FMO DATABASE

FMODB ID: 3M2JL

Calculation Name: 6F2C-A-Xray547

Preferred Name:

Target Type:

Ligand Name: chloride ion

Ligand 3-letter code: CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6F2C

Chain ID: A

ChEMBL ID:

UniProt ID: P42980

Base Structure: X-ray

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
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	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1039502.696162
FMO2-HF: Nuclear repulsion	992009.998615
FMO2-HF: Total energy	-47492.697547
FMO2-MP2: Total energy	-47631.28591

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:-2:SER)

Summations of interaction energy for fragment #1(A:-2:SER)

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.
-124.618	-119.908	0.566	-2.291	-2.987	-0.006

Interaction energy analysis for fragmet #1(A:-2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.826 / q_NPA : 0.893

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	0	VAL	0	0.011	0.045	2.566	0.458	5.034	0.567	-2.272	-2.872	-0.006
4	A	1	MET	0	-0.026	-0.009	4.117	-1.210	-1.076	-0.001	-0.019	-0.115	0.000
5	A	2	LYS	1	0.866	0.928	5.709	34.773	34.773	0.000	0.000	0.000	0.000
6	A	3	ILE	0	0.008	0.004	9.247	1.989	1.989	0.000	0.000	0.000	0.000
7	A	4	ALA	0	0.000	0.005	12.721	0.622	0.622	0.000	0.000	0.000	0.000
8	A	5	LEU	0	-0.008	-0.009	15.754	0.493	0.493	0.000	0.000	0.000	0.000
9	A	6	ILE	0	-0.018	-0.012	18.827	0.466	0.466	0.000	0.000	0.000	0.000
10	A	7	ALA	0	0.023	0.006	22.442	0.124	0.124	0.000	0.000	0.000	0.000
11	A	8	HIS	0	0.036	0.033	25.729	0.366	0.366	0.000	0.000	0.000	0.000
12	A	9	ASP	-1	-0.806	-0.903	29.377	-9.859	-9.859	0.000	0.000	0.000	0.000
13	A	10	LYS	1	0.855	0.920	31.467	8.183	8.183	0.000	0.000	0.000	0.000
14	A	11	LYS	1	0.875	0.953	28.082	10.059	10.059	0.000	0.000	0.000	0.000
15	A	12	LYS	1	0.814	0.892	26.792	10.463	10.463	0.000	0.000	0.000	0.000
16	A	13	GLN	0	0.027	0.018	26.807	-0.340	-0.340	0.000	0.000	0.000	0.000
17	A	14	ASP	-1	-0.851	-0.927	27.259	-10.532	-10.532	0.000	0.000	0.000	0.000
18	A	15	MET	0	0.026	0.010	21.214	-0.515	-0.515	0.000	0.000	0.000	0.000
19	A	16	VAL	0	-0.013	0.015	22.705	-0.571	-0.571	0.000	0.000	0.000	0.000
20	A	17	GLN	0	-0.034	-0.004	23.987	-0.420	-0.420	0.000	0.000	0.000	0.000
21	A	18	PHE	0	0.040	0.005	18.245	-0.201	-0.201	0.000	0.000	0.000	0.000
22	A	19	THR	0	0.003	-0.030	18.470	-0.450	-0.450	0.000	0.000	0.000	0.000
23	A	20	THR	0	-0.032	-0.026	19.294	-0.559	-0.559	0.000	0.000	0.000	0.000
