FMO DATABASE

FMODB ID: MZ53Z

Calculation Name: 1R5S-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1R5S

Chain ID: A

ChEMBL ID:

UniProt ID: P08050

Base Structure: SolutionNMR

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230712

Total energy (hartree)

FMO2-HF: Electronic energy	-704099.841417
FMO2-HF: Nuclear repulsion	653371.132372
FMO2-HF: Total energy	-50728.709044
FMO2-MP2: Total energy	-50873.716279

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:GLY)

Summations of interaction energy for fragment #1(A:1: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.
42.468	43.385	-0.004	-0.336	-0.577	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.870 / 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	3	LEU	0	0.019	0.016	3.858	5.536	6.453	-0.004	-0.336	-0.577	-0.001
4	A	4	GLY	0	0.077	0.023	5.829	3.539	3.539	0.000	0.000	0.000	0.000
5	A	5	SER	0	0.029	0.034	9.195	0.858	0.858	0.000	0.000	0.000	0.000
6	A	6	PRO	0	0.036	0.014	8.315	0.799	0.799	0.000	0.000	0.000	0.000
7	A	7	SER	0	0.015	0.002	9.975	1.416	1.416	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.845	0.909	11.308	24.386	24.386	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.880	-0.952	13.852	-18.465	-18.465	0.000	0.000	0.000	0.000
10	A	10	CYS	0	-0.071	-0.018	16.734	1.005	1.005	0.000	0.000	0.000	0.000
11	A	11	GLY	0	0.071	0.031	18.280	0.835	0.835	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.044	-0.008	16.652	-0.078	-0.078	0.000	0.000	0.000	0.000
13	A	13	PRO	0	0.012	0.011	15.458	0.771	0.771	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.902	0.934	18.189	14.302	14.302	0.000	0.000	0.000	0.000
15	A	15	TYR	0	0.023	0.022	21.124	0.483	0.483	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.032	0.009	19.293	-0.199	-0.199	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.020	-0.013	18.127	-0.548	-0.548	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.037	0.011	19.631	-0.297	-0.297	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.044	-0.012	20.544	0.455	0.455	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.056	0.015	23.315	0.572	0.572	0.000	0.000	0.000	0.000
21	A	21	CYS	0	-0.064	-0.017	21.630	-0.114	-0.114	0.000	0.000	0.000	0.000
22	A	22	SER	0	0.025	0.010	24.670	0.221	0.221	0.000	0.000	0.000	0.000
23	A	23	SER	0	0.003	0.006	25.880	0.226	0.226	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.031	0.013	28.656	0.133	0.133	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.046	-0.015	28.835	0.188	0.188	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.031	0.021	30.552	-0.237	-0.237	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.024	-0.022	33.138	0.040	0.040	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.001	0.008	30.851	-0.242	-0.242	0.000	0.000	0.000	0.000
29	A	29	SER	0	0.011	-0.007	32.160	-0.122	-0.122	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.010	0.003	34.808	0.154	0.154	0.000	0.000	0.000	0.000
31	A	31	MET	0	0.004	0.008	37.731	0.109	0.109	0.000	0.000	0.000	0.000
32	A	32	SER	0	0.001	-0.004	39.534	0.067	0.067	0.000	0.000	0.000	0.000
33	A	33	PRO	0	0.007	0.012	41.951	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.043	0.004	43.437	0.134	0.134	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.008	0.011	46.690	0.081	0.081	0.000	0.000	0.000	0.000
36	A	36	TYR	0	-0.018	-0.008	49.250	0.058	0.058	0.000	0.000	0.000	0.000
37	A	37	LYS	1	0.903	0.946	49.899	6.291	6.291	0.000	0.000	0.000	0.000
38	A	38	LEU	0	0.015	0.014	52.901	0.088	0.088	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.002	-0.008	53.409	-0.095	-0.095	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.032	-0.024	56.249	0.003	0.003	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.046	0.030	59.150	0.096	0.096	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.830	-0.907	55.527	-5.720	-5.720	0.000	0.000	0.000	0.000
