FMO DATABASE

FMODB ID: 3ZJML

Calculation Name: 3IFT-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3IFT

Chain ID: A

ChEMBL ID:

UniProt ID: P9WN55

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1141785.263206
FMO2-HF: Nuclear repulsion	1091624.442437
FMO2-HF: Total energy	-50160.820768
FMO2-MP2: Total energy	-50310.555678

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:-1:HIS)

Summations of interaction energy for fragment #1(A:-1:HIS)

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.
-696.586	-695.916	31.449	-17.137	-14.983	-0.221

Interaction energy analysis for fragmet #1(A:-1:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.630 / q_NPA : 1.779

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	1	VAL	0	0.024	0.028	1.821	-34.548	-34.422	9.631	-5.087	-4.670	-0.062
4	A	2	SER	0	-0.020	-0.038	4.170	11.069	11.240	-0.001	-0.022	-0.148	0.000
136	A	134	GLU	-2	-1.610	-1.760	1.756	-282.733	-282.360	21.819	-12.028	-10.165	-0.159
5	A	3	ASP	-1	-0.851	-0.928	6.039	-52.819	-52.819	0.000	0.000	0.000	0.000
6	A	4	ILE	0	-0.031	0.003	8.785	1.080	1.080	0.000	0.000	0.000	0.000
7	A	5	PRO	0	-0.001	0.020	12.055	1.052	1.052	0.000	0.000	0.000	0.000
8	A	6	SER	0	0.019	0.006	15.737	0.174	0.174	0.000	0.000	0.000	0.000
9	A	7	ASP	-1	-0.928	-0.965	18.176	-28.669	-28.669	0.000	0.000	0.000	0.000
10	A	8	LEU	0	-0.072	-0.022	16.494	1.108	1.108	0.000	0.000	0.000	0.000
11	A	9	HIS	0	0.027	0.016	19.056	-0.459	-0.459	0.000	0.000	0.000	0.000
12	A	10	TYR	0	-0.005	-0.047	13.908	-1.757	-1.757	0.000	0.000	0.000	0.000
13	A	11	THR	0	-0.004	-0.017	17.037	1.039	1.039	0.000	0.000	0.000	0.000
14	A	12	ALA	0	0.017	0.002	15.364	-2.024	-2.024	0.000	0.000	0.000	0.000
15	A	13	GLU	-1	-0.908	-0.939	14.685	-31.494	-31.494	0.000	0.000	0.000	0.000
16	A	14	HIS	0	0.004	0.023	11.142	-2.297	-2.297	0.000	0.000	0.000	0.000
17	A	15	GLU	0	0.030	0.002	13.720	-0.484	-0.484	0.000	0.000	0.000	0.000
18	A	16	TRP	0	-0.040	-0.021	15.252	0.257	0.257	0.000	0.000	0.000	0.000
19	A	17	ILE	0	-0.001	-0.006	17.615	1.150	1.150	0.000	0.000	0.000	0.000
20	A	18	ARG	1	0.868	0.945	19.568	28.128	28.128	0.000	0.000	0.000	0.000
21	A	19	ARG	1	0.747	0.832	22.993	20.133	20.133	0.000	0.000	0.000	0.000
22	A	20	SER	0	-0.008	-0.018	26.715	-0.225	-0.225	0.000	0.000	0.000	0.000
23	A	21	GLY	0	0.010	0.005	28.699	0.505	0.505	0.000	0.000	0.000	0.000
24	A	22	ASP	-1	-0.948	-0.969	31.581	-17.661	-17.661	0.000	0.000	0.000	0.000
25	A	23	ASP	-1	-0.798	-0.868	33.702	-17.638	-17.638	0.000	0.000	0.000	0.000
26	A	24	THR	0	-0.027	-0.021	29.650	-0.122	-0.122	0.000	0.000	0.000	0.000
27	A	25	VAL	0	-0.015	-0.005	25.370	-0.375	-0.375	0.000	0.000	0.000	0.000
