FMO DATABASE

FMODB ID: 2MYMR

Calculation Name: 5C9F-A-Xray547

Preferred Name:

Target Type:

Ligand Name: chloride ion

Ligand 3-letter code: CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5C9F

Chain ID: A

ChEMBL ID:

UniProt ID: Q92FY8

Base Structure: X-ray

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	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1099187.813317
FMO2-HF: Nuclear repulsion	1048129.705559
FMO2-HF: Total energy	-51058.107758
FMO2-MP2: Total energy	-51208.716242

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:104:MET)

Summations of interaction energy for fragment #1(A:104:MET)

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.
43.842	46.604	0.167	-1.416	-1.512	-0.008

Interaction energy analysis for fragmet #1(A:104:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.857 / q_NPA : 0.917

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	106	LYS	1	0.973	0.975	3.026	28.104	30.819	0.168	-1.412	-1.471	-0.008
4	A	107	TRP	0	0.007	0.008	5.020	1.814	1.861	-0.001	-0.004	-0.041	0.000
5	A	108	SER	0	-0.070	-0.063	8.812	-1.136	-1.136	0.000	0.000	0.000	0.000
6	A	109	THR	0	-0.022	-0.024	11.592	0.633	0.633	0.000	0.000	0.000	0.000
7	A	110	GLU	-1	-0.783	-0.854	15.394	-13.564	-13.564	0.000	0.000	0.000	0.000
8	A	111	VAL	0	-0.044	-0.037	17.915	0.523	0.523	0.000	0.000	0.000	0.000
9	A	112	GLY	0	0.047	0.029	20.430	-0.053	-0.053	0.000	0.000	0.000	0.000
10	A	113	GLU	-1	-0.977	-0.993	23.455	-10.532	-10.532	0.000	0.000	0.000	0.000
11	A	114	ILE	0	-0.012	-0.007	27.246	0.024	0.024	0.000	0.000	0.000	0.000
12	A	115	ILE	0	0.016	0.013	30.369	0.163	0.163	0.000	0.000	0.000	0.000
13	A	116	ILE	0	-0.050	-0.022	33.519	0.041	0.041	0.000	0.000	0.000	0.000
14	A	117	ALA	0	0.036	0.016	36.771	0.073	0.073	0.000	0.000	0.000	0.000
15	A	118	ARG	1	0.763	0.875	40.226	6.786	6.786	0.000	0.000	0.000	0.000
16	A	119	ASN	0	-0.022	-0.007	43.350	0.168	0.168	0.000	0.000	0.000	0.000
17	A	120	ARG	1	0.979	0.974	45.607	6.322	6.322	0.000	0.000	0.000	0.000
18	A	121	ASP	-1	-0.771	-0.853	47.797	-6.438	-6.438	0.000	0.000	0.000	0.000
19	A	122	GLY	0	0.032	0.013	48.783	0.063	0.063	0.000	0.000	0.000	0.000
20	A	123	HIS	1	0.875	0.946	45.411	6.364	6.364	0.000	0.000	0.000	0.000
21	A	124	PHE	0	0.049	0.026	40.074	-0.016	-0.016	0.000	0.000	0.000	0.000
22	A	125	TYR	0	-0.061	-0.070	40.574	0.029	0.029	0.000	0.000	0.000	0.000
23	A	126	ILE	0	0.032	0.018	34.194	-0.131	-0.131	0.000	0.000	0.000	0.000
24	A	127	ASN	0	-0.063	-0.033	35.207	0.275	0.275	0.000	0.000	0.000	0.000
25	A	128	ALA	0	0.040	0.024	32.822	-0.248	-0.248	0.000	0.000	0.000	0.000
