FMO DATABASE

FMODB ID: 7KL2K

Calculation Name: 5IVU-B-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5IVU

Chain ID: B

ChEMBL ID:

UniProt ID: D9XKI5

Base Structure: X-ray

Registration Date: 2025-10-05

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	136
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1242390.289965
FMO2-HF: Nuclear repulsion	1188295.335781
FMO2-HF: Total energy	-54094.954184
FMO2-MP2: Total energy	-54252.825085

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:6:GLY)

Summations of interaction energy for fragment #1(A:6:GLY)

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.
-101.126	-100.138	-0.012	-0.389	-0.588	-0.002

Interaction energy analysis for fragmet #1(A:6:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.813 / q_NPA : 0.892

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	8	THR	0	-0.001	0.008	3.841	4.625	5.527	-0.011	-0.351	-0.541	-0.002
33	A	38	THR	0	-0.037	-0.025	4.174	-7.418	-7.332	-0.001	-0.038	-0.047	0.000
4	A	9	LEU	0	0.004	-0.009	6.785	0.806	0.806	0.000	0.000	0.000	0.000
5	A	10	ASN	0	-0.011	-0.017	10.515	-0.628	-0.628	0.000	0.000	0.000	0.000
6	A	11	ASP	-1	-0.855	-0.927	13.397	-19.044	-19.044	0.000	0.000	0.000	0.000
7	A	12	ALA	0	0.042	0.016	16.345	0.724	0.724	0.000	0.000	0.000	0.000
8	A	13	CYS	0	-0.085	-0.012	13.996	1.030	1.030	0.000	0.000	0.000	0.000
9	A	14	VAL	0	0.022	0.011	16.795	0.756	0.756	0.000	0.000	0.000	0.000
10	A	15	GLU	-1	-0.939	-0.966	19.352	-14.132	-14.132	0.000	0.000	0.000	0.000
11	A	16	THR	0	0.018	-0.013	21.002	0.895	0.895	0.000	0.000	0.000	0.000
12	A	17	TYR	0	0.012	-0.015	21.388	0.649	0.649	0.000	0.000	0.000	0.000
13	A	18	GLN	0	-0.016	-0.016	23.172	0.581	0.581	0.000	0.000	0.000	0.000
14	A	19	GLN	0	-0.024	-0.016	25.375	0.342	0.342	0.000	0.000	0.000	0.000
15	A	20	LEU	0	-0.014	0.004	25.650	0.440	0.440	0.000	0.000	0.000	0.000
16	A	21	LYS	1	0.883	0.953	25.004	12.845	12.845	0.000	0.000	0.000	0.000
17	A	22	LEU	0	-0.059	-0.019	28.815	0.465	0.465	0.000	0.000	0.000	0.000
18	A	23	GLY	0	0.031	0.002	31.227	0.410	0.410	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.833	0.915	33.089	9.311	9.311	0.000	0.000	0.000	0.000
20	A	25	LYS	1	0.913	0.946	31.346	9.561	9.561	0.000	0.000	0.000	0.000
21	A	26	LEU	0	0.000	0.011	26.143	-0.132	-0.132	0.000	0.000	0.000	0.000
22	A	27	LYS	1	0.872	0.961	30.097	9.697	9.697	0.000	0.000	0.000	0.000
23	A	28	TYR	0	-0.017	-0.046	25.635	0.018	0.018	0.000	0.000	0.000	0.000
24	A	29	ILE	0	-0.041	-0.015	20.786	0.034	0.034	0.000	0.000	0.000	0.000
25	A	30	ILE	0	0.023	0.026	19.889	-0.098	-0.098	0.000	0.000	0.000	0.000
26	A	31	PHE	0	0.012	-0.015	15.690	-0.388	-0.388	0.000	0.000	0.000	0.000
