FMO DATABASE

FMODB ID: 2RMQR

Calculation Name: 4IT7-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4IT7

Chain ID: A

ChEMBL ID:

UniProt ID: E9N3T6

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	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-741065.209643
FMO2-HF: Nuclear repulsion	700403.659238
FMO2-HF: Total energy	-40661.550404
FMO2-MP2: Total energy	-40778.881078

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.
14.34	16.318	0.74	-1.008	-1.708	-0.007

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 : 0.875 / q_NPA : 0.928

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	PHE	0	-0.033	-0.026	3.829	-5.869	-5.133	-0.012	-0.381	-0.343	0.000
45	A	50	GLN	0	-0.016	0.002	3.972	1.715	1.848	-0.001	-0.026	-0.106	0.000
46	A	51	VAL	0	0.012	0.003	4.306	4.563	4.643	-0.001	-0.010	-0.069	0.000
47	A	52	VAL	0	-0.049	-0.023	2.433	-11.686	-10.779	0.754	-0.555	-1.105	-0.007
48	A	53	ALA	0	0.044	0.023	4.190	3.889	4.011	0.000	-0.036	-0.085	0.000
4	A	9	SER	0	-0.017	0.005	6.812	1.831	1.831	0.000	0.000	0.000	0.000
5	A	10	THR	0	0.029	-0.001	8.960	0.008	0.008	0.000	0.000	0.000	0.000
6	A	11	LYS	1	0.862	0.931	12.681	20.951	20.951	0.000	0.000	0.000	0.000
7	A	12	ASP	-1	-0.802	-0.906	14.917	-14.121	-14.121	0.000	0.000	0.000	0.000
8	A	13	VAL	0	0.009	-0.006	18.635	-0.411	-0.411	0.000	0.000	0.000	0.000
9	A	14	ASN	0	-0.051	-0.018	20.614	0.771	0.771	0.000	0.000	0.000	0.000
10	A	15	ASP	-1	-0.807	-0.885	17.461	-17.087	-17.087	0.000	0.000	0.000	0.000
11	A	16	PRO	0	0.046	0.006	20.770	-0.075	-0.075	0.000	0.000	0.000	0.000
12	A	17	LYS	1	0.823	0.907	16.270	18.506	18.506	0.000	0.000	0.000	0.000
13	A	18	ILE	0	0.000	-0.003	15.042	-0.339	-0.339	0.000	0.000	0.000	0.000
14	A	19	GLN	0	0.004	-0.008	19.023	0.531	0.531	0.000	0.000	0.000	0.000
15	A	20	ALA	0	-0.008	0.003	21.960	0.332	0.332	0.000	0.000	0.000	0.000
16	A	21	LEU	0	-0.066	-0.035	16.223	0.217	0.217	0.000	0.000	0.000	0.000
17	A	22	ALA	0	0.037	0.020	20.422	0.155	0.155	0.000	0.000	0.000	0.000
18	A	23	GLY	0	0.032	0.020	22.223	0.412	0.412	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.788	0.875	20.818	14.916	14.916	0.000	0.000	0.000	0.000
20	A	25	ALA	0	0.040	0.014	20.992	0.186	0.186	0.000	0.000	0.000	0.000
21	A	26	LEU	0	0.024	0.017	23.053	0.212	0.212	0.000	0.000	0.000	0.000
22	A	27	GLN	0	-0.018	-0.013	26.582	0.004	0.004	0.000	0.000	0.000	0.000
23	A	28	ARG	1	0.883	0.944	23.238	13.023	13.023	0.000	0.000	0.000	0.000
24	A	29	ILE	0	0.013	0.005	24.052	0.204	0.204	0.000	0.000	0.000	0.000
25	A	30	ASN	0	-0.027	-0.026	27.341	0.231	0.231	0.000	0.000	0.000	0.000
26	A	31	ALA	0	-0.025	-0.008	29.281	0.348	0.348	0.000	0.000	0.000	0.000
27	A	32	ALA	0	-0.002	0.004	27.824	0.195	0.195	0.000	0.000	0.000	0.000
