FMO DATABASE

FMODB ID: KQJK3

Calculation Name: 4V6Z-A-Other549

Preferred Name:

Target Type:

Ligand 3-letter code: CM0 | 7MG | 6MZ | PSU | 5MU | 4SU | H2U | OMC | FME | NH2 | ACE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4V6Z

Chain ID: A

ChEMBL ID:

UniProt ID: P0A7J7

Base Structure: ElectronMicroscopy

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	Original chain id is "AN", which converted from A;

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	100
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-624612.254629
FMO2-HF: Nuclear repulsion	584699.918815
FMO2-HF: Total energy	-39912.335814
FMO2-MP2: Total energy	-40028.967375

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:ALA)

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

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.
263.597	268.55	1.886	-2.966	-3.872	-0.027

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.846 / q_NPA : 0.920

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	4	GLN	0	0.183	0.081	3.870	2.207	3.543	-0.011	-0.569	-0.756	-0.001
5	A	6	MET	0	-0.096	-0.050	3.360	4.655	4.941	0.009	-0.057	-0.238	0.000
62	A	63	ARG	1	0.874	0.932	4.523	35.337	35.381	-0.001	-0.003	-0.039	0.000
66	A	67	THR	0	-0.108	-0.170	3.330	-4.693	-4.348	0.011	-0.099	-0.257	0.000
67	A	68	GLY	0	0.020	0.008	2.468	-17.944	-16.467	1.547	-1.611	-1.413	-0.021
68	A	69	ARG	1	0.879	0.944	3.040	35.540	36.970	0.316	-0.643	-1.103	-0.005
69	A	70	PRO	0	-0.030	-0.013	3.837	5.349	5.384	0.015	0.016	-0.066	0.000
4	A	5	SER	0	0.046	0.034	6.761	1.771	1.771	0.000	0.000	0.000	0.000
6	A	7	LYS	1	0.876	0.938	5.821	40.228	40.228	0.000	0.000	0.000	0.000
7	A	8	ALA	0	0.096	0.060	8.316	1.544	1.544	0.000	0.000	0.000	0.000
8	A	9	ARG	1	0.855	0.924	8.517	29.313	29.313	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.786	-0.868	11.554	-19.526	-19.526	0.000	0.000	0.000	0.000
10	A	11	VAL	0	0.030	0.029	13.753	1.117	1.117	0.000	0.000	0.000	0.000
11	A	12	LYS	1	1.012	1.007	16.470	14.473	14.473	0.000	0.000	0.000	0.000
12	A	13	ARG	1	0.784	0.878	12.796	19.627	19.627	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.052	0.024	17.255	0.699	0.699	0.000	0.000	0.000	0.000
14	A	15	ALA	0	0.045	0.026	19.135	0.595	0.595	0.000	0.000	0.000	0.000
15	A	16	LEU	0	-0.014	-0.013	21.756	0.560	0.560	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.033	-0.018	21.262	0.395	0.395	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.897	-0.932	23.331	-10.509	-10.509	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.956	0.992	25.928	10.515	10.515	0.000	0.000	0.000	0.000
19	A	20	TYR	0	0.010	-0.017	26.882	0.332	0.332	0.000	0.000	0.000	0.000
20	A	21	PHE	0	-0.078	-0.047	21.850	0.159	0.159	0.000	0.000	0.000	0.000
21	A	22	ALA	0	0.016	0.015	25.909	0.010	0.010	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.989	1.001	27.488	9.607	9.607	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.900	0.944	27.013	10.680	10.680	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.044	-0.013	31.830	0.147	0.147	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.852	-0.927	33.489	-8.171	-8.171	0.000	0.000	0.000	0.000
26	A	27	LEU	0	-0.022	-0.015	34.573	0.191	0.191	0.000	0.000	0.000	0.000
27	A	28	LYS	1	0.924	0.967	35.036	8.495	8.495	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.035	0.016	37.461	0.068	0.068	0.000	0.000	0.000	0.000
29	A	30	ILE	0	-0.008	0.013	38.711	0.137	0.137	0.000	0.000	0.000	0.000
30	A	31	ILE	0	-0.083	-0.037	36.073	-0.023	-0.023	0.000	0.000	0.000	0.000
31	A	32	SER	0	-0.047	-0.049	39.566	-0.210	-0.210	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.828	-0.906	42.062	-6.322	-6.322	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.041	-0.018	45.388	-0.122	-0.122	0.000	0.000	0.000	0.000
34	A	35	ASN	0	-0.030	-0.007	47.840	0.164	0.164	0.000	0.000	0.000	0.000
35	A	36	ALA	0	0.004	0.012	49.528	0.119	0.119	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.043	-0.032	49.811	-0.079	-0.079	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.966	-0.981	48.165	-6.347	-6.347	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.904	-0.940	48.337	-6.093	-6.093	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.826	-0.924	42.076	-7.552	-7.552	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.958	0.983	44.057	6.675	6.675	0.000	0.000	0.000	0.000