27	A	32	HIS	0	0.028	0.007	14.909	-0.289	-0.289	0.000	0.000	0.000	0.000
28	A	33	LEU	0	-0.053	-0.022	8.069	-1.729	-1.729	0.000	0.000	0.000	0.000
29	A	34	ASN	0	0.031	0.016	10.338	2.107	2.107	0.000	0.000	0.000	0.000
30	A	35	LYS	1	0.820	0.879	9.301	21.856	21.856	0.000	0.000	0.000	0.000
31	A	36	GLU	-1	-0.922	-0.951	8.359	-32.628	-32.628	0.000	0.000	0.000	0.000
32	A	37	ASN	0	-0.026	-0.014	6.555	-2.262	-2.262	0.000	0.000	0.000	0.000
34	A	39	GLU	-1	-0.781	-0.864	5.591	-30.877	-30.877	0.000	0.000	0.000	0.000
35	A	40	ILE	0	-0.002	0.005	8.300	1.700	1.700	0.000	0.000	0.000	0.000
36	A	41	ALA	0	-0.001	-0.007	10.794	0.892	0.892	0.000	0.000	0.000	0.000
37	A	42	VAL	0	-0.001	-0.007	14.187	0.252	0.252	0.000	0.000	0.000	0.000
38	A	43	GLU	-1	-0.883	-0.918	17.902	-16.502	-16.502	0.000	0.000	0.000	0.000
39	A	44	LYS	1	0.837	0.889	19.507	12.856	12.856	0.000	0.000	0.000	0.000
40	A	45	SER	0	-0.014	-0.005	22.798	-0.320	-0.320	0.000	0.000	0.000	0.000
41	A	46	SER	0	-0.008	-0.005	25.126	0.332	0.332	0.000	0.000	0.000	0.000
42	A	47	ASP	-1	-0.877	-0.948	28.620	-9.907	-9.907	0.000	0.000	0.000	0.000
43	A	48	SER	0	-0.026	0.004	32.001	0.373	0.373	0.000	0.000	0.000	0.000
44	A	49	VAL	0	-0.002	-0.019	32.776	-0.235	-0.235	0.000	0.000	0.000	0.000
45	A	50	ASP	-1	-0.875	-0.927	35.196	-8.788	-8.788	0.000	0.000	0.000	0.000
46	A	51	TYR	0	-0.020	-0.032	29.938	-0.393	-0.393	0.000	0.000	0.000	0.000
47	A	52	ASP	-1	-0.845	-0.931	31.995	-9.365	-9.365	0.000	0.000	0.000	0.000
48	A	53	ASN	0	-0.078	-0.049	31.728	0.031	0.031	0.000	0.000	0.000	0.000
49	A	54	PHE	0	-0.031	-0.010	24.580	-0.480	-0.480	0.000	0.000	0.000	0.000
50	A	55	LEU	0	-0.009	-0.012	27.595	-0.457	-0.457	0.000	0.000	0.000	0.000
51	A	56	ALA	0	-0.009	-0.002	28.563	-0.244	-0.244	0.000	0.000	0.000	0.000
52	A	57	ASP	-1	-0.812	-0.860	25.305	-12.106	-12.106	0.000	0.000	0.000	0.000
53	A	58	LEU	0	-0.053	-0.016	22.862	-0.881	-0.881	0.000	0.000	0.000	0.000
54	A	59	PRO	0	0.005	0.001	21.220	0.421	0.421	0.000	0.000	0.000	0.000
55	A	60	GLU	-1	-0.900	-0.950	23.835	-11.251	-11.251	0.000	0.000	0.000	0.000
56	A	61	ASP	-1	-0.929	-0.955	23.262	-13.493	-13.493	0.000	0.000	0.000	0.000
57	A	62	GLU	-1	-0.858	-0.928	17.436	-18.592	-18.592	0.000	0.000	0.000	0.000
58	A	63	CYS	0	-0.099	-0.040	15.944	0.424	0.424	0.000	0.000	0.000	0.000
59	A	64	ARG	1	0.751	0.868	17.057	16.628	16.628	0.000	0.000	0.000	0.000
60	A	65	TRP	0	-0.025	-0.011	10.482	-0.549	-0.549	0.000	0.000	0.000	0.000
61	A	66	ALA	0	0.018	0.012	17.912	0.097	0.097	0.000	0.000	0.000	0.000
62	A	67	VAL	0	-0.041	-0.017	20.870	-0.115	-0.115	0.000	0.000	0.000	0.000
63	A	68	TYR	0	0.047	0.024	23.255	0.187	0.187	0.000	0.000	0.000	0.000
64	A	69	ASP	-1	-0.809	-0.894	27.038	-9.935	-9.935	0.000	0.000	0.000	0.000
