FMO DATABASE

FMODB ID: 4G16N

Calculation Name: 1NXJ-A-Xray549

Preferred Name:

Target Type:

Ligand Name: l(+)-tartaric acid | glyoxylic acid

Ligand 3-letter code: TLA | GLV

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1NXJ

Chain ID: A

ChEMBL ID:

UniProt ID: P9WGY3

Base Structure: X-ray

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	156
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1371707.582915
FMO2-HF: Nuclear repulsion	1315816.140577
FMO2-HF: Total energy	-55891.442338
FMO2-MP2: Total energy	-56056.99515

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-107.062	-105.029	0.025	-0.883	-1.175	-0.003

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.834 / q_NPA : 0.905

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	4	SER	0	-0.018	-0.005	3.418	-0.885	0.788	0.026	-0.790	-0.909	-0.003
59	A	60	ALA	0	-0.022	-0.011	4.672	-0.512	-0.470	-0.001	-0.008	-0.033	0.000
60	A	61	GLY	0	-0.005	-0.001	3.984	-9.547	-9.229	0.000	-0.085	-0.233	0.000
4	A	5	PHE	0	0.009	-0.006	5.864	1.500	1.500	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.830	0.887	8.867	21.722	21.722	0.000	0.000	0.000	0.000
6	A	7	PRO	0	0.013	0.013	12.354	-0.284	-0.284	0.000	0.000	0.000	0.000
7	A	8	THR	0	-0.044	-0.055	15.770	-0.082	-0.082	0.000	0.000	0.000	0.000
8	A	9	ALA	0	0.045	0.026	17.398	0.136	0.136	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.859	-0.944	16.711	-17.188	-17.188	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.052	-0.028	13.169	-0.452	-0.452	0.000	0.000	0.000	0.000
11	A	12	VAL	0	-0.015	-0.008	17.430	0.225	0.225	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.949	-0.966	21.045	-13.255	-13.255	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.887	-0.922	17.223	-18.038	-18.038	0.000	0.000	0.000	0.000
14	A	15	ILE	0	-0.096	-0.039	16.173	-0.090	-0.090	0.000	0.000	0.000	0.000
15	A	16	GLY	0	0.011	0.016	20.486	0.532	0.532	0.000	0.000	0.000	0.000
16	A	17	PRO	0	-0.045	-0.050	23.955	-0.166	-0.166	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.943	-0.959	24.481	-11.898	-11.898	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.012	0.008	19.334	-0.555	-0.555	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.803	0.880	16.442	18.597	18.597	0.000	0.000	0.000	0.000
20	A	21	SER	0	0.046	0.007	19.306	-1.059	-1.059	0.000	0.000	0.000	0.000
21	A	22	CYS	0	-0.126	-0.048	20.621	0.697	0.697	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.843	-0.922	22.392	-11.704	-11.704	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.083	-0.050	24.180	0.518	0.518	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.026	-0.024	24.141	-0.370	-0.370	0.000	0.000	0.000	0.000
25	A	26	PHE	0	-0.032	-0.018	21.811	0.312	0.312	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.929	0.967	23.880	10.807	10.807	0.000	0.000	0.000	0.000
27	A	28	GLN	0	0.016	-0.014	17.859	-0.594	-0.594	0.000	0.000	0.000	0.000
28	A	29	PHE	0	-0.093	-0.071	20.386	0.940	0.940	0.000	0.000	0.000	0.000
29	A	30	GLY	0	-0.021	0.002	17.599	0.326	0.326	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.001	0.010	17.753	0.407	0.407	0.000	0.000	0.000	0.000
31	A	32	ARG	1	0.747	0.850	8.271	24.684	24.684	0.000	0.000	0.000	0.000
