FMO DATABASE

FMODB ID: QMR9Y

Calculation Name: 6TCD-D-Xray547

Preferred Name:

Target Type:

Ligand Name: acetate ion

Ligand 3-letter code: ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6TCD

Chain ID: D

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-04

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	133
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1073907.804064
FMO2-HF: Nuclear repulsion	1023930.143025
FMO2-HF: Total energy	-49977.66104
FMO2-MP2: Total energy	-50122.75104

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:-1:SER)

Summations of interaction energy for fragment #1(A:-1: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.
22.066	24.607	0.892	-1.356	-2.076	-0.011

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.860 / 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	1	MET	0	0.003	-0.002	3.137	-9.865	-7.348	0.893	-1.355	-2.055	-0.011
4	A	2	ALA	0	-0.012	-0.004	5.301	3.989	4.013	-0.001	-0.001	-0.021	0.000
5	A	3	ALA	0	0.022	0.019	8.816	0.463	0.463	0.000	0.000	0.000	0.000
6	A	4	VAL	0	-0.002	-0.007	11.552	1.903	1.903	0.000	0.000	0.000	0.000
7	A	5	GLN	0	0.008	0.006	12.902	-0.797	-0.797	0.000	0.000	0.000	0.000
8	A	6	LYS	1	0.943	0.969	9.457	26.659	26.659	0.000	0.000	0.000	0.000
9	A	7	LEU	0	0.022	0.024	15.762	0.282	0.282	0.000	0.000	0.000	0.000
10	A	8	PHE	0	-0.008	-0.020	12.436	-0.732	-0.732	0.000	0.000	0.000	0.000
11	A	9	PRO	0	0.005	0.015	18.565	0.252	0.252	0.000	0.000	0.000	0.000
12	A	10	TYR	0	0.023	0.004	21.846	-0.109	-0.109	0.000	0.000	0.000	0.000
13	A	11	THR	0	0.023	0.002	23.760	0.459	0.459	0.000	0.000	0.000	0.000
14	A	12	PRO	0	-0.018	0.003	26.983	-0.109	-0.109	0.000	0.000	0.000	0.000
15	A	13	ARG	1	0.861	0.913	28.625	9.842	9.842	0.000	0.000	0.000	0.000
16	A	14	ALA	0	0.053	0.036	27.663	0.242	0.242	0.000	0.000	0.000	0.000
17	A	15	PRO	0	0.005	0.006	26.854	-0.250	-0.250	0.000	0.000	0.000	0.000
18	A	16	ILE	0	0.006	0.009	19.837	-0.301	-0.301	0.000	0.000	0.000	0.000
19	A	17	ARG	1	0.899	0.971	20.212	13.453	13.453	0.000	0.000	0.000	0.000
20	A	18	GLN	0	0.098	0.040	17.615	-0.470	-0.470	0.000	0.000	0.000	0.000
21	A	19	GLY	0	-0.017	-0.010	14.799	0.225	0.225	0.000	0.000	0.000	0.000
22	A	20	ILE	0	-0.064	-0.024	14.474	-0.597	-0.597	0.000	0.000	0.000	0.000
23	A	21	TYR	0	0.031	-0.004	15.303	-0.512	-0.512	0.000	0.000	0.000	0.000
24	A	22	SER	0	0.007	0.015	16.060	0.362	0.362	0.000	0.000	0.000	0.000
25	A	23	GLN	0	0.003	-0.007	18.187	0.053	0.053	0.000	0.000	0.000	0.000
26	A	24	ALA	0	0.063	0.029	20.918	0.437	0.437	0.000	0.000	0.000	0.000
27	A	25	VAL	0	-0.051	-0.028	15.007	-0.841	-0.841	0.000	0.000	0.000	0.000