28	A	26	ARG	1	0.805	0.883	23.067	23.294	23.294	0.000	0.000	0.000	0.000
29	A	27	VAL	0	0.012	-0.003	21.014	-0.720	-0.720	0.000	0.000	0.000	0.000
30	A	28	GLY	0	0.064	0.023	18.690	0.597	0.597	0.000	0.000	0.000	0.000
31	A	29	ILE	0	-0.005	0.017	13.845	-0.079	-0.079	0.000	0.000	0.000	0.000
32	A	30	THR	0	0.024	-0.009	10.986	-0.814	-0.814	0.000	0.000	0.000	0.000
33	A	31	ASP	-1	-0.810	-0.901	7.686	-66.180	-66.180	0.000	0.000	0.000	0.000
34	A	32	TYR	0	-0.066	-0.041	5.160	-2.093	-2.093	0.000	0.000	0.000	0.000
35	A	33	ALA	0	0.029	0.021	7.393	-1.651	-1.651	0.000	0.000	0.000	0.000
36	A	34	GLN	0	0.019	0.017	9.627	1.967	1.967	0.000	0.000	0.000	0.000
37	A	35	SER	0	-0.050	-0.014	5.858	0.881	0.881	0.000	0.000	0.000	0.000
38	A	36	ALA	0	-0.009	-0.002	7.617	-0.046	-0.046	0.000	0.000	0.000	0.000
39	A	37	LEU	0	0.006	0.021	8.765	2.556	2.556	0.000	0.000	0.000	0.000
40	A	38	GLY	0	-0.033	-0.005	11.693	2.122	2.122	0.000	0.000	0.000	0.000
41	A	39	ASP	-1	-0.903	-0.956	13.008	-38.411	-38.411	0.000	0.000	0.000	0.000
42	A	40	VAL	0	-0.030	-0.029	15.908	1.424	1.424	0.000	0.000	0.000	0.000
43	A	41	VAL	0	-0.042	-0.038	18.220	0.740	0.740	0.000	0.000	0.000	0.000
44	A	42	PHE	0	-0.019	-0.005	21.561	1.400	1.400	0.000	0.000	0.000	0.000
45	A	43	VAL	0	0.037	0.005	21.046	-1.467	-1.467	0.000	0.000	0.000	0.000
46	A	44	GLN	0	-0.038	0.015	23.468	1.187	1.187	0.000	0.000	0.000	0.000
47	A	45	LEU	0	0.030	0.007	23.450	-0.547	-0.547	0.000	0.000	0.000	0.000
48	A	46	PRO	0	0.008	0.016	27.099	0.779	0.779	0.000	0.000	0.000	0.000
49	A	47	VAL	0	-0.019	-0.010	30.094	-0.028	-0.028	0.000	0.000	0.000	0.000
50	A	48	ILE	0	0.040	0.045	32.523	0.037	0.037	0.000	0.000	0.000	0.000
51	A	49	GLY	0	-0.028	-0.019	34.176	0.558	0.558	0.000	0.000	0.000	0.000
52	A	50	THR	0	-0.092	-0.061	32.628	0.472	0.472	0.000	0.000	0.000	0.000
53	A	51	ALA	0	-0.040	-0.023	33.487	-0.338	-0.338	0.000	0.000	0.000	0.000
54	A	52	VAL	0	0.005	0.011	29.186	-0.035	-0.035	0.000	0.000	0.000	0.000
55	A	53	THR	0	-0.076	-0.070	31.043	0.223	0.223	0.000	0.000	0.000	0.000
56	A	54	ALA	0	0.013	-0.002	27.233	-0.507	-0.507	0.000	0.000	0.000	0.000
57	A	55	GLY	0	-0.002	-0.002	24.700	0.328	0.328	0.000	0.000	0.000	0.000
58	A	56	GLU	-1	-0.878	-0.908	25.789	-19.197	-19.197	0.000	0.000	0.000	0.000
59	A	57	THR	0	-0.029	-0.022	24.419	-0.460	-0.460	0.000	0.000	0.000	0.000
60	A	58	PHE	0	-0.014	-0.002	23.179	0.855	0.855	0.000	0.000	0.000	0.000
61	A	59	GLY	0	0.000	-0.011	25.277	0.545	0.545	0.000	0.000	0.000	0.000
62	A	60	GLU	-1	-0.945	-0.969	21.999	-24.293	-24.293	0.000	0.000	0.000	0.000
63	A	61	VAL	0	-0.017	-0.014	17.364	0.213	0.213	0.000	0.000	0.000	0.000
64	A	62	GLU	-1	-0.882	-0.945	18.919	-26.450	-26.450	0.000	0.000	0.000	0.000
