FMO DATABASE

FMODB ID: 1V95Z

Calculation Name: 6P5K-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6P5K

Chain ID: A

ChEMBL ID:

UniProt ID: G1TZ76

Base Structure: ElectronMicroscopy

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	98
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-722343.90807
FMO2-HF: Nuclear repulsion	683429.011995
FMO2-HF: Total energy	-38914.896075
FMO2-MP2: Total energy	-39025.573517

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:10:SER)

Summations of interaction energy for fragment #1(A:10: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.
51.066	53.907	1.855	-1.845	-2.85	-0.006

Interaction energy analysis for fragmet #1(A:10:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.884 / q_NPA : 0.922

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	12	GLU	-1	-0.801	-0.906	3.861	-30.455	-28.970	-0.017	-0.654	-0.813	-0.002
4	A	13	SER	0	-0.055	-0.008	2.350	1.709	2.122	1.486	-0.792	-1.107	-0.001
5	A	14	ILE	0	0.030	0.015	2.473	2.907	3.740	0.388	-0.376	-0.845	-0.003
6	A	15	ASN	0	0.062	0.044	4.772	4.709	4.727	-0.001	-0.010	-0.007	0.000
8	A	17	ARG	1	0.842	0.902	4.641	42.783	42.875	-0.001	-0.013	-0.078	0.000
7	A	16	SER	0	0.012	-0.001	7.111	3.021	3.021	0.000	0.000	0.000	0.000
9	A	18	LEU	0	0.010	0.003	8.516	2.794	2.794	0.000	0.000	0.000	0.000
10	A	19	GLN	0	0.026	0.015	10.641	0.921	0.921	0.000	0.000	0.000	0.000
11	A	20	LEU	0	-0.024	-0.009	11.942	1.697	1.697	0.000	0.000	0.000	0.000
12	A	21	VAL	0	-0.019	-0.008	12.411	1.448	1.448	0.000	0.000	0.000	0.000
13	A	22	MET	0	-0.062	-0.020	14.456	1.567	1.567	0.000	0.000	0.000	0.000
14	A	23	LYS	1	0.892	0.968	16.557	16.813	16.813	0.000	0.000	0.000	0.000
15	A	24	SER	0	0.009	-0.012	17.484	0.809	0.809	0.000	0.000	0.000	0.000
16	A	25	GLY	0	-0.007	0.023	17.290	0.522	0.522	0.000	0.000	0.000	0.000
17	A	26	LYS	1	0.838	0.921	18.304	13.011	13.011	0.000	0.000	0.000	0.000
18	A	27	TYR	0	0.036	0.013	16.917	-0.532	-0.532	0.000	0.000	0.000	0.000
19	A	28	VAL	0	-0.029	-0.014	18.704	0.860	0.860	0.000	0.000	0.000	0.000
20	A	29	LEU	0	0.036	0.022	17.724	-0.594	-0.594	0.000	0.000	0.000	0.000
21	A	30	GLY	0	0.051	0.023	20.412	0.806	0.806	0.000	0.000	0.000	0.000
22	A	31	TYR	0	0.049	0.024	22.183	0.053	0.053	0.000	0.000	0.000	0.000
23	A	32	LYS	1	0.995	0.992	23.434	9.922	9.922	0.000	0.000	0.000	0.000
24	A	33	GLN	0	-0.019	-0.010	24.433	0.638	0.638	0.000	0.000	0.000	0.000
25	A	34	SER	0	0.059	0.002	20.466	0.129	0.129	0.000	0.000	0.000	0.000
26	A	35	LEU	0	0.006	0.004	22.399	-0.017	-0.017	0.000	0.000	0.000	0.000
27	A	36	LYS	1	0.907	0.956	24.831	10.826	10.826	0.000	0.000	0.000	0.000
