	0.000	0.000
124	A	135	SER	0	-0.005	-0.009	15.215	0.893	0.893	0.000	0.000	0.000	0.000
125	A	136	GLN	0	-0.017	-0.011	18.133	1.066	1.066	0.000	0.000	0.000	0.000
126	A	137	GLY	0	0.018	0.018	20.334	0.633	0.633	0.000	0.000	0.000	0.000
127	A	138	ALA	0	-0.008	-0.009	22.111	0.531	0.531	0.000	0.000	0.000	0.000
128	A	139	GLU	-1	-0.875	-0.949	20.429	-13.756	-13.756	0.000	0.000	0.000	0.000
129	A	140	LYS	1	0.897	0.945	22.747	10.466	10.466	0.000	0.000	0.000	0.000
130	A	141	LYS	0	-0.101	-0.032	24.374	0.465	0.465	0.000	0.000	0.000	0.000
131	A	142	GLN	0	0.051	0.022	21.981	-0.134	-0.134	0.000	0.000	0.000	0.000
132	A	143	THR	0	0.055	0.034	18.440	0.343	0.343	0.000	0.000	0.000	0.000
133	A	144	HIS	0	-0.012	-0.021	21.315	0.097	0.097	0.000	0.000	0.000	0.000
134	A	145	ALA	0	0.011	0.015	24.900	-0.077	-0.077	0.000	0.000	0.000	0.000
135	A	146	LEU	0	-0.081	-0.042	26.251	0.260	0.260	0.000	0.000	0.000	0.000
136	A	147	LEU	0	-0.053	-0.018	24.544	0.302	0.302	0.000	0.000	0.000	0.000
137	A	148	ASP	-1	-0.816	-0.905	20.416	-14.335	-14.335	0.000	0.000	0.000	0.000
138	A	149	LYS	1	0.825	0.904	22.455	13.567	13.567	0.000	0.000	0.000	0.000
139	A	150	LEU	0	-0.053	-0.034	23.409	-0.569	-0.569	0.000	0.000	0.000	0.000
140	A	151	LEU	-1	-0.937	-0.954	21.657	-10.854	-10.854	0.000	0.000	0.000	0.000

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