65	A	70	LEU	0	0.010	0.005	29.922	0.336	0.336	0.000	0.000	0.000	0.000
66	A	71	GLU	-1	-0.886	-0.949	32.024	-8.252	-8.252	0.000	0.000	0.000	0.000
67	A	72	TYR	0	-0.054	-0.029	34.718	-0.098	-0.098	0.000	0.000	0.000	0.000
68	A	73	GLU	-1	-0.912	-0.959	37.215	-7.743	-7.743	0.000	0.000	0.000	0.000
69	A	74	LYS	0	-0.043	0.001	37.662	0.183	0.183	0.000	0.000	0.000	0.000
70	A	75	GLU	-1	-0.815	-0.920	40.272	-7.601	-7.601	0.000	0.000	0.000	0.000
71	A	76	GLU	-1	-0.923	-0.951	42.624	-7.178	-7.178	0.000	0.000	0.000	0.000
72	A	77	GLY	0	-0.056	-0.029	46.147	0.011	0.011	0.000	0.000	0.000	0.000
73	A	78	ALA	0	-0.102	-0.054	45.534	0.125	0.125	0.000	0.000	0.000	0.000
74	A	79	GLY	0	-0.058	-0.044	45.382	0.115	0.115	0.000	0.000	0.000	0.000
75	A	80	LYS	1	0.836	0.914	40.158	7.973	7.973	0.000	0.000	0.000	0.000
76	A	81	ARG	1	0.904	0.959	36.884	8.327	8.327	0.000	0.000	0.000	0.000
77	A	82	ASN	0	-0.017	-0.021	33.219	0.230	0.230	0.000	0.000	0.000	0.000
78	A	83	LYS	1	0.864	0.936	30.409	9.685	9.685	0.000	0.000	0.000	0.000
79	A	84	LEU	0	-0.029	-0.004	26.388	-0.147	-0.147	0.000	0.000	0.000	0.000
80	A	85	THR	0	0.042	0.025	26.058	-0.088	-0.088	0.000	0.000	0.000	0.000
81	A	86	PHE	0	-0.007	-0.012	16.465	-0.457	-0.457	0.000	0.000	0.000	0.000
82	A	87	VAL	0	0.030	0.013	21.605	0.363	0.363	0.000	0.000	0.000	0.000
83	A	88	SER	0	-0.037	-0.029	18.190	-1.323	-1.323	0.000	0.000	0.000	0.000
84	A	89	TRP	0	-0.012	0.003	19.373	0.496	0.496	0.000	0.000	0.000	0.000
85	A	90	ALA	0	-0.021	-0.039	18.298	-1.177	-1.177	0.000	0.000	0.000	0.000
86	A	91	PRO	0	0.073	0.057	19.918	0.271	0.271	0.000	0.000	0.000	0.000
87	A	92	ASP	-1	-0.886	-0.960	22.218	-12.846	-12.846	0.000	0.000	0.000	0.000
88	A	93	SER	0	-0.039	-0.030	23.685	-0.361	-0.361	0.000	0.000	0.000	0.000
89	A	94	ALA	0	0.023	0.043	18.832	-0.324	-0.324	0.000	0.000	0.000	0.000
90	A	95	LYS	1	0.938	0.945	17.001	15.311	15.311	0.000	0.000	0.000	0.000
91	A	96	MET	0	0.083	0.031	16.700	-1.200	-1.200	0.000	0.000	0.000	0.000
92	A	97	LYS	1	0.933	0.960	10.629	25.368	25.368	0.000	0.000	0.000	0.000
93	A	98	GLN	0	-0.019	-0.006	11.964	-1.477	-1.477	0.000	0.000	0.000	0.000
94	A	99	LYS	1	0.935	0.973	13.234	13.715	13.715	0.000	0.000	0.000	0.000
95	A	100	MET	0	-0.035	-0.015	12.103	-0.335	-0.335	0.000	0.000	0.000	0.000
96	A	101	ALA	0	-0.012	0.021	8.850	-1.519	-1.519	0.000	0.000	0.000	0.000
97	A	102	TYR	0	0.102	0.042	9.384	-2.165	-2.165	0.000	0.000	0.000	0.000
98	A	103	ALA	0	-0.005	-0.006	12.072	0.267	0.267	0.000	0.000	0.000	0.000
99	A	104	SER	0	-0.072	-0.059	8.179	-1.091	-1.091	0.000	0.000	0.000	0.000
100	A	105	SER	0	0.001	-0.006	7.369	-3.619	-3.619	0.000	0.000	0.000	0.000
101	A	106	LYS	1	0.897	0.968	8.906	18.480	18.480	0.000	0.000	0.000	0.000