32	A	33	SER	0	0.003	0.002	15.177	-0.327	-0.327	0.000	0.000	0.000	0.000
33	A	34	GLN	0	0.012	0.015	12.908	0.401	0.401	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.026	-0.017	9.908	-0.704	-0.704	0.000	0.000	0.000	0.000
35	A	36	ALA	0	0.032	0.008	7.783	1.601	1.601	0.000	0.000	0.000	0.000
36	A	37	GLY	0	-0.010	0.000	6.053	-4.640	-4.640	0.000	0.000	0.000	0.000
37	A	38	PRO	0	-0.018	0.005	5.215	3.147	3.147	0.000	0.000	0.000	0.000
38	A	39	ILE	0	0.000	0.012	8.180	1.101	1.101	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.015	-0.004	11.851	0.061	0.061	0.000	0.000	0.000	0.000
40	A	41	THR	0	0.008	-0.026	13.993	0.125	0.125	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.027	-0.020	17.723	0.247	0.247	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.820	0.924	20.923	12.180	12.180	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.048	-0.032	24.432	0.060	0.060	0.000	0.000	0.000	0.000
44	A	45	PHE	0	0.070	0.022	27.221	0.106	0.106	0.000	0.000	0.000	0.000
45	A	46	GLN	0	0.023	0.031	29.882	0.271	0.271	0.000	0.000	0.000	0.000
46	A	47	ASP	-1	-0.686	-0.783	29.026	-10.062	-10.062	0.000	0.000	0.000	0.000
47	A	48	ASN	0	-0.006	-0.029	24.996	-0.031	-0.031	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.000	0.011	24.872	-0.407	-0.407	0.000	0.000	0.000	0.000
49	A	50	LEU	0	0.031	0.040	23.190	-0.430	-0.430	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.048	0.042	20.676	-0.470	-0.470	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.949	0.978	19.882	11.640	11.640	0.000	0.000	0.000	0.000
52	A	53	SER	0	-0.062	-0.029	20.658	-0.464	-0.464	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.047	0.020	15.859	-0.394	-0.394	0.000	0.000	0.000	0.000
54	A	55	LEU	0	0.011	0.003	15.345	-0.819	-0.819	0.000	0.000	0.000	0.000
55	A	56	SER	0	-0.057	-0.033	16.804	-0.100	-0.100	0.000	0.000	0.000	0.000
56	A	57	GLN	0	-0.017	0.002	15.337	0.283	0.283	0.000	0.000	0.000	0.000
57	A	58	PRO	0	-0.007	-0.010	12.508	-0.523	-0.523	0.000	0.000	0.000	0.000
58	A	59	SER	0	0.005	0.019	9.385	-1.416	-1.416	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.020	0.014	5.752	-0.929	-0.929	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.013	-0.013	8.074	1.670	1.670	0.000	0.000	0.000	0.000
63	A	64	LEU	0	-0.025	-0.009	11.220	0.542	0.542	0.000	0.000	0.000	0.000
64	A	65	VAL	0	0.007	0.007	14.667	0.618	0.618	0.000	0.000	0.000	0.000
65	A	66	ILE	0	0.000	-0.014	17.515	0.434	0.434	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.737	-0.872	20.903	-11.571	-11.571	0.000	0.000	0.000	0.000
67	A	68	GLY	0	0.018	0.000	23.992	0.252	0.252	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.041	-0.028	26.887	0.474	0.474	0.000	0.000	0.000	0.000
69	A	70	GLY	0	0.044	0.033	27.952	0.336	0.336	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.061	-0.047	29.275	0.286	0.286	0.000	0.000	0.000	0.000
71	A	72	LEU	0	0.040	0.009	29.934	-0.288	-0.288	0.000	0.000	0.000	0.000
72	A	73	HIS	0	-0.002	0.010	32.245	0.176	0.176	0.000	0.000	0.000	0.000
73	A	74	THR	0	-0.028	-0.036	30.764	0.296	0.296	0.000	0.000	0.000	0.000
74	A	75	ALA	0	0.002	0.028	27.692	-0.230	-0.230	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.008	0.024	24.686	0.131	0.131	0.000	0.000	0.000	0.000