28	A	33	SER	0	-0.040	-0.006	29.811	0.216	0.216	0.000	0.000	0.000	0.000
29	A	34	ASN	0	0.020	-0.011	31.552	0.230	0.230	0.000	0.000	0.000	0.000
30	A	35	ASP	-1	-0.842	-0.902	34.372	-8.568	-8.568	0.000	0.000	0.000	0.000
31	A	36	LEU	0	0.035	0.007	36.238	-0.038	-0.038	0.000	0.000	0.000	0.000
32	A	37	PHE	0	-0.060	-0.019	37.950	0.190	0.190	0.000	0.000	0.000	0.000
33	A	38	GLN	0	-0.003	0.003	34.575	-0.566	-0.566	0.000	0.000	0.000	0.000
34	A	39	GLN	0	-0.034	-0.018	30.873	0.076	0.076	0.000	0.000	0.000	0.000
35	A	40	THR	0	0.020	0.012	31.337	-0.179	-0.179	0.000	0.000	0.000	0.000
36	A	41	ILE	0	-0.010	-0.007	25.393	-0.154	-0.154	0.000	0.000	0.000	0.000
37	A	42	VAL	0	-0.023	-0.001	28.976	0.272	0.272	0.000	0.000	0.000	0.000
38	A	43	LYS	1	0.940	0.954	25.877	11.737	11.737	0.000	0.000	0.000	0.000
39	A	44	VAL	0	0.038	0.024	20.115	-0.146	-0.146	0.000	0.000	0.000	0.000
40	A	45	ILE	0	-0.058	-0.026	21.713	0.302	0.302	0.000	0.000	0.000	0.000
41	A	46	SER	0	-0.050	-0.059	17.459	-0.441	-0.441	0.000	0.000	0.000	0.000
42	A	47	ALA	0	0.061	0.020	15.806	0.160	0.160	0.000	0.000	0.000	0.000
43	A	48	LYS	1	0.925	0.983	10.839	25.610	25.610	0.000	0.000	0.000	0.000
44	A	49	THR	0	0.029	0.012	9.380	1.278	1.278	0.000	0.000	0.000	0.000
49	A	54	GLY	0	0.070	0.057	7.971	3.657	3.657	0.000	0.000	0.000	0.000
50	A	55	THR	0	-0.028	-0.024	7.736	-5.588	-5.588	0.000	0.000	0.000	0.000
51	A	56	ASN	0	-0.016	-0.006	8.006	5.055	5.055	0.000	0.000	0.000	0.000
52	A	57	THR	0	0.021	0.000	9.083	-3.067	-3.067	0.000	0.000	0.000	0.000
53	A	58	VAL	0	-0.054	-0.031	11.280	0.838	0.838	0.000	0.000	0.000	0.000
54	A	59	LEU	0	0.003	-0.005	13.485	-0.148	-0.148	0.000	0.000	0.000	0.000
55	A	60	GLU	-1	-0.859	-0.882	17.008	-16.357	-16.357	0.000	0.000	0.000	0.000
56	A	61	LEU	0	-0.021	-0.015	19.986	0.289	0.289	0.000	0.000	0.000	0.000
57	A	62	LEU	0	0.018	0.019	23.291	0.213	0.213	0.000	0.000	0.000	0.000
58	A	63	ILE	0	0.000	-0.008	26.639	0.133	0.133	0.000	0.000	0.000	0.000
59	A	64	ALA	0	0.023	0.006	29.266	0.131	0.131	0.000	0.000	0.000	0.000
60	A	65	PRO	0	0.042	0.046	33.040	-0.051	-0.051	0.000	0.000	0.000	0.000
61	A	66	THR	0	-0.019	-0.025	35.419	0.154	0.154	0.000	0.000	0.000	0.000
62	A	67	SER	0	0.017	-0.001	38.081	0.000	0.000	0.000	0.000	0.000	0.000
63	A	68	CYS	0	-0.056	-0.011	36.162	0.433	0.433	0.000	0.000	0.000	0.000
64	A	69	ARG	1	0.868	0.926	39.079	7.010	7.010	0.000	0.000	0.000	0.000
65	A	70	LYS	1	0.867	0.928	33.578	9.482	9.482	0.000	0.000	0.000	0.000
66	A	71	ASN	0	-0.046	-0.011	39.017	-0.131	-0.131	0.000	0.000	0.000	0.000
67	A	72	GLU	-1	-0.848	-0.927	41.662	-6.906	-6.906	0.000	0.000	0.000	0.000
68	A	73	THR	0	-0.049	-0.028	41.612	-0.152	-0.152	0.000	0.000	0.000	0.000
69	A	74	SER	0	0.054	0.036	39.845	0.124	0.124	0.000	0.000	0.000	0.000
