FMO DATABASE

FMODB ID: VZ611

Calculation Name: 1RTU-A-Xray547

Preferred Name:

Target Type:

Ligand Name: beta-l-aspartic acid | sulfate ion

Ligand 3-letter code: IAS | SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1RTU

Chain ID: A

ChEMBL ID:

UniProt ID: P00654

Base Structure: X-ray

Registration Date: 2025-10-06

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	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-870719.945347
FMO2-HF: Nuclear repulsion	825815.876877
FMO2-HF: Total energy	-44904.068471
FMO2-MP2: Total energy	-45031.1338

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:CYS)

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

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.
-346.603	-342.915	31.088	-17.407	-17.369	-0.175

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.625 / q_NPA : 0.804

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	ILE	0	-0.025	-0.001	3.542	-0.466	1.682	0.763	-1.113	-1.798	-0.008
4	A	4	PRO	0	0.004	0.016	4.649	3.958	4.213	0.001	-0.027	-0.229	0.000
45	A	45	ASN	0	-0.017	-0.015	5.363	-0.306	-0.281	-0.002	0.002	-0.025	0.000
51	A	51	ILE	0	-0.041	-0.007	4.666	-1.978	-1.935	-0.002	-0.008	-0.033	0.000
52	A	52	THR	0	-0.038	-0.019	3.086	-2.736	0.539	0.138	-1.722	-1.692	-0.004
55	A	56	GLY	0	0.011	0.009	3.659	9.565	11.541	-0.009	-0.962	-1.005	0.004
93	A	94	GLU	-1	-0.894	-0.928	1.732	-117.006	-120.671	16.406	-7.733	-5.008	-0.093
94	A	95	PHE	0	0.041	0.002	3.043	0.879	3.551	1.217	-1.069	-2.819	-0.007
95	A	97	ALA	0	0.120	0.052	1.815	-16.322	-19.581	12.580	-4.730	-4.591	-0.067
96	A	98	THR	0	-0.001	-0.004	4.560	1.954	2.092	-0.002	-0.044	-0.092	0.000
110	A	112	GLN	0	0.007	0.008	4.632	0.684	0.764	-0.002	-0.001	-0.077	0.000
5	A	5	GLN	0	-0.033	-0.035	7.141	1.299	1.299	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.056	-0.036	10.557	2.086	2.086	0.000	0.000	0.000	0.000
7	A	7	THR	0	0.019	0.010	9.752	-1.831	-1.831	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.040	-0.039	11.531	1.744	1.744	0.000	0.000	0.000	0.000
9	A	9	CYS	0	-0.079	-0.016	9.464	1.453	1.453	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.045	0.016	15.145	0.941	0.941	0.000	0.000	0.000	0.000
11	A	11	GLY	0	-0.061	-0.034	18.040	0.967	0.967	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.069	-0.038	18.069	0.999	0.999	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.021	-0.004	15.760	-1.051	-1.051	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.039	-0.019	13.734	0.912	0.912	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.031	-0.050	13.512	-1.035	-1.035	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.033	-0.006	10.572	0.462	0.462	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.901	-0.950	11.469	-21.207	-21.207	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.804	-0.877	14.368	-18.434	-18.434	0.000	0.000	0.000	0.000
19	A	19	ILE	0	0.009	-0.003	8.241	-0.259	-0.259	0.000	0.000	0.000	0.000
20	A	20	ASN	0	0.000	-0.004	10.180	-3.028	-3.028	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.016	-0.006	11.095	0.204	0.204	0.000	0.000	0.000	0.000
22	A	22	ALA	0	-0.022	-0.009	12.752	0.964	0.964	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.030	-0.005	7.257	0.020	0.020	0.000	0.000	0.000	0.000
24	A	24	GLN	0	-0.034	-0.032	10.583	2.075	2.075	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.043	0.022	13.948	1.082	1.082	0.000	0.000	0.000	0.000
26	A	26	ALA	0	0.021	0.023	13.754	0.911	0.911	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.040	-0.023	10.947	0.531	0.531	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.902	-0.955	15.401	-16.677	-16.677	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.930	-0.961	18.686	-15.041	-15.041	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.033	-0.028	17.804	0.963	0.963	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.071	-0.027	18.850	0.754	0.754	0.000	0.000	0.000	0.000
32	A	32	ASN	0	-0.106	-0.065	20.647	1.303	1.303	0.000	0.000	0.000	0.000
33	A	33	GLY	0	-0.073	-0.027	23.045	0.692	0.692	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.868	-0.905	23.832	-12.294	-12.294	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.943	0.958	20.678	14.312	14.312	0.000	0.000	0.000	0.000
36	A	36	PRO	0	0.023	0.043	21.104	0.675	0.675	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.840	-0.942	22.265	-13.326	-13.326	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.076	-0.039	22.617	-0.058	-0.058	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.029	0.016	16.651	-0.705	-0.705	0.000	0.000	0.000	0.000
40	A	40	PRO	0	-0.008	-0.013	15.429	0.668	0.668	0.000	0.000	0.000	0.000