76	A	77	VAL	0	0.067	0.030	20.420	-0.166	-0.166	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.038	-0.001	23.601	0.527	0.527	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.840	-0.919	22.678	-12.113	-12.113	0.000	0.000	0.000	0.000
79	A	80	VAL	0	-0.033	-0.020	21.985	-0.558	-0.558	0.000	0.000	0.000	0.000
80	A	81	ILE	0	-0.087	-0.043	20.239	-0.213	-0.213	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.056	0.029	18.226	-0.707	-0.707	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.765	-0.847	17.110	-16.722	-16.722	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.066	-0.018	17.549	-0.414	-0.414	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.041	0.030	14.888	-0.698	-0.698	0.000	0.000	0.000	0.000
85	A	86	ARG	1	0.833	0.887	13.065	16.424	16.424	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.129	-0.070	13.029	-0.939	-0.939	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.025	-0.032	13.777	-0.745	-0.745	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.040	0.025	9.714	-1.208	-1.208	0.000	0.000	0.000	0.000
89	A	90	TRP	0	-0.042	-0.024	8.462	-3.701	-3.701	0.000	0.000	0.000	0.000
90	A	91	THR	0	0.003	-0.014	7.028	0.964	0.964	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.001	0.004	9.491	1.134	1.134	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.049	-0.016	12.436	0.070	0.070	0.000	0.000	0.000	0.000
93	A	94	ILE	0	0.047	0.028	15.239	0.427	0.427	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.019	-0.015	18.323	0.262	0.262	0.000	0.000	0.000	0.000
95	A	96	HIS	0	0.020	0.009	21.872	0.622	0.622	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.024	-0.002	24.741	0.390	0.390	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.017	0.010	26.336	-0.218	-0.218	0.000	0.000	0.000	0.000
98	A	99	VAL	0	0.011	0.016	22.851	-0.237	-0.237	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.779	0.873	26.218	10.651	10.651	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.774	-0.900	26.077	-11.033	-11.033	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.041	0.021	25.407	-0.240	-0.240	0.000	0.000	0.000	0.000
102	A	103	ALA	0	-0.032	-0.013	25.647	-0.206	-0.206	0.000	0.000	0.000	0.000
103	A	104	ALA	0	0.030	0.019	24.999	0.011	0.011	0.000	0.000	0.000	0.000
104	A	105	LEU	0	0.005	0.004	21.269	-0.394	-0.394	0.000	0.000	0.000	0.000
105	A	106	ARG	1	0.933	0.964	20.249	10.416	10.416	0.000	0.000	0.000	0.000
106	A	107	GLY	0	-0.016	-0.003	21.022	-0.093	-0.093	0.000	0.000	0.000	0.000
107	A	108	ILE	0	-0.043	-0.014	16.668	-0.117	-0.117	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.831	-0.879	12.685	-21.269	-21.269	0.000	0.000	0.000	0.000
109	A	110	ILE	0	-0.016	-0.022	12.264	-1.419	-1.419	0.000	0.000	0.000	0.000
110	A	111	GLY	0	0.037	0.036	12.712	1.109	1.109	0.000	0.000	0.000	0.000
111	A	112	ILE	0	-0.064	-0.046	14.377	0.021	0.021	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.877	0.939	17.311	16.953	16.953	0.000	0.000	0.000	0.000
113	A	114	ALA	0	-0.033	-0.009	19.905	-0.098	-0.098	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.057	0.038	23.341	0.178	0.178	0.000	0.000	0.000	0.000