26	A	129	PHE	0	-0.002	0.000	30.392	0.275	0.275	0.000	0.000	0.000	0.000
27	A	130	VAL	0	0.012	0.012	31.452	-0.301	-0.301	0.000	0.000	0.000	0.000
28	A	131	ASN	0	0.007	-0.017	32.314	-0.067	-0.067	0.000	0.000	0.000	0.000
29	A	132	ASN	0	0.013	0.006	30.080	-0.141	-0.141	0.000	0.000	0.000	0.000
30	A	133	VAL	0	0.024	0.021	32.085	0.086	0.086	0.000	0.000	0.000	0.000
31	A	134	LYS	1	0.932	0.981	35.418	8.015	8.015	0.000	0.000	0.000	0.000
32	A	135	ILE	0	-0.009	-0.003	36.313	0.275	0.275	0.000	0.000	0.000	0.000
33	A	136	LYS	1	0.937	0.977	37.502	6.890	6.890	0.000	0.000	0.000	0.000
34	A	137	PHE	0	0.027	0.006	36.662	0.129	0.129	0.000	0.000	0.000	0.000
35	A	138	MET	0	-0.001	0.003	40.515	0.003	0.003	0.000	0.000	0.000	0.000
36	A	139	VAL	0	-0.041	-0.031	38.726	-0.103	-0.103	0.000	0.000	0.000	0.000
37	A	140	ASP	-1	-0.845	-0.932	41.330	-6.661	-6.661	0.000	0.000	0.000	0.000
38	A	141	THR	0	-0.009	-0.022	41.215	-0.104	-0.104	0.000	0.000	0.000	0.000
39	A	142	GLY	0	0.013	0.018	43.394	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	143	ALA	0	-0.014	0.012	43.466	0.064	0.064	0.000	0.000	0.000	0.000
41	A	144	SER	0	0.058	0.031	42.297	-0.149	-0.149	0.000	0.000	0.000	0.000
42	A	145	ASP	-1	-0.830	-0.866	40.179	-7.622	-7.622	0.000	0.000	0.000	0.000
43	A	146	ILE	0	0.001	0.004	36.380	0.151	0.151	0.000	0.000	0.000	0.000
44	A	147	ALA	0	-0.023	0.003	40.874	0.090	0.090	0.000	0.000	0.000	0.000
45	A	148	LEU	0	0.013	-0.002	40.166	-0.072	-0.072	0.000	0.000	0.000	0.000
46	A	149	THR	0	0.052	0.023	44.190	0.156	0.156	0.000	0.000	0.000	0.000
47	A	150	LYS	1	0.890	0.923	46.096	5.809	5.809	0.000	0.000	0.000	0.000
48	A	151	GLU	-1	-0.872	-0.922	46.444	-6.591	-6.591	0.000	0.000	0.000	0.000
49	A	152	ASP	-1	-0.759	-0.881	42.050	-7.374	-7.374	0.000	0.000	0.000	0.000
50	A	153	ALA	0	-0.024	-0.015	42.254	-0.188	-0.188	0.000	0.000	0.000	0.000
51	A	154	GLN	0	-0.006	-0.012	43.426	-0.072	-0.072	0.000	0.000	0.000	0.000
52	A	155	LYS	1	0.857	0.936	40.650	7.363	7.363	0.000	0.000	0.000	0.000
53	A	156	LEU	0	-0.071	-0.030	37.170	-0.198	-0.198	0.000	0.000	0.000	0.000
54	A	157	GLY	0	0.007	0.014	39.998	-0.145	-0.145	0.000	0.000	0.000	0.000
55	A	158	PHE	0	-0.060	-0.031	39.547	0.044	0.044	0.000	0.000	0.000	0.000
56	A	159	ASP	-1	-0.778	-0.873	44.204	-6.249	-6.249	0.000	0.000	0.000	0.000
57	A	160	LEU	0	0.009	-0.023	47.574	0.016	0.016	0.000	0.000	0.000	0.000
58	A	161	THR	0	-0.071	-0.049	49.826	0.090	0.090	0.000	0.000	0.000	0.000
59	A	162	LYS	1	0.912	0.962	48.116	6.375	6.375	0.000	0.000	0.000	0.000
60	A	163	LEU	0	-0.054	-0.004	45.363	-0.078	-0.078	0.000	0.000	0.000	0.000
61	A	164	LYS	1	1.010	1.006	47.447	6.894	6.894	0.000	0.000	0.000	0.000