28	A	37	MET	0	0.005	0.001	22.349	0.304	0.304	0.000	0.000	0.000	0.000
29	A	38	ILE	0	0.016	0.016	20.460	-0.033	-0.033	0.000	0.000	0.000	0.000
30	A	39	ARG	1	0.932	0.975	23.100	10.720	10.720	0.000	0.000	0.000	0.000
31	A	40	GLN	0	-0.030	-0.015	26.153	0.400	0.400	0.000	0.000	0.000	0.000
32	A	41	GLY	0	0.042	0.031	24.194	0.184	0.184	0.000	0.000	0.000	0.000
33	A	42	LYS	1	0.886	0.941	23.252	10.811	10.811	0.000	0.000	0.000	0.000
34	A	43	ALA	0	-0.028	-0.010	18.875	-0.448	-0.448	0.000	0.000	0.000	0.000
35	A	44	LYS	1	0.924	0.964	16.314	14.879	14.879	0.000	0.000	0.000	0.000
36	A	45	LEU	0	0.010	0.009	9.902	-0.429	-0.429	0.000	0.000	0.000	0.000
37	A	46	VAL	0	-0.044	-0.031	14.332	0.801	0.801	0.000	0.000	0.000	0.000
38	A	47	ILE	0	0.007	0.014	9.823	-0.725	-0.725	0.000	0.000	0.000	0.000
39	A	48	LEU	0	-0.006	-0.015	13.383	1.865	1.865	0.000	0.000	0.000	0.000
40	A	49	ALA	0	0.040	0.025	13.851	-1.438	-1.438	0.000	0.000	0.000	0.000
41	A	50	ASN	0	0.047	0.017	13.626	2.370	2.370	0.000	0.000	0.000	0.000
42	A	51	ASN	0	0.046	0.022	15.970	0.065	0.065	0.000	0.000	0.000	0.000
43	A	52	CYS	0	-0.089	-0.032	17.997	0.964	0.964	0.000	0.000	0.000	0.000
44	A	53	PRO	0	0.020	-0.005	20.775	-0.080	-0.080	0.000	0.000	0.000	0.000
45	A	54	ALA	0	0.059	0.027	22.256	-0.128	-0.128	0.000	0.000	0.000	0.000
46	A	55	LEU	0	0.062	0.049	23.270	-0.215	-0.215	0.000	0.000	0.000	0.000
47	A	56	ARG	1	0.939	0.961	22.497	12.956	12.956	0.000	0.000	0.000	0.000
48	A	57	LYS	1	0.879	0.943	16.351	17.823	17.823	0.000	0.000	0.000	0.000
49	A	58	SER	0	0.041	0.010	20.379	-0.108	-0.108	0.000	0.000	0.000	0.000
50	A	59	GLU	-1	-0.888	-0.929	22.418	-11.136	-11.136	0.000	0.000	0.000	0.000
51	A	60	ILE	0	-0.044	-0.029	18.445	0.125	0.125	0.000	0.000	0.000	0.000
52	A	61	GLU	-1	-0.825	-0.905	17.416	-16.766	-16.766	0.000	0.000	0.000	0.000
53	A	62	TYR	0	0.016	0.015	19.732	-0.015	-0.015	0.000	0.000	0.000	0.000
54	A	63	TYR	0	-0.038	-0.041	23.086	0.381	0.381	0.000	0.000	0.000	0.000
55	A	64	ALA	0	-0.025	-0.012	18.152	0.206	0.206	0.000	0.000	0.000	0.000
56	A	65	MET	0	0.014	0.009	20.283	-0.073	-0.073	0.000	0.000	0.000	0.000
57	A	66	LEU	0	-0.045	-0.018	21.189	0.264	0.264	0.000	0.000	0.000	0.000
58	A	67	ALA	0	-0.044	-0.025	21.871	0.304	0.304	0.000	0.000	0.000	0.000
59	A	68	LYS	1	0.918	0.962	20.231	11.967	11.967	0.000	0.000	0.000	0.000
60	A	69	THR	0	-0.041	-0.004	16.945	-0.246	-0.246	0.000	0.000	0.000	0.000
61	A	70	GLY	0	0.043	0.031	13.486	-0.126	-0.126	0.000	0.000	0.000	0.000
62	A	71	VAL	0	0.008	-0.019	13.531	0.429	0.429	0.000	0.000	0.000	0.000
63	A	72	HIS	0	0.028	0.015	6.722	-1.460	-1.460	0.000	0.000	0.000	0.000