24	A	21	ALA	0	-0.050	-0.024	21.327	-0.258	-0.258	0.000	0.000	0.000	0.000
25	A	22	TYR	0	0.032	0.007	17.628	0.013	0.013	0.000	0.000	0.000	0.000
26	A	23	ARG	1	0.874	0.942	16.299	15.607	15.607	0.000	0.000	0.000	0.000
27	A	24	ASP	-1	-0.920	-0.984	15.226	-18.336	-18.336	0.000	0.000	0.000	0.000
28	A	25	ILE	0	0.042	0.037	12.774	-1.333	-1.333	0.000	0.000	0.000	0.000
29	A	26	LEU	0	-0.005	-0.018	11.682	-1.941	-1.941	0.000	0.000	0.000	0.000
30	A	27	LYS	1	0.803	0.906	11.453	22.332	22.332	0.000	0.000	0.000	0.000
31	A	28	ASN	0	-0.076	-0.021	8.036	-0.197	-0.197	0.000	0.000	0.000	0.000
32	A	29	HIS	0	0.015	-0.009	6.634	-6.617	-6.617	0.000	0.000	0.000	0.000
33	A	30	ASP	-1	-0.884	-0.929	6.595	-34.260	-34.260	0.000	0.000	0.000	0.000
34	A	31	LEU	0	-0.029	-0.013	8.924	1.836	1.836	0.000	0.000	0.000	0.000
35	A	32	TYR	0	0.044	0.020	10.352	0.441	0.441	0.000	0.000	0.000	0.000
36	A	33	ALA	0	0.001	-0.005	15.452	0.533	0.533	0.000	0.000	0.000	0.000
37	A	34	THR	0	0.008	0.018	19.200	0.245	0.245	0.000	0.000	0.000	0.000
38	A	35	GLY	0	0.010	0.001	22.666	0.403	0.403	0.000	0.000	0.000	0.000
39	A	36	THR	0	-0.038	-0.030	24.322	-0.417	-0.417	0.000	0.000	0.000	0.000
40	A	37	THR	0	0.011	0.016	22.390	0.264	0.264	0.000	0.000	0.000	0.000
41	A	38	GLY	0	0.075	0.032	20.513	-0.215	-0.215	0.000	0.000	0.000	0.000
42	A	39	LEU	0	-0.067	-0.015	21.182	-0.265	-0.265	0.000	0.000	0.000	0.000
43	A	40	LYS	1	0.869	0.915	23.904	10.612	10.612	0.000	0.000	0.000	0.000
44	A	41	ILE	0	0.044	0.027	18.427	0.155	0.155	0.000	0.000	0.000	0.000
45	A	42	HIS	0	-0.048	-0.004	18.801	0.477	0.477	0.000	0.000	0.000	0.000
46	A	43	GLU	-1	-0.858	-0.941	21.113	-10.794	-10.794	0.000	0.000	0.000	0.000
47	A	44	ALA	0	-0.031	-0.005	23.628	0.237	0.237	0.000	0.000	0.000	0.000
48	A	45	THR	0	-0.012	-0.010	19.531	-0.310	-0.310	0.000	0.000	0.000	0.000
49	A	46	GLY	0	0.038	0.022	19.921	-0.441	-0.441	0.000	0.000	0.000	0.000
50	A	47	LEU	0	-0.034	-0.007	14.280	-0.767	-0.767	0.000	0.000	0.000	0.000
51	A	48	GLN	0	-0.011	-0.004	13.089	1.562	1.562	0.000	0.000	0.000	0.000
52	A	49	ILE	0	-0.027	-0.017	13.905	-0.677	-0.677	0.000	0.000	0.000	0.000
53	A	50	GLU	-1	-0.871	-0.923	14.011	-17.393	-17.393	0.000	0.000	0.000	0.000
54	A	51	ARG	1	0.818	0.891	15.934	13.544	13.544	0.000	0.000	0.000	0.000
55	A	52	PHE	0	0.038	0.026	16.430	0.378	0.378	0.000	0.000	0.000	0.000
56	A	53	GLN	0	0.037	0.014	21.527	0.560	0.560	0.000	0.000	0.000	0.000
57	A	54	SER	0	0.033	-0.002	24.618	-0.343	-0.343	0.000	0.000	0.000	0.000