62	A	165	TYR	0	0.034	0.013	50.077	-0.105	-0.105	0.000	0.000	0.000	0.000
63	A	166	THR	0	-0.028	-0.032	49.506	0.109	0.109	0.000	0.000	0.000	0.000
64	A	167	ARG	1	0.869	0.956	46.613	6.747	6.747	0.000	0.000	0.000	0.000
65	A	168	THR	0	0.040	0.010	50.828	0.045	0.045	0.000	0.000	0.000	0.000
66	A	169	TYR	0	-0.094	-0.076	44.953	-0.113	-0.113	0.000	0.000	0.000	0.000
67	A	170	LEU	0	0.046	0.030	51.586	0.103	0.103	0.000	0.000	0.000	0.000
68	A	171	THR	0	-0.002	-0.004	51.571	-0.160	-0.160	0.000	0.000	0.000	0.000
69	A	172	ALA	0	0.009	0.003	53.734	0.084	0.084	0.000	0.000	0.000	0.000
70	A	173	ASN	0	-0.022	-0.014	55.760	0.139	0.139	0.000	0.000	0.000	0.000
71	A	174	GLY	0	0.028	0.023	57.279	0.088	0.088	0.000	0.000	0.000	0.000
72	A	175	GLU	-1	-0.943	-0.982	56.093	-5.664	-5.664	0.000	0.000	0.000	0.000
73	A	176	ASN	0	-0.038	-0.020	53.475	0.134	0.134	0.000	0.000	0.000	0.000
74	A	177	LYS	1	0.862	0.928	53.385	5.730	5.730	0.000	0.000	0.000	0.000
75	A	178	ALA	0	0.002	-0.023	48.678	-0.021	-0.021	0.000	0.000	0.000	0.000
76	A	179	ALA	0	-0.008	0.020	48.104	0.033	0.033	0.000	0.000	0.000	0.000
77	A	180	PRO	0	-0.050	-0.026	44.153	-0.105	-0.105	0.000	0.000	0.000	0.000
78	A	181	ILE	0	0.009	0.010	40.984	0.023	0.023	0.000	0.000	0.000	0.000
79	A	182	THR	0	-0.083	-0.051	35.581	-0.115	-0.115	0.000	0.000	0.000	0.000
80	A	183	LEU	0	0.010	0.015	35.159	0.049	0.049	0.000	0.000	0.000	0.000
81	A	184	ASN	0	0.027	0.010	31.836	-0.147	-0.147	0.000	0.000	0.000	0.000
82	A	185	SER	0	-0.035	-0.045	28.016	-0.339	-0.339	0.000	0.000	0.000	0.000
83	A	186	VAL	0	0.018	0.004	29.829	0.407	0.407	0.000	0.000	0.000	0.000
84	A	187	VAL	0	0.012	0.011	26.294	-0.274	-0.274	0.000	0.000	0.000	0.000
85	A	188	ILE	0	-0.009	-0.017	28.304	0.429	0.429	0.000	0.000	0.000	0.000
86	A	189	GLY	0	0.049	0.035	26.214	-0.065	-0.065	0.000	0.000	0.000	0.000
87	A	190	LYS	1	0.907	0.967	23.113	12.511	12.511	0.000	0.000	0.000	0.000
88	A	191	GLU	-1	-0.802	-0.867	23.842	-11.416	-11.416	0.000	0.000	0.000	0.000
89	A	192	PHE	0	-0.055	-0.028	25.323	-0.383	-0.383	0.000	0.000	0.000	0.000
90	A	193	LYS	1	0.862	0.914	25.665	11.925	11.925	0.000	0.000	0.000	0.000
91	A	194	ASN	0	-0.021	-0.019	29.276	0.159	0.159	0.000	0.000	0.000	0.000
92	A	195	ILE	0	-0.012	0.012	31.473	0.129	0.129	0.000	0.000	0.000	0.000
93	A	196	LYS	1	0.976	0.983	34.583	8.061	8.061	0.000	0.000	0.000	0.000
94	A	197	GLY	0	0.070	0.030	38.174	-0.046	-0.046	0.000	0.000	0.000	0.000
95	A	198	HIS	1	0.803	0.892	41.023	7.145	7.145	0.000	0.000	0.000	0.000
96	A	199	VAL	0	0.043	0.041	44.612	-0.029	-0.029	0.000	0.000	0.000	0.000
97	A	200	GLY	0	0.049	0.023	46.852	0.085	0.085	0.000	0.000	0.000	0.000