64	A	73	HIS	0	-0.062	-0.051	10.635	0.153	0.153	0.000	0.000	0.000	0.000
65	A	74	TYR	0	-0.013	-0.029	8.305	-1.423	-1.423	0.000	0.000	0.000	0.000
66	A	75	SER	0	-0.025	-0.025	7.691	0.467	0.467	0.000	0.000	0.000	0.000
67	A	76	GLY	0	0.093	0.066	9.841	0.503	0.503	0.000	0.000	0.000	0.000
68	A	77	ASN	0	0.004	0.001	12.752	0.348	0.348	0.000	0.000	0.000	0.000
69	A	78	ASN	0	0.031	-0.028	15.615	-0.638	-0.638	0.000	0.000	0.000	0.000
70	A	79	ILE	0	-0.003	0.003	17.849	0.425	0.425	0.000	0.000	0.000	0.000
71	A	80	GLU	-1	-0.870	-0.916	11.226	-26.399	-26.399	0.000	0.000	0.000	0.000
72	A	81	LEU	0	-0.012	-0.001	12.909	-0.570	-0.570	0.000	0.000	0.000	0.000
73	A	82	GLY	0	0.022	-0.001	14.255	0.004	0.004	0.000	0.000	0.000	0.000
74	A	83	THR	0	-0.016	-0.013	15.346	0.621	0.621	0.000	0.000	0.000	0.000
75	A	84	ALA	0	-0.009	0.001	10.983	0.006	0.006	0.000	0.000	0.000	0.000
76	A	85	CYS	0	-0.082	-0.050	12.969	-0.063	-0.063	0.000	0.000	0.000	0.000
77	A	86	GLY	0	0.026	0.017	15.546	0.959	0.959	0.000	0.000	0.000	0.000
78	A	87	LYS	1	0.817	0.910	17.841	15.434	15.434	0.000	0.000	0.000	0.000
79	A	88	TYR	0	0.039	0.018	20.456	-0.174	-0.174	0.000	0.000	0.000	0.000
80	A	89	TYR	0	-0.029	-0.019	21.847	0.679	0.679	0.000	0.000	0.000	0.000
81	A	90	ARG	1	0.954	0.990	20.211	12.012	12.012	0.000	0.000	0.000	0.000
82	A	91	VAL	0	-0.001	-0.018	17.511	0.838	0.838	0.000	0.000	0.000	0.000
83	A	92	CYS	-1	-0.888	-0.920	17.780	-15.440	-15.440	0.000	0.000	0.000	0.000
84	A	93	THR	0	-0.015	-0.006	17.234	-0.584	-0.584	0.000	0.000	0.000	0.000
85	A	94	LEU	0	0.013	0.011	13.271	0.865	0.865	0.000	0.000	0.000	0.000
86	A	95	SER	0	-0.017	0.002	15.736	-0.488	-0.488	0.000	0.000	0.000	0.000
87	A	96	ILE	0	0.023	0.001	12.156	0.703	0.703	0.000	0.000	0.000	0.000
88	A	97	ILE	0	-0.017	0.001	16.458	0.239	0.239	0.000	0.000	0.000	0.000
89	A	98	ASP	-1	-0.832	-0.928	18.793	-13.407	-13.407	0.000	0.000	0.000	0.000
90	A	99	PRO	0	0.006	0.000	13.756	0.071	0.071	0.000	0.000	0.000	0.000
91	A	100	GLY	0	0.043	0.029	15.719	-0.253	-0.253	0.000	0.000	0.000	0.000
92	A	101	ASP	-1	-0.895	-0.942	17.126	-15.243	-15.243	0.000	0.000	0.000	0.000
93	A	102	SER	0	-0.041	-0.033	11.720	-1.478	-1.478	0.000	0.000	0.000	0.000
94	A	103	ASP	-1	-0.831	-0.900	9.246	-26.136	-26.136	0.000	0.000	0.000	0.000
95	A	104	ILE	0	0.015	0.002	7.132	-2.865	-2.865	0.000	0.000	0.000	0.000
96	A	105	ILE	0	-0.048	-0.025	8.812	-0.972	-0.972	0.000	0.000	0.000	0.000
97	A	106	ARG	1	0.868	0.931	9.483	22.594	22.594	0.000	0.000	0.000	0.000
98	A	107	SER	-1	-0.913	-0.938	5.048	-40.461	-40.461	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:SER)