58	A	55	GLY	0	0.019	0.018	26.649	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	56	PRO	0	-0.015	-0.025	27.533	0.026	0.026	0.000	0.000	0.000	0.000
60	A	57	LEU	0	-0.031	-0.001	29.131	0.290	0.290	0.000	0.000	0.000	0.000
61	A	58	GLY	0	0.067	0.034	27.418	-0.147	-0.147	0.000	0.000	0.000	0.000
62	A	59	GLY	0	-0.032	-0.011	23.780	-0.380	-0.380	0.000	0.000	0.000	0.000
63	A	60	ASP	-1	-0.780	-0.926	22.523	-12.226	-12.226	0.000	0.000	0.000	0.000
64	A	61	GLN	0	-0.037	-0.036	22.925	-0.474	-0.474	0.000	0.000	0.000	0.000
65	A	62	GLN	0	-0.011	0.002	20.598	-0.190	-0.190	0.000	0.000	0.000	0.000
66	A	63	ILE	0	0.028	0.015	17.362	-0.659	-0.659	0.000	0.000	0.000	0.000
67	A	64	GLY	0	0.032	0.008	18.268	-0.567	-0.567	0.000	0.000	0.000	0.000
68	A	65	ALA	0	-0.019	-0.020	19.868	-0.218	-0.218	0.000	0.000	0.000	0.000
69	A	66	LEU	0	0.000	0.001	13.883	-0.296	-0.296	0.000	0.000	0.000	0.000
70	A	67	ILE	0	-0.005	0.004	15.128	-0.835	-0.835	0.000	0.000	0.000	0.000
71	A	68	ALA	0	-0.021	-0.010	16.826	-0.285	-0.285	0.000	0.000	0.000	0.000
72	A	69	ALA	0	-0.053	-0.018	15.677	0.167	0.167	0.000	0.000	0.000	0.000
73	A	70	ASN	0	-0.070	-0.037	13.279	-0.702	-0.702	0.000	0.000	0.000	0.000
74	A	71	ALA	0	0.003	0.004	10.714	-1.706	-1.706	0.000	0.000	0.000	0.000
75	A	72	LEU	0	-0.049	-0.036	10.817	-0.805	-0.805	0.000	0.000	0.000	0.000
76	A	73	ASP	-1	-0.807	-0.887	8.092	-30.325	-30.325	0.000	0.000	0.000	0.000
77	A	74	LEU	0	-0.023	-0.006	11.351	0.815	0.815	0.000	0.000	0.000	0.000
78	A	75	VAL	0	-0.010	0.001	14.154	0.033	0.033	0.000	0.000	0.000	0.000
79	A	76	ILE	0	0.008	0.008	17.334	0.760	0.760	0.000	0.000	0.000	0.000
80	A	77	PHE	0	0.025	0.002	19.844	0.250	0.250	0.000	0.000	0.000	0.000
81	A	78	LEU	0	0.012	0.012	23.021	0.583	0.583	0.000	0.000	0.000	0.000
82	A	79	ARG	1	0.968	0.971	25.819	10.475	10.475	0.000	0.000	0.000	0.000
83	A	80	ASP	-1	-0.811	-0.905	28.429	-8.904	-8.904	0.000	0.000	0.000	0.000
84	A	81	PRO	0	-0.062	-0.026	31.866	0.123	0.123	0.000	0.000	0.000	0.000
85	A	82	LEU	0	-0.011	-0.007	34.306	0.262	0.262	0.000	0.000	0.000	0.000
86	A	83	THR	0	-0.062	-0.055	35.752	0.351	0.351	0.000	0.000	0.000	0.000
87	A	84	ALA	0	0.006	0.012	35.862	-0.224	-0.224	0.000	0.000	0.000	0.000
88	A	85	GLN	0	-0.002	-0.005	31.954	-0.054	-0.054	0.000	0.000	0.000	0.000
89	A	86	PRO	0	-0.012	-0.005	34.185	0.097	0.097	0.000	0.000	0.000	0.000
90	A	87	HIS	0	0.002	-0.003	28.305	0.409	0.409	0.000	0.000	0.000	0.000
91	A	88	GLU	-1	-0.863	-0.913	31.243	-9.234	-9.234	0.000	0.000	0.000	0.000