102	A	107	ASP	-1	-0.851	-0.945	12.337	-18.865	-18.865	0.000	0.000	0.000	0.000
103	A	108	ILE	0	-0.066	-0.022	6.564	0.881	0.881	0.000	0.000	0.000	0.000
104	A	109	LEU	0	0.030	0.025	11.021	0.977	0.977	0.000	0.000	0.000	0.000
105	A	110	ARG	1	0.836	0.904	13.672	16.074	16.074	0.000	0.000	0.000	0.000
106	A	111	ARG	1	0.930	0.973	13.366	20.999	20.999	0.000	0.000	0.000	0.000
107	A	112	ALA	0	-0.006	0.005	14.992	0.790	0.790	0.000	0.000	0.000	0.000
108	A	113	LEU	0	-0.010	0.010	17.002	0.995	0.995	0.000	0.000	0.000	0.000
109	A	114	THR	0	0.015	-0.002	19.777	0.660	0.660	0.000	0.000	0.000	0.000
110	A	115	GLY	0	-0.035	-0.016	22.656	0.292	0.292	0.000	0.000	0.000	0.000
111	A	116	ILE	0	-0.038	-0.002	21.572	0.312	0.312	0.000	0.000	0.000	0.000
112	A	117	ALA	0	-0.061	-0.036	24.806	0.038	0.038	0.000	0.000	0.000	0.000
113	A	118	VAL	0	0.032	0.039	26.659	0.331	0.331	0.000	0.000	0.000	0.000
114	A	119	GLU	-1	-0.898	-0.947	20.727	-15.082	-15.082	0.000	0.000	0.000	0.000
115	A	120	ILE	0	0.009	0.012	23.860	0.345	0.345	0.000	0.000	0.000	0.000
116	A	121	GLN	0	-0.023	-0.013	19.044	-1.008	-1.008	0.000	0.000	0.000	0.000
117	A	122	GLY	0	0.003	0.002	22.488	0.632	0.632	0.000	0.000	0.000	0.000
118	A	123	THR	0	-0.127	-0.075	22.771	-0.718	-0.718	0.000	0.000	0.000	0.000
119	A	124	ASP	-1	-0.740	-0.869	24.779	-10.366	-10.366	0.000	0.000	0.000	0.000
120	A	125	PHE	0	0.032	0.004	27.399	-0.051	-0.051	0.000	0.000	0.000	0.000
121	A	126	SER	0	-0.085	-0.060	29.766	0.172	0.172	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.824	-0.898	27.204	-11.327	-11.327	0.000	0.000	0.000	0.000
123	A	128	VAL	0	0.004	-0.001	25.336	-0.090	-0.090	0.000	0.000	0.000	0.000
124	A	129	ALA	0	0.037	0.040	28.658	0.063	0.063	0.000	0.000	0.000	0.000
125	A	130	HIS	0	-0.006	-0.008	32.351	0.116	0.116	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.895	-0.952	33.966	-8.183	-8.183	0.000	0.000	0.000	0.000
127	A	132	ASN	0	-0.001	-0.001	32.317	-0.057	-0.057	0.000	0.000	0.000	0.000
128	A	133	VAL	0	-0.008	-0.008	29.029	-0.185	-0.185	0.000	0.000	0.000	0.000
129	A	134	LEU	0	-0.037	-0.016	31.508	-0.088	-0.088	0.000	0.000	0.000	0.000
130	A	135	ASP	-1	-0.726	-0.834	34.717	-8.737	-8.737	0.000	0.000	0.000	0.000
131	A	136	LYS	1	0.842	0.922	29.029	10.216	10.216	0.000	0.000	0.000	0.000
132	A	137	ALA	0	0.006	0.000	31.583	-0.071	-0.071	0.000	0.000	0.000	0.000
133	A	138	SER	-1	-0.792	-0.875	32.767	-8.522	-8.522	0.000	0.000	0.000	0.000
134	A	139	ARG	1	0.724	0.835	33.596	9.140	9.140	0.000	0.000	0.000	0.000
135	A	140	GLY	0	-0.095	-0.049	33.056	-0.124	-0.124	0.000	0.000	0.000	0.000
136	A	141	HIS	-1	-0.827	-0.914	27.462	-11.047	-11.047	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:6:GLY)