98	A	201	LEU	0	0.037	-0.004	50.430	-0.021	-0.021	0.000	0.000	0.000	0.000
99	A	202	GLY	0	-0.059	-0.043	53.414	0.065	0.065	0.000	0.000	0.000	0.000
100	A	203	ASP	-1	-0.809	-0.858	53.767	-5.742	-5.742	0.000	0.000	0.000	0.000
101	A	204	LEU	0	-0.068	-0.035	46.525	-0.041	-0.041	0.000	0.000	0.000	0.000
102	A	205	ASP	-1	-0.904	-0.936	50.523	-6.136	-6.136	0.000	0.000	0.000	0.000
103	A	206	ILE	0	0.016	-0.009	43.792	-0.093	-0.093	0.000	0.000	0.000	0.000
104	A	207	SER	0	-0.015	-0.020	42.258	0.046	0.046	0.000	0.000	0.000	0.000
105	A	208	LEU	0	-0.030	-0.009	43.053	-0.069	-0.069	0.000	0.000	0.000	0.000
106	A	209	LEU	0	-0.035	-0.024	35.149	-0.120	-0.120	0.000	0.000	0.000	0.000
107	A	210	GLY	0	0.060	0.028	39.691	0.074	0.074	0.000	0.000	0.000	0.000
108	A	211	MET	0	0.046	0.010	38.254	-0.259	-0.259	0.000	0.000	0.000	0.000
109	A	212	SER	0	-0.036	-0.036	36.954	-0.218	-0.218	0.000	0.000	0.000	0.000
110	A	213	LEU	0	-0.081	-0.039	31.581	-0.274	-0.274	0.000	0.000	0.000	0.000
111	A	214	LEU	0	0.012	0.006	33.012	-0.312	-0.312	0.000	0.000	0.000	0.000
112	A	215	GLU	-1	-0.912	-0.965	33.453	-8.592	-8.592	0.000	0.000	0.000	0.000
113	A	216	ARG	1	0.862	0.944	29.587	9.639	9.639	0.000	0.000	0.000	0.000
114	A	217	PHE	0	-0.030	-0.013	28.486	-0.499	-0.499	0.000	0.000	0.000	0.000
115	A	218	LYS	1	0.891	0.951	23.446	12.722	12.722	0.000	0.000	0.000	0.000
116	A	219	GLY	0	0.033	0.013	27.712	0.090	0.090	0.000	0.000	0.000	0.000
117	A	220	PHE	0	0.029	0.013	30.718	-0.053	-0.053	0.000	0.000	0.000	0.000
118	A	221	ARG	1	0.953	0.981	33.951	8.286	8.286	0.000	0.000	0.000	0.000
119	A	222	ILE	0	0.026	0.016	36.703	-0.026	-0.026	0.000	0.000	0.000	0.000
120	A	223	ASP	-1	-0.886	-0.950	39.130	-7.418	-7.418	0.000	0.000	0.000	0.000
121	A	224	LYS	1	0.868	0.930	40.762	6.977	6.977	0.000	0.000	0.000	0.000
122	A	225	ASP	-1	-0.811	-0.882	42.669	-6.743	-6.743	0.000	0.000	0.000	0.000
123	A	226	LEU	0	0.005	0.009	36.884	-0.052	-0.052	0.000	0.000	0.000	0.000
124	A	227	LEU	0	-0.018	-0.007	35.952	0.077	0.077	0.000	0.000	0.000	0.000
125	A	228	ILE	0	-0.003	-0.008	31.835	-0.105	-0.105	0.000	0.000	0.000	0.000
126	A	229	LEU	0	-0.019	-0.003	30.936	0.084	0.084	0.000	0.000	0.000	0.000
127	A	230	ASN	0	0.027	0.011	27.012	0.049	0.049	0.000	0.000	0.000	0.000
128	A	231	TYR	0	-0.080	-0.068	22.232	0.389	0.389	0.000	0.000	0.000	0.000
129	A	232	ALA	0	0.038	0.010	20.509	-0.282	-0.282	0.000	0.000	0.000	0.000
130	A	233	ALA	0	-0.031	-0.010	19.793	0.525	0.525	0.000	0.000	0.000	0.000
131	A	234	ALA	0	-0.004	-0.002	15.146	-0.370	-0.370	0.000	0.000	0.000	0.000
132	A	235	LEU	-1	-0.850	-0.884	11.401	-18.775	-18.775	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:104:MET)