FMO DATABASE

FMODB ID: 2579R

Calculation Name: 2K87-A-Other549

Preferred Name: Replicase polyprotein 1ab

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2K87

Chain ID: A

ChEMBL ID: CHEMBL5118

UniProt ID: P0C6X7

Base Structure: SolutionNMR

Registration Date: 2025-10-12

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-945950.65678
FMO2-HF: Nuclear repulsion	899389.980988
FMO2-HF: Total energy	-46560.675792
FMO2-MP2: Total energy	-46695.516992

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:MET)

Summations of interaction energy for fragment #1(A:1: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.
9.698	11.408	-0.022	-0.79	-0.898	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.850 / q_NPA : 0.913

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

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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	3	THR	0	0.041	0.015	3.831	-1.983	-0.273	-0.022	-0.790	-0.898	-0.001
4	A	4	GLU	-1	-0.936	-0.964	6.543	-25.483	-25.483	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.027	0.001	9.281	3.289	3.289	0.000	0.000	0.000	0.000
6	A	6	PRO	0	-0.014	-0.008	11.665	-0.078	-0.078	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.010	-0.005	14.715	-0.529	-0.529	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.907	-0.970	16.149	-15.247	-15.247	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.085	-0.016	18.057	0.922	0.922	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.010	-0.001	20.004	-0.208	-0.208	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.015	-0.018	22.598	0.375	0.375	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.015	-0.001	25.848	0.134	0.134	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.038	-0.026	29.357	0.223	0.223	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.004	0.003	32.958	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	15	LEU	0	0.041	0.025	35.762	0.038	0.038	0.000	0.000	0.000	0.000
16	A	16	PRO	0	0.001	0.005	38.534	0.152	0.152	0.000	0.000	0.000	0.000
17	A	17	ASN	0	-0.035	-0.051	41.487	0.207	0.207	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.014	0.015	41.049	0.111	0.111	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.006	-0.019	43.099	-0.049	-0.049	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.014	-0.011	42.818	-0.157	-0.157	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.889	-0.941	44.935	-6.704	-6.704	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.008	-0.004	46.569	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.030	-0.020	39.804	-0.014	-0.014	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.883	0.946	43.046	7.345	7.345	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.035	-0.002	36.712	-0.148	-0.148	0.000	0.000	0.000	0.000
26	A	26	THR	0	0.004	-0.024	38.266	0.124	0.124	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.017	-0.002	33.161	-0.326	-0.326	0.000	0.000	0.000	0.000
28	A	28	SER	0	0.047	0.032	32.141	0.215	0.215	0.000	0.000	0.000	0.000
29	A	29	ASN	0	0.020	0.009	33.469	0.339	0.339	0.000	0.000	0.000	0.000
30	A	30	THR	0	0.066	0.023	35.426	-0.092	-0.092	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.914	0.958	37.156	8.392	8.392	0.000	0.000	0.000	0.000
32	A	32	PHE	0	0.002	-0.017	31.034	0.019	0.019	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.007	0.005	35.667	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.885	-0.954	38.117	-7.457	-7.457	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.881	-0.913	37.668	-8.315	-8.315	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.018	-0.010	34.033	0.094	0.094	0.000	0.000	0.000	0.000
37	A	37	ASN	0	-0.007	-0.015	38.553	0.114	0.114	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.001	0.003	42.038	0.183	0.183	0.000	0.000	0.000	0.000
39	A	39	MET	0	-0.093	-0.023	36.175	0.020	0.020	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.052	-0.022	41.069	0.002	0.002	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.019	0.029	42.943	0.112	0.112	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.008	-0.021	44.459	0.146	0.146	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.004	0.006	46.435	0.107	0.107	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.918	0.976	49.928	6.298	6.298	0.000	0.000	0.000	0.000
45	A	45	PRO	0	0.027	0.002	51.428	0.090	0.090	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.010	0.003	46.494	-0.033	-0.033	0.000	0.000	0.000	0.000
47	A	47	SER	0	0.004	0.002	47.194	0.085	0.085	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.949	0.975	41.576	7.408	7.408	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.876	-0.926	42.391	-7.228	-7.228	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.020	0.025	37.233	-0.064	-0.064	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.017	-0.010	35.559	0.109	0.109	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.045	-0.016	30.825	-0.178	-0.178	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.020	-0.035	28.432	0.275	0.275	0.000	0.000	0.000	0.000