70	A	75	ALA	0	-0.004	-0.007	41.667	-0.127	-0.127	0.000	0.000	0.000	0.000
71	A	76	GLY	0	-0.006	-0.008	40.770	0.111	0.111	0.000	0.000	0.000	0.000
72	A	77	ASN	0	-0.068	-0.030	36.128	-0.126	-0.126	0.000	0.000	0.000	0.000
73	A	79	GLU	-1	-0.819	-0.915	36.038	-8.964	-8.964	0.000	0.000	0.000	0.000
74	A	80	ALA	0	-0.010	-0.010	34.820	0.063	0.063	0.000	0.000	0.000	0.000
75	A	81	VAL	0	-0.008	0.001	36.865	0.213	0.213	0.000	0.000	0.000	0.000
76	A	82	SER	0	0.015	-0.008	38.560	-0.204	-0.204	0.000	0.000	0.000	0.000
77	A	83	ASN	0	-0.055	-0.009	39.230	-0.308	-0.308	0.000	0.000	0.000	0.000
78	A	84	GLY	0	0.058	0.026	37.325	0.196	0.196	0.000	0.000	0.000	0.000
79	A	85	THR	0	-0.007	-0.019	34.837	-0.068	-0.068	0.000	0.000	0.000	0.000
80	A	86	LYS	1	0.885	0.947	31.379	8.990	8.990	0.000	0.000	0.000	0.000
81	A	87	GLN	0	0.032	0.010	28.573	-0.144	-0.144	0.000	0.000	0.000	0.000
82	A	88	ILE	0	0.002	0.011	23.144	-0.125	-0.125	0.000	0.000	0.000	0.000
83	A	89	CYS	0	-0.046	-0.018	22.829	-0.097	-0.097	0.000	0.000	0.000	0.000
84	A	90	THR	0	-0.003	0.011	17.446	-0.461	-0.461	0.000	0.000	0.000	0.000
85	A	91	VAL	0	-0.031	-0.023	18.228	0.323	0.323	0.000	0.000	0.000	0.000
86	A	92	ALA	0	-0.008	-0.001	13.701	-1.163	-1.163	0.000	0.000	0.000	0.000
87	A	93	ILE	0	0.001	-0.006	14.043	1.350	1.350	0.000	0.000	0.000	0.000
88	A	94	TRP	0	-0.028	-0.015	10.488	-1.271	-1.271	0.000	0.000	0.000	0.000
89	A	95	GLU	-1	-0.800	-0.895	12.517	-18.447	-18.447	0.000	0.000	0.000	0.000
90	A	96	LYS	1	0.824	0.903	12.548	18.235	18.235	0.000	0.000	0.000	0.000
91	A	97	PRO	0	0.011	-0.006	14.326	1.179	1.179	0.000	0.000	0.000	0.000
92	A	98	TRP	0	-0.003	-0.006	11.479	0.397	0.397	0.000	0.000	0.000	0.000
93	A	99	GLU	-1	-0.830	-0.895	16.850	-18.106	-18.106	0.000	0.000	0.000	0.000
94	A	100	ASN	0	-0.064	-0.031	19.666	0.751	0.751	0.000	0.000	0.000	0.000
95	A	101	PHE	0	-0.017	0.009	15.449	0.463	0.463	0.000	0.000	0.000	0.000
96	A	102	GLU	-1	-0.787	-0.890	17.288	-16.484	-16.484	0.000	0.000	0.000	0.000
97	A	103	GLU	-1	-0.904	-0.939	16.757	-17.481	-17.481	0.000	0.000	0.000	0.000
98	A	104	ILE	0	-0.018	-0.026	17.084	-0.990	-0.990	0.000	0.000	0.000	0.000
99	A	105	THR	0	0.005	0.008	17.149	1.251	1.251	0.000	0.000	0.000	0.000
100	A	106	ILE	0	-0.003	-0.009	18.529	-0.740	-0.740	0.000	0.000	0.000	0.000
101	A	107	LYS	1	0.884	0.941	15.925	18.111	18.111	0.000	0.000	0.000	0.000
102	A	108	GLU	-1	-0.822	-0.905	19.707	-14.457	-14.457	0.000	0.000	0.000	0.000
103	A	110	LYS	1	0.896	0.947	22.598	14.251	14.251	0.000	0.000	0.000	0.000
104	A	111	SER	0	0.015	-0.008	27.931	-0.121	-0.121	0.000	0.000	0.000	0.000
105	A	112	ALA	-1	-0.933	-0.950	28.636	-10.370	-10.370	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:GLY)