FMO DATABASE

FMODB ID: 1328Z

Calculation Name: 2K3U-A-Other549

Preferred Name:

Target Type:

Ligand Name: o-sulfo-l-tyrosine | amino group | acetyl group

Ligand 3-letter code: TYS | NH2 | ACE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2K3U

Chain ID: A

ChEMBL ID:

UniProt ID: A6QIG7

Base Structure: SolutionNMR

Registration Date: 2025-10-12

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	91
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-651548.301267
FMO2-HF: Nuclear repulsion	615206.730228
FMO2-HF: Total energy	-36341.571039
FMO2-MP2: Total energy	-36448.549365

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:31:ASN)

Summations of interaction energy for fragment #1(A:31:ASN)

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.
67.105	70.087	-0.034	-1.5	-1.448	-0.007

Interaction energy analysis for fragmet #1(A:31:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.873 / 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	33	GLY	0	0.050	0.049	3.627	7.709	10.691	-0.034	-1.500	-1.448	-0.007
4	A	34	LEU	0	-0.001	0.004	5.479	6.305	6.305	0.000	0.000	0.000	0.000
5	A	35	PRO	0	-0.052	-0.022	7.283	-0.243	-0.243	0.000	0.000	0.000	0.000
6	A	36	THR	0	0.084	0.016	7.656	-1.172	-1.172	0.000	0.000	0.000	0.000
7	A	37	THR	0	0.011	0.014	9.624	0.473	0.473	0.000	0.000	0.000	0.000
8	A	38	LEU	0	0.023	0.023	13.444	0.424	0.424	0.000	0.000	0.000	0.000
9	A	39	GLY	0	0.034	0.014	16.305	0.545	0.545	0.000	0.000	0.000	0.000
10	A	40	LYS	1	0.946	0.974	12.519	21.270	21.270	0.000	0.000	0.000	0.000
11	A	41	LEU	0	-0.036	-0.007	14.610	0.117	0.117	0.000	0.000	0.000	0.000
12	A	42	ASP	-1	-0.746	-0.863	17.643	-12.052	-12.052	0.000	0.000	0.000	0.000
13	A	43	GLU	-1	-0.895	-0.945	21.019	-12.599	-12.599	0.000	0.000	0.000	0.000
14	A	44	ARG	1	0.911	0.956	17.328	16.983	16.983	0.000	0.000	0.000	0.000
15	A	45	LEU	0	-0.003	-0.001	20.409	0.593	0.593	0.000	0.000	0.000	0.000
16	A	46	ARG	1	0.826	0.876	23.103	12.204	12.204	0.000	0.000	0.000	0.000
17	A	47	ASN	0	-0.036	-0.034	24.493	0.996	0.996	0.000	0.000	0.000	0.000
18	A	48	TYR	0	0.037	-0.003	20.576	0.053	0.053	0.000	0.000	0.000	0.000
19	A	49	LEU	0	-0.022	0.003	26.098	0.324	0.324	0.000	0.000	0.000	0.000
20	A	50	LYS	1	0.877	0.951	28.889	10.831	10.831	0.000	0.000	0.000	0.000
21	A	51	LYS	1	0.927	0.969	26.105	11.674	11.674	0.000	0.000	0.000	0.000
22	A	52	GLY	0	0.029	0.031	29.459	-0.045	-0.045	0.000	0.000	0.000	0.000
23	A	53	THR	0	-0.094	-0.037	30.424	0.277	0.277	0.000	0.000	0.000	0.000
