FMO DATABASE

FMODB ID: 3ZKZL

Calculation Name: 3SSR-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3SSR

Chain ID: B

ChEMBL ID:

UniProt ID: Q8DKB2

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	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-664863.640867
FMO2-HF: Nuclear repulsion	628328.988128
FMO2-HF: Total energy	-36534.652739
FMO2-MP2: Total energy	-36642.282691

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:PRO)

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

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.
-71.698	-62.681	3.702	-4.97	-7.747	-0.033

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.810 / q_NPA : 0.879

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	ALA	0	0.034	0.025	3.856	7.633	9.194	-0.009	-0.630	-0.921	-0.002
4	A	5	VAL	0	0.027	0.013	5.213	3.448	3.510	-0.001	-0.008	-0.053	0.000
48	A	49	ASP	-1	-0.905	-0.948	3.132	-84.956	-82.054	0.074	-1.563	-1.413	-0.014
49	A	50	VAL	0	-0.056	-0.044	2.118	7.529	8.756	2.480	-1.143	-2.563	-0.006
50	A	51	SER	0	0.007	0.015	4.476	4.843	5.056	-0.001	-0.044	-0.168	0.000
78	A	79	ALA	0	0.031	-0.002	3.345	-2.663	-2.447	0.010	-0.055	-0.172	0.000
79	A	80	ARG	1	0.925	0.948	2.417	24.418	27.158	1.149	-1.496	-2.393	-0.011
80	A	81	PRO	0	0.021	0.035	4.250	4.412	4.508	0.000	-0.031	-0.064	0.000
5	A	6	GLY	0	0.007	0.001	8.828	-0.325	-0.325	0.000	0.000	0.000	0.000
6	A	7	MET	0	-0.056	-0.023	11.579	1.465	1.465	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.034	0.013	15.199	0.123	0.123	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.765	-0.813	18.454	-12.935	-12.935	0.000	0.000	0.000	0.000
9	A	10	THR	0	0.016	-0.008	21.654	-0.022	-0.022	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.830	0.911	25.131	10.488	10.488	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.006	0.005	28.819	0.132	0.132	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.004	-0.010	26.354	-0.318	-0.318	0.000	0.000	0.000	0.000
13	A	14	PRO	0	0.036	0.000	27.388	-0.375	-0.375	0.000	0.000	0.000	0.000
14	A	15	ALA	0	0.053	0.029	26.491	-0.230	-0.230	0.000	0.000	0.000	0.000
15	A	16	VAL	0	0.020	0.017	22.288	-0.508	-0.508	0.000	0.000	0.000	0.000
16	A	17	VAL	0	-0.019	-0.008	22.575	-0.639	-0.639	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.884	-0.945	23.317	-13.122	-13.122	0.000	0.000	0.000	0.000
18	A	19	ALA	0	-0.034	-0.013	20.106	-0.522	-0.522	0.000	0.000	0.000	0.000
19	A	20	ALA	0	0.028	-0.001	18.637	-0.937	-0.937	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.826	-0.886	18.813	-14.273	-14.273	0.000	0.000	0.000	0.000
21	A	22	ALA	0	0.017	0.000	20.022	-0.473	-0.473	0.000	0.000	0.000	0.000
22	A	23	MET	0	-0.070	-0.030	14.030	-0.510	-0.510	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.023	-0.021	15.427	-1.001	-1.001	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.782	0.882	16.502	13.331	13.331	0.000	0.000	0.000	0.000
25	A	26	ALA	0	-0.040	-0.004	16.013	0.314	0.314	0.000	0.000	0.000	0.000
26	A	27	ALA	0	-0.048	-0.016	11.258	-0.613	-0.613	0.000	0.000	0.000	0.000
27	A	28	ARG	1	0.927	0.959	10.035	25.633	25.633	0.000	0.000	0.000	0.000
28	A	29	VAL	0	-0.048	-0.025	9.176	-3.648	-3.648	0.000	0.000	0.000	0.000
29	A	30	THR	0	0.055	0.038	11.370	1.338	1.338	0.000	0.000	0.000	0.000
30	A	31	LEU	0	0.001	-0.008	13.425	-1.047	-1.047	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.033	-0.017	13.295	0.542	0.542	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.008	0.017	16.265	0.873	0.873	0.000	0.000	0.000	0.000
33	A	34	TYR	0	-0.038	-0.032	18.212	0.129	0.129	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.862	-0.923	20.399	-13.118	-13.118	0.000	0.000	0.000	0.000
35	A	36	LYS	1	0.885	0.931	22.360	11.645	11.645	0.000	0.000	0.000	0.000
36	A	37	ILE	0	0.054	0.037	23.636	0.238	0.238	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.028	0.028	26.735	0.349	0.349	0.000	0.000	0.000	0.000
38	A	39	SER	0	0.000	-0.017	29.534	-0.107	-0.107	0.000	0.000	0.000	0.000
39	A	40	GLY	0	0.007	0.001	31.239	-0.030	-0.030	0.000	0.000	0.000	0.000
40	A	41	ARG	1	0.793	0.877	24.342	12.050	12.050	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.036	-0.017	24.925	0.134	0.134	0.000	0.000	0.000	0.000