43	A	43	ARG	1	0.901	0.950	54.939	5.464	5.464	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.045	-0.010	51.175	-0.161	-0.161	0.000	0.000	0.000	0.000
45	A	45	ASN	0	0.015	-0.010	48.490	0.019	0.019	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.013	-0.006	51.294	0.005	0.005	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.009	0.011	51.831	0.138	0.138	0.000	0.000	0.000	0.000
48	A	48	CYS	0	0.000	0.001	51.554	0.120	0.120	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.953	0.980	48.157	6.049	6.049	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.009	-0.014	46.184	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	51	TYR	0	-0.010	0.005	43.911	-0.125	-0.125	0.000	0.000	0.000	0.000
52	A	52	ASN	0	0.073	0.039	44.226	-0.155	-0.155	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.930	0.961	40.506	7.503	7.503	0.000	0.000	0.000	0.000
54	A	54	GLN	0	0.009	0.007	44.131	-0.051	-0.051	0.000	0.000	0.000	0.000
55	A	55	ALA	0	-0.006	0.005	46.556	0.118	0.118	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.020	0.001	49.456	0.010	0.010	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.889	-0.947	51.637	-5.661	-5.661	0.000	0.000	0.000	0.000
58	A	58	GLN	0	-0.021	-0.029	52.319	0.015	0.015	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.062	-0.035	56.097	0.080	0.080	0.000	0.000	0.000	0.000
60	A	60	TRP	0	0.061	0.027	57.770	0.116	0.116	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.002	0.005	60.648	0.077	0.077	0.000	0.000	0.000	0.000
62	A	62	ASN	0	0.052	0.031	58.500	0.120	0.120	0.000	0.000	0.000	0.000
63	A	63	TYR	0	0.009	-0.009	62.184	0.065	0.065	0.000	0.000	0.000	0.000
64	A	64	SER	0	-0.062	-0.021	61.430	0.000	0.000	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.009	0.012	63.362	0.022	0.022	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.874	-0.946	64.921	-4.620	-4.620	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.030	0.020	59.518	0.046	0.046	0.000	0.000	0.000	0.000
68	A	68	ASN	0	0.016	0.001	64.278	-0.055	-0.055	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.910	0.963	67.603	4.602	4.602	0.000	0.000	0.000	0.000
70	A	70	MET	0	0.008	0.006	63.223	0.021	0.021	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.017	0.015	65.369	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.048	-0.039	66.189	0.012	0.012	0.000	0.000	0.000	0.000
73	A	73	ALA	0	0.020	0.012	67.339	0.031	0.031	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.051	0.038	65.277	0.019	0.019	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.045	-0.035	66.215	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.097	-0.058	68.586	0.063	0.063	0.000	0.000	0.000	0.000
77	A	77	ILE	0	-0.055	-0.014	66.814	0.038	0.038	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.002	0.001	68.706	0.057	0.057	0.000	0.000	0.000	0.000
79	A	79	ASN	0	-0.012	-0.016	65.435	-0.058	-0.058	0.000	0.000	0.000	0.000
80	A	80	SER	0	-0.024	-0.011	63.789	-0.028	-0.028	0.000	0.000	0.000	0.000
81	A	81	HIS	0	-0.011	-0.022	61.389	-0.103	-0.103	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.065	0.054	61.212	-0.094	-0.094	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.060	-0.035	58.258	0.034	0.034	0.000	0.000	0.000	0.000
84	A	84	PRO	0	-0.045	-0.020	62.144	0.004	0.004	0.000	0.000	0.000	0.000
85	A	85	PHE	0	-0.039	-0.031	65.571	0.069	0.069	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.784	-0.882	63.959	-5.001	-5.001	0.000	0.000	0.000	0.000