24	A	54	LYS	1	1.004	0.989	33.222	8.560	8.560	0.000	0.000	0.000	0.000
25	A	55	ASN	0	0.054	0.017	36.005	0.089	0.089	0.000	0.000	0.000	0.000
26	A	56	SER	0	0.058	0.038	32.253	-0.119	-0.119	0.000	0.000	0.000	0.000
27	A	57	ALA	0	0.041	0.022	34.512	-0.106	-0.106	0.000	0.000	0.000	0.000
28	A	58	GLN	0	-0.010	-0.004	36.050	0.235	0.235	0.000	0.000	0.000	0.000
29	A	59	PHE	0	-0.052	-0.028	31.863	0.021	0.021	0.000	0.000	0.000	0.000
30	A	60	GLU	-1	-0.833	-0.907	33.006	-8.618	-8.618	0.000	0.000	0.000	0.000
31	A	61	LYS	1	0.922	0.956	28.774	9.639	9.639	0.000	0.000	0.000	0.000
32	A	62	MET	0	-0.039	0.004	22.988	0.158	0.158	0.000	0.000	0.000	0.000
33	A	63	VAL	0	-0.012	0.003	23.387	-0.079	-0.079	0.000	0.000	0.000	0.000
34	A	64	ILE	0	-0.004	-0.014	18.273	0.077	0.077	0.000	0.000	0.000	0.000
35	A	65	LEU	0	-0.024	-0.009	18.721	0.000	0.000	0.000	0.000	0.000	0.000
36	A	66	THR	0	-0.036	-0.024	13.288	0.171	0.171	0.000	0.000	0.000	0.000
37	A	67	GLU	-1	-0.771	-0.883	9.978	-28.149	-28.149	0.000	0.000	0.000	0.000
38	A	68	ASN	0	-0.013	-0.030	8.854	0.410	0.410	0.000	0.000	0.000	0.000
39	A	69	LYS	1	0.934	0.969	12.883	15.955	15.955	0.000	0.000	0.000	0.000
40	A	70	GLY	0	0.027	0.044	15.131	0.791	0.791	0.000	0.000	0.000	0.000
41	A	71	TYR	0	-0.007	-0.017	16.018	0.662	0.662	0.000	0.000	0.000	0.000
42	A	72	TYR	0	0.017	0.003	14.158	-0.026	-0.026	0.000	0.000	0.000	0.000
43	A	73	THR	0	-0.020	-0.016	20.234	0.432	0.432	0.000	0.000	0.000	0.000
44	A	74	VAL	0	-0.012	-0.008	22.732	-0.024	-0.024	0.000	0.000	0.000	0.000
45	A	75	TYR	0	0.066	0.029	25.565	0.205	0.205	0.000	0.000	0.000	0.000
46	A	76	LEU	0	-0.059	-0.043	27.131	-0.156	-0.156	0.000	0.000	0.000	0.000
47	A	77	ASN	0	0.007	-0.010	29.677	0.011	0.011	0.000	0.000	0.000	0.000
48	A	78	THR	0	-0.008	0.012	30.213	0.277	0.277	0.000	0.000	0.000	0.000
49	A	79	PRO	0	0.006	0.000	28.732	-0.379	-0.379	0.000	0.000	0.000	0.000
50	A	80	LEU	0	-0.057	-0.016	21.785	0.104	0.104	0.000	0.000	0.000	0.000
51	A	81	ALA	0	0.066	0.019	25.518	-0.083	-0.083	0.000	0.000	0.000	0.000
52	A	82	GLU	-1	-0.880	-0.947	22.806	-12.731	-12.731	0.000	0.000	0.000	0.000
53	A	83	ASP	-1	-0.843	-0.918	20.846	-13.756	-13.756	0.000	0.000	0.000	0.000
54	A	84	ARG	1	0.900	0.939	19.875	11.379	11.379	0.000	0.000	0.000	0.000
55	A	85	LYS	1	0.897	0.946	19.696	12.102	12.102	0.000	0.000	0.000	0.000
56	A	86	ASN	0	0.036	0.005	16.623	-1.106	-1.106	0.000	0.000	0.000	0.000
57	A	87	VAL	0	0.003	0.025	15.429	-0.983	-0.983	0.000	0.000	0.000	0.000