28	A	26	VAL	0	-0.005	0.004	18.262	0.580	0.580	0.000	0.000	0.000	0.000
29	A	27	VAL	0	-0.011	-0.023	14.984	-1.066	-1.066	0.000	0.000	0.000	0.000
30	A	28	ASP	-1	-0.893	-0.943	18.294	-13.193	-13.193	0.000	0.000	0.000	0.000
31	A	29	ARG	1	0.966	0.988	21.121	11.512	11.512	0.000	0.000	0.000	0.000
32	A	30	THR	0	-0.005	0.023	21.243	0.657	0.657	0.000	0.000	0.000	0.000
33	A	31	MET	0	-0.039	-0.018	20.955	-0.720	-0.720	0.000	0.000	0.000	0.000
34	A	32	TYR	0	0.024	0.011	19.020	0.598	0.598	0.000	0.000	0.000	0.000
35	A	33	ILE	0	-0.019	-0.021	21.128	-0.434	-0.434	0.000	0.000	0.000	0.000
36	A	34	SER	0	0.010	-0.006	20.258	0.068	0.068	0.000	0.000	0.000	0.000
37	A	35	GLY	0	0.017	0.020	22.619	0.458	0.458	0.000	0.000	0.000	0.000
38	A	36	GLN	0	-0.069	-0.040	25.609	0.213	0.213	0.000	0.000	0.000	0.000
39	A	37	LEU	0	0.062	0.023	27.742	0.333	0.333	0.000	0.000	0.000	0.000
40	A	38	GLY	0	0.028	0.019	30.534	0.004	0.004	0.000	0.000	0.000	0.000
41	A	39	LEU	0	-0.070	-0.050	28.841	0.216	0.216	0.000	0.000	0.000	0.000
42	A	40	ASP	-1	-0.753	-0.856	32.804	-8.617	-8.617	0.000	0.000	0.000	0.000
43	A	41	VAL	0	-0.048	-0.025	29.006	-0.104	-0.104	0.000	0.000	0.000	0.000
44	A	42	ALA	0	-0.018	0.001	31.622	-0.148	-0.148	0.000	0.000	0.000	0.000
45	A	43	SER	0	-0.020	-0.034	34.302	-0.052	-0.052	0.000	0.000	0.000	0.000
46	A	44	GLY	0	0.029	0.024	31.384	-0.061	-0.061	0.000	0.000	0.000	0.000
47	A	45	LYS	1	0.896	0.949	31.936	8.643	8.643	0.000	0.000	0.000	0.000
48	A	46	LEU	0	0.002	0.011	32.912	-0.098	-0.098	0.000	0.000	0.000	0.000
49	A	47	VAL	0	-0.036	-0.009	35.620	0.182	0.182	0.000	0.000	0.000	0.000
50	A	48	GLU	-1	-0.901	-0.951	38.527	-6.966	-6.966	0.000	0.000	0.000	0.000
51	A	49	GLY	0	0.011	-0.008	42.160	-0.016	-0.016	0.000	0.000	0.000	0.000
52	A	50	GLY	0	-0.005	0.001	41.359	0.050	0.050	0.000	0.000	0.000	0.000
53	A	51	VAL	0	0.053	0.017	38.625	-0.115	-0.115	0.000	0.000	0.000	0.000
54	A	52	GLN	0	0.028	0.020	39.584	-0.112	-0.112	0.000	0.000	0.000	0.000
55	A	53	ALA	0	-0.002	0.007	40.852	-0.091	-0.091	0.000	0.000	0.000	0.000
56	A	54	GLN	0	0.029	0.009	36.106	-0.323	-0.323	0.000	0.000	0.000	0.000
57	A	55	ALA	0	0.040	0.018	35.746	-0.260	-0.260	0.000	0.000	0.000	0.000
58	A	56	ARG	1	0.985	0.995	36.355	7.445	7.445	0.000	0.000	0.000	0.000
59	A	57	GLN	0	-0.039	-0.017	34.363	0.129	0.129	0.000	0.000	0.000	0.000
60	A	58	ALA	0	0.010	0.012	32.142	-0.217	-0.217	0.000	0.000	0.000	0.000
61	A	59	LEU	0	0.027	0.015	31.914	-0.314	-0.314	0.000	0.000	0.000	0.000
62	A	60	VAL	0	0.021	0.026	33.918	-0.082	-0.082	0.000	0.000	0.000	0.000
63	A	61	ASN	0	-0.030	-0.020	29.964	0.005	0.005	0.000	0.000	0.000	0.000