54	A	54	PHE	0	0.001	-0.012	26.545	-0.149	-0.149	0.000	0.000	0.000	0.000
55	A	55	PHE	0	0.039	0.036	18.979	-0.166	-0.166	0.000	0.000	0.000	0.000
56	A	56	PRO	0	-0.015	-0.019	20.520	-0.201	-0.201	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.853	-0.921	22.504	-11.552	-11.552	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.036	-0.009	22.996	0.183	0.183	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.004	-0.012	26.740	-0.079	-0.079	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.020	0.034	30.096	0.379	0.379	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.923	-0.961	31.366	-9.223	-9.223	0.000	0.000	0.000	0.000
62	A	62	VAL	0	0.001	-0.006	31.115	-0.243	-0.243	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.013	-0.007	25.392	-0.074	-0.074	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.013	0.003	27.217	0.109	0.109	0.000	0.000	0.000	0.000
65	A	65	ILE	0	0.012	-0.002	20.987	-0.471	-0.471	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.793	-0.872	19.374	-15.961	-15.961	0.000	0.000	0.000	0.000
67	A	67	TYR	0	0.048	-0.001	21.766	-0.245	-0.245	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.849	0.914	14.711	19.137	19.137	0.000	0.000	0.000	0.000
69	A	69	HIS	0	0.028	0.006	15.077	-0.961	-0.961	0.000	0.000	0.000	0.000
70	A	70	TYR	0	-0.035	-0.012	19.916	0.404	0.404	0.000	0.000	0.000	0.000
71	A	71	SER	0	0.044	0.022	20.668	0.265	0.265	0.000	0.000	0.000	0.000
72	A	72	ALA	0	0.020	-0.001	22.624	0.457	0.457	0.000	0.000	0.000	0.000
73	A	73	SER	0	-0.014	-0.011	22.511	0.296	0.296	0.000	0.000	0.000	0.000
74	A	74	PHE	0	0.027	0.007	20.410	0.376	0.376	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.907	0.970	26.331	9.955	9.955	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.911	0.949	29.752	9.214	9.214	0.000	0.000	0.000	0.000
77	A	77	GLY	0	0.091	0.049	29.928	0.292	0.292	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.030	-0.027	24.854	-0.215	-0.215	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.861	0.937	24.865	12.418	12.418	0.000	0.000	0.000	0.000
80	A	80	LEU	0	0.065	0.042	20.813	-0.471	-0.471	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.041	0.023	20.391	0.538	0.538	0.000	0.000	0.000	0.000
82	A	82	HIS	0	-0.001	-0.008	23.128	0.085	0.085	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.871	0.946	26.412	11.201	11.201	0.000	0.000	0.000	0.000
84	A	84	PRO	0	0.037	0.018	26.977	-0.456	-0.456	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.017	-0.012	24.258	-0.141	-0.141	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.006	0.024	27.556	0.271	0.271	0.000	0.000	0.000	0.000
87	A	87	TRP	0	-0.003	-0.002	22.434	-0.429	-0.429	0.000	0.000	0.000	0.000
88	A	88	HIS	0	0.021	0.008	24.582	0.897	0.897	0.000	0.000	0.000	0.000
89	A	89	ILE	0	0.003	-0.012	26.244	-0.603	-0.603	0.000	0.000	0.000	0.000
90	A	90	ASN	0	-0.024	-0.014	26.823	0.300	0.300	0.000	0.000	0.000	0.000
91	A	91	GLN	0	0.021	0.023	28.315	0.644	0.644	0.000	0.000	0.000	0.000
92	A	92	ALA	0	0.017	0.012	30.187	0.383	0.383	0.000	0.000	0.000	0.000
93	A	93	THR	0	-0.031	-0.019	31.144	-0.437	-0.437	0.000	0.000	0.000	0.000
94	A	94	THR	0	0.061	0.018	31.835	0.163	0.163	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.986	0.982	34.311	8.255	8.255	0.000	0.000	0.000	0.000
96	A	96	THR	0	0.012	0.004	29.612	0.242	0.242	0.000	0.000	0.000	0.000
97	A	97	THR	0	0.053	0.019	28.665	0.023	0.023	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.042	0.026	31.347	-0.027	-0.027	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.966	0.984	34.029	8.340	8.340	0.000	0.000	0.000	0.000
100	A	100	PRO	0	0.010	0.016	29.799	0.190	0.190	0.000	0.000	0.000	0.000
101	A	101	ASN	0	0.009	-0.017	30.959	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	102	THR	0	-0.059	-0.034	33.318	0.168	0.168	0.000	0.000	0.000	0.000
103	A	103	TRP	0	-0.032	-0.013	32.859	0.260	0.260	0.000	0.000	0.000	0.000
104	A	104	CYS	0	0.005	0.000	30.632	0.132	0.132	0.000	0.000	0.000	0.000
105	A	105	LEU	0	0.030	0.012	33.279	0.109	0.109	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.930	0.967	36.884	8.012	8.012	0.000	0.000	0.000	0.000
107	A	107	CYS	0	-0.064	-0.030	33.602	0.012	0.012	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.010	0.011	34.285	0.001	0.001	0.000	0.000	0.000	0.000
109	A	109	TRP	0	-0.066	-0.026	37.562	0.225	0.225	0.000	0.000	0.000	0.000
110	A	110	SER	0	0.011	0.008	40.086	-0.144	-0.144	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.048	-0.013	42.310	0.050	0.050	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.966	0.996	44.845	6.248	6.248	0.000	0.000	0.000	0.000
113	A	113	PRO	0	0.031	0.026	48.269	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.030	-0.035	51.099	0.029	0.029	0.000	0.000	0.000	0.000
115	A	115	ASP	-1	-0.953	-0.963	53.551	-5.515	-5.515	0.000	0.000	0.000	0.000
116	A	116	THR	-1	-0.984	-0.981	56.608	-5.378	-5.378	0.000	0.000	0.000	0.000

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