115	A	116	GLY	0	-0.021	-0.020	26.910	0.397	0.397	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.041	-0.013	27.620	-0.312	-0.312	0.000	0.000	0.000	0.000
117	A	118	ASN	0	-0.002	-0.014	29.887	0.459	0.459	0.000	0.000	0.000	0.000
118	A	119	PRO	0	0.041	0.026	31.237	-0.252	-0.252	0.000	0.000	0.000	0.000
119	A	120	ARG	1	0.865	0.937	33.072	8.313	8.313	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.945	0.966	31.189	8.811	8.811	0.000	0.000	0.000	0.000
121	A	122	SER	0	0.062	0.023	29.056	0.311	0.311	0.000	0.000	0.000	0.000
122	A	123	THR	0	-0.056	-0.046	31.190	0.077	0.077	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.792	0.856	29.242	10.040	10.040	0.000	0.000	0.000	0.000
124	A	125	THR	0	0.002	-0.029	31.076	0.059	0.059	0.000	0.000	0.000	0.000
125	A	126	GLY	0	-0.022	-0.010	27.858	0.016	0.016	0.000	0.000	0.000	0.000
126	A	127	ALA	0	-0.026	-0.004	28.166	-0.213	-0.213	0.000	0.000	0.000	0.000
127	A	128	GLY	0	-0.002	-0.003	27.125	-0.150	-0.150	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.914	-0.965	25.364	-11.007	-11.007	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.841	0.904	17.278	15.737	15.737	0.000	0.000	0.000	0.000
130	A	131	ASP	-1	-0.866	-0.935	17.656	-16.144	-16.144	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.018	0.010	19.565	0.156	0.156	0.000	0.000	0.000	0.000
132	A	133	GLU	-1	-0.855	-0.912	20.620	-14.596	-14.596	0.000	0.000	0.000	0.000
133	A	134	ILE	0	-0.055	-0.032	19.740	0.818	0.818	0.000	0.000	0.000	0.000
134	A	135	THR	0	0.014	0.024	21.622	-0.622	-0.622	0.000	0.000	0.000	0.000
135	A	136	LEU	0	-0.031	-0.020	21.852	0.556	0.556	0.000	0.000	0.000	0.000
136	A	137	GLY	0	0.013	0.009	23.644	-0.398	-0.398	0.000	0.000	0.000	0.000
137	A	138	GLY	0	0.065	0.037	25.093	-0.202	-0.202	0.000	0.000	0.000	0.000
138	A	139	VAL	0	0.013	0.023	19.196	-0.034	-0.034	0.000	0.000	0.000	0.000
139	A	140	THR	0	-0.019	-0.018	21.190	0.205	0.205	0.000	0.000	0.000	0.000
140	A	141	PHE	0	-0.015	-0.014	16.172	-0.848	-0.848	0.000	0.000	0.000	0.000
141	A	142	VAL	0	0.066	0.021	16.666	0.903	0.903	0.000	0.000	0.000	0.000
142	A	143	PRO	0	-0.055	-0.037	14.494	-1.321	-1.321	0.000	0.000	0.000	0.000
143	A	144	GLY	0	-0.031	-0.008	11.125	0.530	0.530	0.000	0.000	0.000	0.000
144	A	145	ASP	-1	-0.796	-0.867	10.676	-22.097	-22.097	0.000	0.000	0.000	0.000
145	A	146	ILE	0	-0.064	-0.044	7.230	-2.502	-2.502	0.000	0.000	0.000	0.000
146	A	147	ALA	0	0.019	0.021	10.357	2.197	2.197	0.000	0.000	0.000	0.000
147	A	148	TYR	0	0.004	-0.007	9.425	-4.231	-4.231	0.000	0.000	0.000	0.000
148	A	149	SER	0	0.002	0.002	12.459	2.413	2.413	0.000	0.000	0.000	0.000
149	A	150	ASP	-1	-0.730	-0.847	14.023	-18.082	-18.082	0.000	0.000	0.000	0.000
150	A	151	ASP	-1	-0.830	-0.919	16.710	-14.249	-14.249	0.000	0.000	0.000	0.000
151	A	152	ASP	-1	-0.921	-0.921	19.928	-12.993	-12.993	0.000	0.000	0.000	0.000
152	A	153	GLY	0	0.003	-0.008	19.611	0.649	0.649	0.000	0.000	0.000	0.000
153	A	154	ILE	0	-0.100	-0.072	15.959	-0.821	-0.821	0.000	0.000	0.000	0.000
154	A	155	ILE	0	0.021	0.036	15.726	0.809	0.809	0.000	0.000	0.000	0.000
155	A	156	VAL	0	-0.048	-0.028	14.381	-1.456	-1.456	0.000	0.000	0.000	0.000
156	A	157	VAL	-1	-0.830	-0.904	12.433	-21.996	-21.996	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)