92	A	89	PRO	0	0.048	0.029	31.585	-0.252	-0.252	0.000	0.000	0.000	0.000
93	A	90	ASP	-1	-0.833	-0.912	27.923	-10.230	-10.230	0.000	0.000	0.000	0.000
94	A	91	VAL	0	-0.059	-0.025	27.134	-0.463	-0.463	0.000	0.000	0.000	0.000
95	A	92	SER	0	-0.025	-0.044	27.169	-0.432	-0.432	0.000	0.000	0.000	0.000
96	A	93	ALA	0	-0.060	-0.028	27.717	-0.168	-0.168	0.000	0.000	0.000	0.000
97	A	94	LEU	0	-0.012	-0.001	20.586	-0.286	-0.286	0.000	0.000	0.000	0.000
98	A	95	ILE	0	-0.002	-0.002	23.120	-0.471	-0.471	0.000	0.000	0.000	0.000
99	A	96	ARG	1	0.993	1.005	24.159	10.575	10.575	0.000	0.000	0.000	0.000
100	A	97	LEU	0	-0.050	-0.016	21.196	0.018	0.018	0.000	0.000	0.000	0.000
101	A	98	CYS	0	-0.025	-0.016	19.860	-0.686	-0.686	0.000	0.000	0.000	0.000
102	A	99	ASP	-1	-0.878	-0.936	20.634	-12.453	-12.453	0.000	0.000	0.000	0.000
103	A	100	VAL	0	-0.101	-0.050	22.661	-0.022	-0.022	0.000	0.000	0.000	0.000
104	A	101	TYR	0	-0.022	-0.016	17.816	0.200	0.200	0.000	0.000	0.000	0.000
105	A	102	SER	0	-0.047	-0.016	18.266	-0.604	-0.604	0.000	0.000	0.000	0.000
106	A	103	ILE	0	-0.015	0.000	14.822	-0.617	-0.617	0.000	0.000	0.000	0.000
107	A	104	PRO	0	0.001	0.001	14.823	0.960	0.960	0.000	0.000	0.000	0.000
108	A	105	LEU	0	0.039	0.020	17.357	-0.373	-0.373	0.000	0.000	0.000	0.000
109	A	106	ALA	0	0.003	0.011	20.195	0.461	0.461	0.000	0.000	0.000	0.000
110	A	107	THR	0	-0.004	-0.007	22.453	0.088	0.088	0.000	0.000	0.000	0.000
111	A	108	ASN	0	-0.041	-0.016	25.428	0.407	0.407	0.000	0.000	0.000	0.000
112	A	109	MET	0	0.089	0.033	24.578	-0.525	-0.525	0.000	0.000	0.000	0.000
113	A	110	GLY	0	0.042	0.039	24.888	-0.365	-0.365	0.000	0.000	0.000	0.000
114	A	111	THR	0	-0.027	-0.031	22.881	-0.174	-0.174	0.000	0.000	0.000	0.000
115	A	112	ALA	0	0.007	-0.006	21.044	-0.580	-0.580	0.000	0.000	0.000	0.000
116	A	113	GLU	-1	-0.850	-0.928	20.149	-13.020	-13.020	0.000	0.000	0.000	0.000
117	A	114	ILE	0	-0.016	0.001	21.229	-0.322	-0.322	0.000	0.000	0.000	0.000
118	A	115	LEU	0	-0.025	-0.010	17.686	-0.575	-0.575	0.000	0.000	0.000	0.000
119	A	116	VAL	0	-0.021	-0.010	15.684	-1.034	-1.034	0.000	0.000	0.000	0.000
120	A	117	ARG	1	0.882	0.943	16.192	12.850	12.850	0.000	0.000	0.000	0.000
121	A	118	THR	0	-0.054	-0.032	16.334	-0.224	-0.224	0.000	0.000	0.000	0.000
122	A	119	LEU	0	-0.111	-0.045	10.414	-0.614	-0.614	0.000	0.000	0.000	0.000
123	A	120	ASP	-1	-0.865	-0.926	10.008	-33.402	-33.402	0.000	0.000	0.000	0.000
124	A	121	GLU	-2	-1.870	-1.915	12.817	-36.666	-36.666	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:SER)