65	A	63	SER	0	-0.015	-0.021	15.444	0.626	0.626	0.000	0.000	0.000	0.000
66	A	64	THR	0	-0.013	-0.019	18.225	0.397	0.397	0.000	0.000	0.000	0.000
67	A	65	LYS	1	0.806	0.903	12.195	44.322	44.322	0.000	0.000	0.000	0.000
68	A	66	SER	0	-0.096	-0.059	15.590	-1.453	-1.453	0.000	0.000	0.000	0.000
69	A	67	VAL	0	0.070	0.059	17.661	-0.468	-0.468	0.000	0.000	0.000	0.000
70	A	68	SER	0	-0.053	-0.026	16.316	-1.358	-1.358	0.000	0.000	0.000	0.000
71	A	69	ASP	-1	-0.827	-0.909	18.461	-24.107	-24.107	0.000	0.000	0.000	0.000
72	A	70	LEU	0	-0.066	-0.023	19.010	-1.632	-1.632	0.000	0.000	0.000	0.000
73	A	71	TYR	0	0.026	-0.004	19.529	0.829	0.829	0.000	0.000	0.000	0.000
74	A	72	ALA	0	0.020	0.034	22.757	-0.735	-0.735	0.000	0.000	0.000	0.000
75	A	73	PRO	0	-0.020	-0.017	21.581	0.304	0.304	0.000	0.000	0.000	0.000
76	A	74	ILE	0	-0.007	-0.003	23.814	0.277	0.277	0.000	0.000	0.000	0.000
77	A	75	SER	0	-0.002	-0.008	27.414	-0.102	-0.102	0.000	0.000	0.000	0.000
78	A	76	GLY	0	-0.001	-0.003	30.906	0.037	0.037	0.000	0.000	0.000	0.000
79	A	77	LYS	1	0.846	0.910	32.713	15.909	15.909	0.000	0.000	0.000	0.000
80	A	78	VAL	0	0.034	0.025	29.166	-0.254	-0.254	0.000	0.000	0.000	0.000
81	A	79	SER	0	-0.004	-0.008	31.101	0.397	0.397	0.000	0.000	0.000	0.000
82	A	80	GLU	-1	-0.883	-0.960	29.810	-18.549	-18.549	0.000	0.000	0.000	0.000
83	A	81	VAL	0	-0.038	-0.022	27.801	-0.567	-0.567	0.000	0.000	0.000	0.000
84	A	82	ASN	0	-0.018	-0.017	23.038	1.408	1.408	0.000	0.000	0.000	0.000
85	A	83	SER	0	0.007	-0.003	26.717	-0.141	-0.141	0.000	0.000	0.000	0.000
86	A	84	ASP	-1	-0.929	-0.957	25.507	-22.145	-22.145	0.000	0.000	0.000	0.000
87	A	85	LEU	0	-0.071	-0.041	21.687	-0.616	-0.616	0.000	0.000	0.000	0.000
88	A	86	ASP	-1	-0.943	-0.958	24.772	-20.638	-20.638	0.000	0.000	0.000	0.000
89	A	87	GLY	0	-0.029	-0.015	27.687	0.012	0.012	0.000	0.000	0.000	0.000
90	A	88	THR	0	-0.072	-0.040	22.432	-0.222	-0.222	0.000	0.000	0.000	0.000
91	A	89	PRO	0	0.045	0.037	21.539	-1.048	-1.048	0.000	0.000	0.000	0.000
92	A	90	GLN	0	-0.033	-0.024	16.727	0.387	0.387	0.000	0.000	0.000	0.000
93	A	91	LEU	0	-0.014	0.002	17.492	-1.896	-1.896	0.000	0.000	0.000	0.000
94	A	92	VAL	0	-0.008	-0.003	15.555	-1.320	-1.320	0.000	0.000	0.000	0.000
95	A	93	ASN	0	-0.007	-0.025	12.906	0.530	0.530	0.000	0.000	0.000	0.000
96	A	94	SER	0	-0.051	-0.025	13.037	-2.208	-2.208	0.000	0.000	0.000	0.000
97	A	95	ASP	-1	-0.867	-0.935	15.101	-33.346	-33.346	0.000	0.000	0.000	0.000
98	A	96	PRO	0	0.028	0.033	12.106	1.785	1.785	0.000	0.000	0.000	0.000
99	A	97	TYR	0	-0.016	-0.037	11.331	1.422	1.422	0.000	0.000	0.000	0.000
100	A	98	GLY	0	0.000	0.009	17.292	1.820	1.820	0.000	0.000	0.000	0.000