64	A	62	MET	0	0.013	0.001	28.725	-0.220	-0.220	0.000	0.000	0.000	0.000
65	A	63	GLY	0	0.057	0.035	29.888	-0.196	-0.196	0.000	0.000	0.000	0.000
66	A	64	GLU	-1	-0.856	-0.905	30.805	-9.246	-9.246	0.000	0.000	0.000	0.000
67	A	65	ILE	0	-0.025	-0.012	24.836	-0.226	-0.226	0.000	0.000	0.000	0.000
68	A	66	LEU	0	-0.042	-0.015	26.931	-0.327	-0.327	0.000	0.000	0.000	0.000
69	A	67	LYS	1	0.894	0.936	29.029	8.836	8.836	0.000	0.000	0.000	0.000
70	A	68	ALA	0	-0.057	-0.014	25.959	0.004	0.004	0.000	0.000	0.000	0.000
71	A	69	ALA	0	-0.032	-0.022	25.079	-0.415	-0.415	0.000	0.000	0.000	0.000
72	A	70	GLY	0	-0.012	0.004	26.459	0.004	0.004	0.000	0.000	0.000	0.000
73	A	71	CYS	0	-0.088	-0.033	28.444	0.195	0.195	0.000	0.000	0.000	0.000
74	A	72	GLY	0	0.037	0.003	30.972	0.145	0.145	0.000	0.000	0.000	0.000
75	A	73	TYR	0	-0.036	-0.058	32.642	-0.155	-0.155	0.000	0.000	0.000	0.000
76	A	74	ASP	-1	-0.825	-0.910	34.178	-8.148	-8.148	0.000	0.000	0.000	0.000
77	A	75	ASN	0	-0.021	-0.009	30.027	0.156	0.156	0.000	0.000	0.000	0.000
78	A	76	VAL	0	-0.024	-0.013	29.692	-0.386	-0.386	0.000	0.000	0.000	0.000
79	A	77	VAL	0	0.029	0.019	27.980	0.274	0.274	0.000	0.000	0.000	0.000
80	A	78	LYS	1	0.857	0.924	27.622	10.635	10.635	0.000	0.000	0.000	0.000
81	A	79	THR	0	0.039	0.028	28.826	-0.137	-0.137	0.000	0.000	0.000	0.000
82	A	80	THR	0	-0.078	-0.043	27.478	0.223	0.223	0.000	0.000	0.000	0.000
83	A	81	VAL	0	-0.039	-0.016	30.290	-0.078	-0.078	0.000	0.000	0.000	0.000
84	A	82	LEU	0	0.025	0.022	27.764	0.120	0.120	0.000	0.000	0.000	0.000
85	A	83	LEU	0	0.023	-0.003	32.514	0.069	0.069	0.000	0.000	0.000	0.000
86	A	84	ALA	0	0.035	0.021	35.571	-0.093	-0.093	0.000	0.000	0.000	0.000
87	A	85	ASP	-1	-0.782	-0.889	37.035	-7.080	-7.080	0.000	0.000	0.000	0.000
88	A	86	MET	0	0.002	0.008	38.473	-0.078	-0.078	0.000	0.000	0.000	0.000
89	A	87	ASN	0	-0.073	-0.055	41.387	0.156	0.156	0.000	0.000	0.000	0.000
90	A	88	ASP	-1	-0.877	-0.939	40.835	-7.285	-7.285	0.000	0.000	0.000	0.000
91	A	89	PHE	0	-0.012	-0.013	38.839	-0.043	-0.043	0.000	0.000	0.000	0.000
92	A	90	VAL	0	0.005	0.004	41.823	-0.073	-0.073	0.000	0.000	0.000	0.000
93	A	91	ASN	0	0.059	0.025	44.031	0.048	0.048	0.000	0.000	0.000	0.000
94	A	92	VAL	0	-0.003	-0.004	37.497	-0.060	-0.060	0.000	0.000	0.000	0.000
95	A	93	ASN	0	0.008	0.007	40.182	-0.335	-0.335	0.000	0.000	0.000	0.000
96	A	94	ASP	-1	-0.869	-0.943	41.618	-6.709	-6.709	0.000	0.000	0.000	0.000
97	A	95	VAL	0	-0.008	0.002	39.603	0.015	0.015	0.000	0.000	0.000	0.000
98	A	96	TYR	0	0.014	0.000	33.953	0.018	0.018	0.000	0.000	0.000	0.000
99	A	97	LYS	1	0.880	0.944	39.351	6.702	6.702	0.000	0.000	0.000	0.000