41	A	42	TRP	0	-0.011	-0.019	40.280	-0.130	-0.130	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.015	-0.008	36.970	-0.525	-0.525	0.000	0.000	0.000	0.000
43	A	44	ALA	0	0.039	0.013	36.637	-0.276	-0.276	0.000	0.000	0.000	0.000
44	A	45	VAL	0	0.054	0.026	36.475	-0.230	-0.230	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.009	0.002	33.441	-0.292	-0.292	0.000	0.000	0.000	0.000
46	A	47	LYS	1	0.896	0.952	32.140	8.539	8.539	0.000	0.000	0.000	0.000
47	A	48	LEU	0	0.039	0.029	31.629	-0.347	-0.347	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.004	-0.010	30.397	-0.508	-0.508	0.000	0.000	0.000	0.000
49	A	50	THR	0	-0.130	-0.091	27.893	-0.398	-0.398	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.053	0.059	27.487	-0.326	-0.326	0.000	0.000	0.000	0.000
51	A	52	PRO	0	-0.033	-0.011	25.435	-0.478	-0.478	0.000	0.000	0.000	0.000
52	A	53	ARG	1	1.005	0.991	20.419	13.137	13.137	0.000	0.000	0.000	0.000
53	A	54	ASP	-1	-0.882	-0.928	15.664	-18.532	-18.532	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.019	-0.015	17.729	-0.662	-0.662	0.000	0.000	0.000	0.000
55	A	56	SER	0	-0.041	-0.026	19.528	0.463	0.463	0.000	0.000	0.000	0.000
56	A	57	PRO	0	0.082	0.057	20.646	-0.414	-0.414	0.000	0.000	0.000	0.000
57	A	58	SER	0	0.080	0.048	19.728	-0.435	-0.435	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.883	0.925	14.915	16.622	16.622	0.000	0.000	0.000	0.000
59	A	60	GLN	0	-0.031	-0.026	14.193	-2.164	-2.164	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.912	0.939	10.612	20.338	20.338	0.000	0.000	0.000	0.000
61	A	62	ASN	0	0.019	0.016	12.062	0.766	0.766	0.000	0.000	0.000	0.000
63	A	64	CYS	-1	-0.748	-0.735	5.709	-34.760	-34.760	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.916	0.912	6.537	16.237	16.237	0.000	0.000	0.000	0.000
65	A	66	GLN	0	0.093	0.056	8.097	0.035	0.035	0.000	0.000	0.000	0.000
70	A	71	HIS	0	0.094	0.041	5.444	3.451	3.451	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.044	0.007	8.054	-2.255	-2.255	0.000	0.000	0.000	0.000
72	A	73	PHE	0	-0.009	-0.001	10.724	0.572	0.572	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.033	0.014	12.060	0.959	0.959	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.993	0.991	15.825	16.495	16.495	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.986	0.994	18.007	12.339	12.339	0.000	0.000	0.000	0.000
76	A	77	PHE	0	0.045	0.023	16.936	0.360	0.360	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.029	0.028	17.352	-0.233	-0.233	0.000	0.000	0.000	0.000
78	A	79	LEU	0	0.001	0.004	11.463	-1.092	-1.092	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.007	-0.025	8.778	1.192	1.192	0.000	0.000	0.000	0.000
80	A	81	ARG	1	1.003	0.987	11.072	20.429	20.429	0.000	0.000	0.000	0.000
81	A	82	ILE	0	-0.071	-0.043	6.241	0.006	0.006	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.902	0.938	8.675	29.086	29.086	0.000	0.000	0.000	0.000
83	A	84	VAL	0	0.024	0.037	11.994	1.126	1.126	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.978	0.995	15.274	17.414	17.414	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.787	-0.881	12.482	-23.232	-23.232	0.000	0.000	0.000	0.000
86	A	87	ALA	0	0.021	0.015	15.430	0.467	0.467	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.010	-0.001	17.305	0.764	0.764	0.000	0.000	0.000	0.000
88	A	89	MET	0	-0.060	-0.038	20.010	0.854	0.854	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.869	0.928	15.327	18.683	18.683	0.000	0.000	0.000	0.000
90	A	91	GLY	0	0.034	0.031	21.970	0.429	0.429	0.000	0.000	0.000	0.000
91	A	92	GLU	-1	-0.933	-0.967	18.731	-15.188	-15.188	0.000	0.000	0.000	0.000
92	A	93	ILE	0	-0.100	-0.045	16.425	-0.375	-0.375	0.000	0.000	0.000	0.000
93	A	94	PRO	0	0.059	0.051	20.700	0.333	0.333	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.000	-0.011	23.667	-0.183	-0.183	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.073	-0.052	19.788	0.176	0.176	0.000	0.000	0.000	0.000
96	A	97	LYS	1	1.028	1.013	23.798	10.075	10.075	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.869	0.929	25.722	11.529	11.529	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.008	0.003	27.137	0.304	0.304	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.053	-0.038	28.378	-0.029	-0.029	0.000	0.000	0.000	0.000
100	A	101	TRP	-1	-0.843	-0.894	28.652	-9.637	-9.637	0.000	0.000	0.000	0.000

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