101	A	99	ALA	0	-0.016	-0.030	20.176	0.920	0.920	0.000	0.000	0.000	0.000
102	A	100	GLY	0	-0.004	0.003	18.401	0.966	0.966	0.000	0.000	0.000	0.000
103	A	101	TRP	0	-0.075	-0.023	19.232	-0.458	-0.458	0.000	0.000	0.000	0.000
104	A	102	LEU	0	0.021	0.015	18.879	0.391	0.391	0.000	0.000	0.000	0.000
105	A	103	LEU	0	-0.008	-0.010	22.608	1.059	1.059	0.000	0.000	0.000	0.000
106	A	104	ASP	-1	-0.773	-0.845	25.029	-22.888	-22.888	0.000	0.000	0.000	0.000
107	A	105	ILE	0	-0.020	-0.012	26.040	0.491	0.491	0.000	0.000	0.000	0.000
108	A	106	GLN	0	-0.030	-0.015	29.285	-0.184	-0.184	0.000	0.000	0.000	0.000
109	A	107	VAL	0	-0.016	-0.029	31.202	0.179	0.179	0.000	0.000	0.000	0.000
110	A	108	ASP	-1	-0.803	-0.882	33.989	-14.977	-14.977	0.000	0.000	0.000	0.000
111	A	109	SER	0	-0.037	-0.038	37.697	-0.058	-0.058	0.000	0.000	0.000	0.000
112	A	110	SER	0	-0.116	-0.070	38.608	0.262	0.262	0.000	0.000	0.000	0.000
113	A	111	ASP	-1	-0.894	-0.922	38.099	-15.076	-15.076	0.000	0.000	0.000	0.000
114	A	112	VAL	0	-0.048	-0.021	34.030	-0.131	-0.131	0.000	0.000	0.000	0.000
115	A	113	ALA	0	-0.018	-0.008	33.030	0.216	0.216	0.000	0.000	0.000	0.000
116	A	114	ALA	0	0.064	0.022	33.801	-0.292	-0.292	0.000	0.000	0.000	0.000
117	A	115	LEU	0	0.038	0.033	28.508	-0.302	-0.302	0.000	0.000	0.000	0.000
118	A	116	GLU	-1	-0.816	-0.882	30.241	-19.143	-19.143	0.000	0.000	0.000	0.000
119	A	117	SER	0	-0.054	-0.024	30.927	-0.074	-0.074	0.000	0.000	0.000	0.000
120	A	118	ALA	0	0.009	0.023	29.363	-0.395	-0.395	0.000	0.000	0.000	0.000
121	A	119	LEU	0	0.045	0.018	25.015	-0.605	-0.605	0.000	0.000	0.000	0.000
122	A	120	THR	0	-0.107	-0.061	25.429	-0.659	-0.659	0.000	0.000	0.000	0.000
123	A	121	THR	0	-0.090	-0.050	25.849	-0.319	-0.319	0.000	0.000	0.000	0.000
124	A	122	LEU	0	-0.034	0.002	21.442	-0.712	-0.712	0.000	0.000	0.000	0.000
125	A	123	LEU	0	-0.018	-0.002	16.227	0.291	0.291	0.000	0.000	0.000	0.000
126	A	124	ASP	-1	-0.792	-0.896	18.580	-29.922	-29.922	0.000	0.000	0.000	0.000
127	A	125	ALA	0	0.037	-0.006	15.003	-1.392	-1.392	0.000	0.000	0.000	0.000
128	A	126	GLU	-1	-1.013	-0.990	13.928	-34.753	-34.753	0.000	0.000	0.000	0.000
129	A	127	ALA	0	-0.003	-0.017	14.731	-1.793	-1.793	0.000	0.000	0.000	0.000
130	A	128	TYR	0	0.030	0.005	10.891	-2.068	-2.068	0.000	0.000	0.000	0.000
131	A	129	ARG	1	0.855	0.928	6.648	61.187	61.187	0.000	0.000	0.000	0.000
132	A	130	GLY	0	-0.038	-0.014	10.402	-3.284	-3.284	0.000	0.000	0.000	0.000
133	A	131	THR	0	-0.091	-0.058	12.469	0.698	0.698	0.000	0.000	0.000	0.000
134	A	132	LEU	0	-0.036	-0.003	7.021	-1.066	-1.066	0.000	0.000	0.000	0.000
135	A	133	THR	0	-0.053	-0.021	6.444	0.396	0.396	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:-1:HIS)