41	A	41	HIS	0	-0.060	-0.023	15.296	1.232	1.232	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.057	-0.030	13.504	-1.736	-1.736	0.000	0.000	0.000	0.000
43	A	43	TYR	-1	-0.819	-0.909	5.986	-26.483	-26.483	0.000	0.000	0.000	0.000
44	A	44	TYR	0	-0.045	-0.052	11.000	-0.025	-0.025	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.896	-0.954	6.477	-23.815	-23.815	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.147	-0.073	8.472	0.904	0.904	0.000	0.000	0.000	0.000
48	A	48	SER	-1	-0.729	-0.853	7.530	-21.141	-21.141	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-1.035	-1.024	9.187	-14.581	-14.581	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.984	-0.993	9.679	-18.822	-18.822	0.000	0.000	0.000	0.000
56	A	57	SER	0	0.015	-0.007	7.105	-0.555	-0.555	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.050	0.066	9.606	-1.648	-1.648	0.000	0.000	0.000	0.000
58	A	59	PRO	0	-0.069	-0.052	10.560	1.290	1.290	0.000	0.000	0.000	0.000
59	A	60	TRP	0	0.024	0.007	6.625	-0.260	-0.260	0.000	0.000	0.000	0.000
60	A	61	SER	0	-0.038	-0.026	9.982	3.767	3.767	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.838	-0.926	10.279	-24.065	-24.065	0.000	0.000	0.000	0.000
62	A	63	PHE	0	0.014	-0.011	12.023	1.960	1.960	0.000	0.000	0.000	0.000
63	A	64	PRO	0	-0.030	-0.005	13.696	-1.194	-1.194	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.044	-0.002	11.863	-0.384	-0.384	0.000	0.000	0.000	0.000
65	A	66	VAL	0	0.012	-0.011	15.352	1.042	1.042	0.000	0.000	0.000	0.000
66	A	67	TYR	0	-0.041	-0.036	18.145	-0.175	-0.175	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.115	-0.062	20.314	0.729	0.729	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.035	0.053	18.356	0.434	0.434	0.000	0.000	0.000	0.000
69	A	70	PRO	0	0.034	0.004	17.547	0.219	0.219	0.000	0.000	0.000	0.000
70	A	71	TYR	0	-0.029	-0.032	18.413	0.891	0.891	0.000	0.000	0.000	0.000
71	A	72	TYR	0	-0.040	-0.056	20.384	0.206	0.206	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.017	0.001	23.472	0.603	0.603	0.000	0.000	0.000	0.000
73	A	74	SER	0	0.044	0.015	26.456	0.070	0.070	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.824	0.896	29.564	9.495	9.495	0.000	0.000	0.000	0.000
75	A	76	ASP	-1	-0.854	-0.909	32.405	-8.762	-8.762	0.000	0.000	0.000	0.000
76	A	77	ASN	0	-0.087	-0.055	30.497	0.506	0.506	0.000	0.000	0.000	0.000
77	A	78	TYR	0	-0.034	-0.002	25.132	-0.194	-0.194	0.000	0.000	0.000	0.000
78	A	79	VAL	0	0.000	0.002	25.232	0.291	0.291	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.003	0.005	24.519	-0.481	-0.481	0.000	0.000	0.000	0.000
80	A	81	PRO	0	0.039	0.029	19.557	-0.105	-0.105	0.000	0.000	0.000	0.000
81	A	82	GLY	0	0.003	0.003	19.632	-0.678	-0.678	0.000	0.000	0.000	0.000
82	A	83	PRO	0	-0.030	-0.014	18.267	-0.184	-0.184	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.695	-0.790	14.950	-18.045	-18.045	0.000	0.000	0.000	0.000
84	A	85	ARG	1	0.845	0.928	11.640	18.901	18.901	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.009	-0.004	8.477	-1.659	-1.659	0.000	0.000	0.000	0.000
86	A	87	ILE	0	0.052	0.025	6.234	1.891	1.891	0.000	0.000	0.000	0.000
87	A	88	TYR	0	0.003	-0.011	6.520	-6.101	-6.101	0.000	0.000	0.000	0.000
88	A	89	GLN	0	0.046	0.014	6.807	1.810	1.810	0.000	0.000	0.000	0.000
89	A	90	THR	0	0.010	0.004	8.417	0.294	0.294	0.000	0.000	0.000	0.000
90	A	91	ASN	0	-0.053	-0.030	11.657	1.610	1.610	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.061	-0.041	7.398	1.086	1.086	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.048	0.033	8.486	1.057	1.057	0.000	0.000	0.000	0.000
97	A	99	VAL	0	0.033	0.019	7.509	0.147	0.147	0.000	0.000	0.000	0.000
98	A	100	THR	0	-0.005	-0.051	10.139	1.266	1.266	0.000	0.000	0.000	0.000
99	A	101	HIS	0	-0.014	-0.001	13.865	0.022	0.022	0.000	0.000	0.000	0.000
100	A	102	THR	0	-0.089	-0.043	16.740	1.237	1.237	0.000	0.000	0.000	0.000
101	A	103	GLY	0	-0.015	-0.010	17.104	-0.498	-0.498	0.000	0.000	0.000	0.000
102	A	104	ALA	0	0.015	0.033	15.978	0.009	0.009	0.000	0.000	0.000	0.000
103	A	105	ALA	0	-0.049	-0.033	17.472	0.707	0.707	0.000	0.000	0.000	0.000
104	A	106	SER	0	-0.077	-0.068	19.435	0.565	0.565	0.000	0.000	0.000	0.000
105	A	107	TYR	0	-0.053	-0.042	19.651	-0.232	-0.232	0.000	0.000	0.000	0.000
106	A	108	ASP	-1	-0.866	-0.905	19.340	-13.126	-13.126	0.000	0.000	0.000	0.000
107	A	109	GLY	0	0.005	0.024	16.229	-0.636	-0.636	0.000	0.000	0.000	0.000
108	A	110	PHE	0	-0.012	-0.017	11.616	0.019	0.019	0.000	0.000	0.000	0.000
109	A	111	THR	0	-0.012	-0.004	11.572	0.620	0.620	0.000	0.000	0.000	0.000
111	A	114	SER	-1	-0.843	-0.888	9.421	-25.195	-25.195	0.000	0.000	0.000	0.000

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