58	A	88	GLU	-1	-0.895	-0.947	10.209	-26.310	-26.310	0.000	0.000	0.000	0.000
59	A	89	LEU	0	-0.112	-0.042	10.966	1.500	1.500	0.000	0.000	0.000	0.000
60	A	90	LEU	0	0.070	0.034	9.607	-2.169	-2.169	0.000	0.000	0.000	0.000
61	A	91	GLY	0	0.021	0.018	9.476	-2.039	-2.039	0.000	0.000	0.000	0.000
62	A	92	LYS	1	0.818	0.906	9.598	29.839	29.839	0.000	0.000	0.000	0.000
63	A	93	MET	0	0.021	0.013	11.753	1.248	1.248	0.000	0.000	0.000	0.000
64	A	94	TYR	0	0.015	0.025	15.385	1.180	1.180	0.000	0.000	0.000	0.000
65	A	95	LYS	1	0.867	0.943	17.426	14.693	14.693	0.000	0.000	0.000	0.000
66	A	96	THR	0	0.012	0.012	20.353	-0.513	-0.513	0.000	0.000	0.000	0.000
67	A	97	TYR	0	0.002	0.002	22.798	0.513	0.513	0.000	0.000	0.000	0.000
68	A	98	PHE	0	0.007	-0.010	24.835	-0.120	-0.120	0.000	0.000	0.000	0.000
69	A	99	PHE	0	-0.015	-0.011	27.960	0.248	0.248	0.000	0.000	0.000	0.000
70	A	100	LYS	1	0.859	0.903	32.357	8.360	8.360	0.000	0.000	0.000	0.000
71	A	101	LYS	1	0.882	0.932	35.697	8.297	8.297	0.000	0.000	0.000	0.000
72	A	102	GLY	0	0.064	0.049	37.066	0.248	0.248	0.000	0.000	0.000	0.000
73	A	103	GLU	-1	-0.817	-0.887	35.088	-8.710	-8.710	0.000	0.000	0.000	0.000
74	A	104	SER	0	-0.038	-0.043	33.831	-0.203	-0.203	0.000	0.000	0.000	0.000
75	A	105	LYS	1	0.946	0.968	32.959	8.435	8.435	0.000	0.000	0.000	0.000
76	A	106	SER	0	-0.017	0.018	30.018	0.077	0.077	0.000	0.000	0.000	0.000
77	A	107	SER	0	0.000	-0.006	32.087	0.158	0.158	0.000	0.000	0.000	0.000
78	A	108	TYR	0	-0.018	-0.007	28.463	0.190	0.190	0.000	0.000	0.000	0.000
79	A	109	VAL	0	0.028	0.007	26.847	-0.181	-0.181	0.000	0.000	0.000	0.000
80	A	110	ILE	0	-0.024	-0.003	22.663	0.162	0.162	0.000	0.000	0.000	0.000
81	A	111	ASN	0	0.006	-0.004	22.028	-0.397	-0.397	0.000	0.000	0.000	0.000
82	A	112	GLY	0	0.012	0.010	18.528	0.190	0.190	0.000	0.000	0.000	0.000
83	A	113	PRO	0	-0.034	-0.019	14.239	0.117	0.117	0.000	0.000	0.000	0.000
84	A	114	GLY	0	0.082	0.023	13.616	-0.449	-0.449	0.000	0.000	0.000	0.000
85	A	115	LYS	1	0.927	0.981	14.615	15.952	15.952	0.000	0.000	0.000	0.000
86	A	116	THR	0	0.024	0.001	16.284	1.337	1.337	0.000	0.000	0.000	0.000
87	A	117	ASN	0	0.037	0.009	16.260	-1.199	-1.199	0.000	0.000	0.000	0.000
88	A	118	GLU	-1	-0.977	-0.986	15.761	-15.932	-15.932	0.000	0.000	0.000	0.000
89	A	119	TYR	0	-0.014	-0.016	11.325	-0.029	-0.029	0.000	0.000	0.000	0.000
90	A	120	ALA	0	-0.028	-0.006	11.304	0.853	0.853	0.000	0.000	0.000	0.000
91	A	121	TYR	-1	-0.945	-0.957	9.362	-27.871	-27.871	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:31:ASN)