42	A	43	THR	0	0.015	0.004	18.412	-0.246	-0.246	0.000	0.000	0.000	0.000
43	A	44	VAL	0	-0.011	0.008	18.439	0.293	0.293	0.000	0.000	0.000	0.000
44	A	45	ILE	0	-0.032	-0.020	13.448	-0.681	-0.681	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.051	0.022	11.249	0.537	0.537	0.000	0.000	0.000	0.000
46	A	47	ARG	1	0.737	0.829	6.547	30.919	30.919	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.108	0.049	7.196	3.532	3.532	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.791	-0.895	6.717	-26.199	-26.199	0.000	0.000	0.000	0.000
52	A	53	VAL	0	0.004	0.024	7.168	4.273	4.273	0.000	0.000	0.000	0.000
53	A	54	GLN	0	-0.028	-0.030	8.551	2.672	2.672	0.000	0.000	0.000	0.000
54	A	55	ALA	0	0.002	0.008	10.546	2.431	2.431	0.000	0.000	0.000	0.000
55	A	56	SER	0	-0.003	-0.009	11.266	1.992	1.992	0.000	0.000	0.000	0.000
56	A	57	VAL	0	0.015	0.001	12.614	1.743	1.743	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.007	-0.003	14.580	1.544	1.544	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.038	0.017	16.497	1.202	1.202	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.052	0.038	17.419	1.054	1.054	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.006	-0.013	18.327	1.101	1.101	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.878	-0.943	20.545	-13.264	-13.264	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.083	-0.042	21.954	0.915	0.915	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.041	0.018	23.018	0.639	0.639	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.831	0.901	23.744	13.666	13.666	0.000	0.000	0.000	0.000
65	A	66	ARG	1	0.869	0.950	24.378	12.779	12.779	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.020	0.012	27.299	0.371	0.371	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.008	-0.010	29.961	0.136	0.136	0.000	0.000	0.000	0.000
68	A	69	GLY	0	-0.004	-0.004	33.260	0.001	0.001	0.000	0.000	0.000	0.000
69	A	70	GLY	0	-0.014	0.003	29.220	-0.092	-0.092	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.823	-0.909	28.438	-10.272	-10.272	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.006	-0.012	21.778	-0.206	-0.206	0.000	0.000	0.000	0.000
72	A	73	LEU	0	-0.101	-0.040	23.858	0.306	0.306	0.000	0.000	0.000	0.000
73	A	74	SER	0	-0.038	-0.050	20.190	-0.182	-0.182	0.000	0.000	0.000	0.000
74	A	75	THR	0	0.025	0.000	16.592	0.008	0.008	0.000	0.000	0.000	0.000
75	A	76	HIS	0	-0.014	0.005	12.459	0.397	0.397	0.000	0.000	0.000	0.000
76	A	77	ILE	0	0.020	0.011	7.628	-0.847	-0.847	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.019	0.009	7.498	0.519	0.519	0.000	0.000	0.000	0.000
81	A	82	HIS	0	0.025	0.009	7.247	-1.208	-1.208	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.806	-0.907	9.747	-20.835	-20.835	0.000	0.000	0.000	0.000
83	A	84	ASN	0	-0.011	-0.015	11.121	1.326	1.326	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.017	-0.013	11.547	0.887	0.887	0.000	0.000	0.000	0.000
85	A	86	GLU	-1	-0.795	-0.870	9.264	-27.284	-27.284	0.000	0.000	0.000	0.000
86	A	87	TYR	0	-0.079	-0.051	13.560	1.324	1.324	0.000	0.000	0.000	0.000
87	A	88	VAL	0	-0.050	-0.016	16.625	1.049	1.049	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.007	0.001	14.822	0.665	0.665	0.000	0.000	0.000	0.000
89	A	90	PRO	0	-0.016	0.002	16.436	-0.676	-0.676	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.024	-0.034	10.383	-0.403	-0.403	0.000	0.000	0.000	0.000
91	A	92	ARG	1	0.924	0.997	12.182	14.494	14.494	0.000	0.000	0.000	0.000
92	A	93	TYR	0	0.062	0.028	9.998	-0.831	-0.831	0.000	0.000	0.000	0.000
93	A	94	THR	0	-0.039	-0.036	14.991	1.143	1.143	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.808	-0.897	18.725	-14.444	-14.444	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.032	-0.026	20.728	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	97	VAL	0	-0.066	-0.039	16.512	0.237	0.237	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.902	-0.945	15.302	-20.958	-20.958	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.138	-0.080	18.018	0.438	0.438	0.000	0.000	0.000	0.000
99	A	100	PHE	-1	-0.988	-0.965	17.479	-16.342	-16.342	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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