87	A	87	PHE	0	0.017	0.003	66.787	0.050	0.050	0.000	0.000	0.000	0.000
88	A	88	PRO	0	-0.067	-0.041	69.866	0.042	0.042	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.938	-0.964	67.480	-4.701	-4.701	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.858	-0.902	67.894	-4.832	-4.832	0.000	0.000	0.000	0.000
91	A	91	ASN	0	0.013	-0.003	69.336	0.022	0.022	0.000	0.000	0.000	0.000
92	A	92	GLN	0	-0.082	-0.048	71.494	0.025	0.025	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.022	-0.031	66.664	0.013	0.013	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.123	0.074	68.421	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	95	LYS	1	0.925	0.957	69.339	4.228	4.228	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.874	0.931	70.464	4.478	4.478	0.000	0.000	0.000	0.000
97	A	97	VAL	0	0.034	0.036	65.887	0.008	0.008	0.000	0.000	0.000	0.000
98	A	98	ALA	0	0.031	0.010	69.210	0.003	0.003	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.020	-0.004	71.292	0.023	0.023	0.000	0.000	0.000	0.000
100	A	100	GLY	0	-0.029	-0.033	71.455	0.036	0.036	0.000	0.000	0.000	0.000
101	A	101	HIS	0	-0.040	-0.015	63.629	-0.015	-0.015	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.972	-0.969	68.498	-4.355	-4.355	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.073	-0.030	69.714	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	104	GLN	0	0.002	-0.003	69.917	-0.043	-0.043	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.038	0.024	69.713	0.059	0.059	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.029	-0.007	72.537	0.061	0.061	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.007	-0.015	74.993	-0.031	-0.031	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.009	0.002	77.751	0.050	0.050	0.000	0.000	0.000	0.000
109	A	109	VAL	0	0.041	0.016	79.966	0.062	0.062	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.876	-0.938	77.383	-4.149	-4.149	0.000	0.000	0.000	0.000
111	A	111	GLN	0	-0.035	-0.023	79.951	0.013	0.013	0.000	0.000	0.000	0.000
112	A	112	ARG	1	0.937	0.976	77.365	4.114	4.114	0.000	0.000	0.000	0.000
113	A	113	PRO	0	-0.024	-0.019	84.318	0.035	0.035	0.000	0.000	0.000	0.000
114	A	114	SER	0	0.068	0.047	87.503	0.034	0.034	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.026	-0.016	89.006	0.029	0.029	0.000	0.000	0.000	0.000
116	A	116	ARG	1	0.917	0.953	89.850	3.523	3.523	0.000	0.000	0.000	0.000
117	A	117	ALA	0	0.059	0.021	88.277	0.005	0.005	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.030	-0.010	90.376	0.007	0.007	0.000	0.000	0.000	0.000
119	A	119	SER	0	0.046	0.019	90.882	0.016	0.016	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.891	0.944	92.868	3.264	3.264	0.000	0.000	0.000	0.000
121	A	121	ALA	0	0.007	0.008	96.085	0.036	0.036	0.000	0.000	0.000	0.000
122	A	122	SER	0	-0.001	-0.008	97.772	0.018	0.018	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.009	0.034	100.305	0.031	0.031	0.000	0.000	0.000	0.000
124	A	124	ARG	1	0.891	0.919	96.947	3.268	3.268	0.000	0.000	0.000	0.000
125	A	125	PRO	0	0.087	0.078	104.012	-0.005	-0.005	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.874	0.913	105.836	3.005	3.005	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.027	0.008	109.294	-0.013	-0.013	0.000	0.000	0.000	0.000
128	A	128	ASP	-1	-0.875	-0.935	111.199	-2.903	-2.903	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.924	-0.980	109.861	-2.994	-2.994	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.113	-0.070	109.796	0.008	0.008	0.000	0.000	0.000	0.000
131	A	131	GLU	-1	-0.965	-0.972	113.651	-2.802	-2.802	0.000	0.000	0.000	0.000
132	A	132	ILE	-1	-0.942	-0.959	116.675	-2.756	-2.756	0.000	0.000	0.000	0.000

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