100	A	98	THR	0	-0.095	-0.051	41.735	0.076	0.076	0.000	0.000	0.000	0.000
101	A	99	PHE	0	-0.032	-0.009	36.994	0.007	0.007	0.000	0.000	0.000	0.000
102	A	100	PHE	0	-0.025	-0.018	33.112	-0.132	-0.132	0.000	0.000	0.000	0.000
103	A	101	SER	0	0.041	0.015	38.992	0.077	0.077	0.000	0.000	0.000	0.000
104	A	102	LYS	1	0.861	0.917	40.497	7.854	7.854	0.000	0.000	0.000	0.000
105	A	103	ASN	0	-0.049	-0.028	38.326	-0.025	-0.025	0.000	0.000	0.000	0.000
106	A	104	PHE	0	0.009	0.017	37.225	-0.180	-0.180	0.000	0.000	0.000	0.000
107	A	105	PRO	0	0.024	0.030	32.444	-0.043	-0.043	0.000	0.000	0.000	0.000
108	A	106	ALA	0	0.019	0.021	31.787	0.202	0.202	0.000	0.000	0.000	0.000
109	A	107	ARG	1	0.815	0.890	32.469	8.010	8.010	0.000	0.000	0.000	0.000
110	A	108	ALA	0	0.000	0.011	31.393	0.117	0.117	0.000	0.000	0.000	0.000
111	A	109	ALA	0	-0.009	-0.017	33.195	-0.123	-0.123	0.000	0.000	0.000	0.000
112	A	110	TYR	0	0.013	0.008	28.545	0.148	0.148	0.000	0.000	0.000	0.000
113	A	111	GLN	0	-0.018	0.001	34.718	-0.034	-0.034	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.019	-0.016	30.573	-0.152	-0.152	0.000	0.000	0.000	0.000
115	A	113	VAL	0	0.001	-0.001	33.095	0.168	0.168	0.000	0.000	0.000	0.000
116	A	114	ALA	0	0.007	-0.002	31.748	0.203	0.203	0.000	0.000	0.000	0.000
117	A	115	LEU	0	0.004	0.025	29.825	-0.294	-0.294	0.000	0.000	0.000	0.000
118	A	116	PRO	0	0.029	0.012	25.963	0.136	0.136	0.000	0.000	0.000	0.000
119	A	117	ARG	1	0.774	0.850	28.053	10.073	10.073	0.000	0.000	0.000	0.000
120	A	118	GLY	0	0.031	0.034	30.527	0.241	0.241	0.000	0.000	0.000	0.000
121	A	119	GLY	0	-0.032	-0.007	32.298	0.252	0.252	0.000	0.000	0.000	0.000
122	A	120	LEU	0	0.031	0.000	33.821	0.008	0.008	0.000	0.000	0.000	0.000
123	A	121	VAL	0	-0.018	-0.010	34.520	0.080	0.080	0.000	0.000	0.000	0.000
124	A	122	GLU	-1	-0.907	-0.963	26.621	-11.246	-11.246	0.000	0.000	0.000	0.000
125	A	123	ILE	0	-0.029	-0.016	30.284	0.172	0.172	0.000	0.000	0.000	0.000
126	A	124	GLU	-1	-0.831	-0.889	24.467	-12.006	-12.006	0.000	0.000	0.000	0.000
127	A	125	ALA	0	-0.015	-0.032	25.671	0.466	0.466	0.000	0.000	0.000	0.000
128	A	126	VAL	0	-0.013	0.002	23.510	-0.595	-0.595	0.000	0.000	0.000	0.000
129	A	127	ALA	0	0.000	0.001	25.376	0.560	0.560	0.000	0.000	0.000	0.000
130	A	128	VAL	0	0.003	0.002	25.570	-0.533	-0.533	0.000	0.000	0.000	0.000
131	A	129	LEU	0	-0.009	-0.002	24.615	0.370	0.370	0.000	0.000	0.000	0.000
132	A	130	GLY	0	0.006	0.003	28.016	0.059	0.059	0.000	0.000	0.000	0.000
133	A	131	PRO	-1	-0.954	-0.974	29.469	-10.302	-10.302	0.000	0.000	0.000	0.000

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