FMO DATABASE

FMODB ID: 194RZ

Calculation Name: 1S6B-A-Xray547

Preferred Name:

Target Type:

Ligand Name: phosphate ion | acetic acid | calcium ion

Ligand 3-letter code: PO4 | ACY | CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1S6B

Chain ID: A

ChEMBL ID:

UniProt ID: P60044

Base Structure: X-ray

Registration Date: 2025-10-05

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	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-962301.749409
FMO2-HF: Nuclear repulsion	912251.138043
FMO2-HF: Total energy	-50050.611365
FMO2-MP2: Total energy	-50184.070979

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:ASN)

Summations of interaction energy for fragment #1(A:1: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.
-106.768	-93.779	41.152	-23.377	-30.764	-0.156

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.767 / q_NPA : 0.887

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	TYR	0	0.001	0.004	2.358	1.094	3.911	3.172	-2.175	-3.815	0.021
4	A	4	GLN	0	-0.012	0.003	2.012	-36.423	-35.169	13.015	-5.996	-8.273	-0.015
5	A	5	PHE	0	0.057	0.045	3.682	4.931	5.660	0.016	-0.328	-0.417	0.001
6	A	6	LYS	1	0.890	0.956	5.290	29.421	29.548	-0.001	-0.006	-0.119	0.000
50	A	52	TYR	0	-0.047	-0.090	4.643	-0.929	-0.867	-0.001	-0.004	-0.057	0.000
61	A	63	PRO	0	0.002	0.007	4.721	-7.084	-6.856	-0.001	-0.028	-0.199	0.000
62	A	64	LYS	1	0.990	1.004	2.487	13.458	15.915	1.066	-1.555	-1.968	-0.018
63	A	65	GLN	0	0.024	0.005	2.672	-12.323	-9.842	1.099	-1.707	-1.873	-0.020
64	A	66	LYS	1	0.899	0.966	2.712	33.209	35.460	1.373	-1.428	-2.197	-0.015
65	A	67	THR	0	0.016	0.007	1.824	-51.977	-54.530	17.210	-7.059	-7.598	-0.075
66	A	68	TYR	0	-0.073	-0.058	2.242	7.349	8.382	4.146	-1.907	-3.272	-0.023
67	A	69	SER	0	0.001	-0.002	5.199	-0.961	-0.939	-0.001	-0.001	-0.020	0.000
86	A	90	VAL	0	-0.001	-0.003	3.391	-0.474	-0.207	0.012	-0.080	-0.198	-0.001
88	A	94	ASP	-1	-0.718	-0.807	2.961	-73.629	-71.815	0.047	-1.103	-0.758	-0.011
7	A	7	ASN	0	-0.031	-0.028	6.279	4.564	4.564	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.033	-0.009	5.854	3.186	3.186	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.042	0.025	9.072	2.616	2.616	0.000	0.000	0.000	0.000
10	A	10	GLN	0	-0.034	-0.021	10.400	0.658	0.658	0.000	0.000	0.000	0.000
11	A	11	CYS	0	-0.076	-0.011	11.677	1.808	1.808	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.018	-0.034	12.905	1.084	1.084	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.008	0.002	14.932	1.453	1.453	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.012	0.012	16.681	0.067	0.067	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.872	0.935	17.646	13.759	13.759	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.879	0.948	18.176	14.740	14.740	0.000	0.000	0.000	0.000
17	A	18	SER	0	0.030	0.034	16.168	-1.094	-1.094	0.000	0.000	0.000	0.000
18	A	19	TRP	0	0.107	0.021	10.738	0.015	0.015	0.000	0.000	0.000	0.000
19	A	20	TRP	0	-0.023	-0.022	13.318	-0.828	-0.828	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.801	-0.873	15.543	-14.690	-14.690	0.000	0.000	0.000	0.000
21	A	22	PHE	0	0.063	0.017	13.871	0.469	0.469	0.000	0.000	0.000	0.000
22	A	23	ALA	0	-0.062	-0.037	13.049	-0.044	-0.044	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.919	-0.959	14.417	-15.446	-15.446	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.050	-0.048	17.312	1.010	1.010	0.000	0.000	0.000	0.000
25	A	26	GLY	0	0.009	-0.008	18.463	-0.640	-0.640	0.000	0.000	0.000	0.000
26	A	27	CYS	0	-0.102	-0.024	20.791	0.173	0.173	0.000	0.000	0.000	0.000
27	A	28	TYR	0	-0.052	-0.053	16.352	-0.445	-0.445	0.000	0.000	0.000	0.000
28	A	29	CYS	0	-0.121	-0.020	13.815	-2.782	-2.782	0.000	0.000	0.000	0.000
29	A	30	GLY	0	0.027	0.017	13.448	-1.527	-1.527	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.874	0.933	14.673	15.817	15.817	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.078	0.044	17.477	0.409	0.409	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.034	-0.011	17.215	0.034	0.034	0.000	0.000	0.000	0.000
33	A	34	SER	0	-0.083	-0.047	17.858	0.323	0.323	0.000	0.000	0.000	0.000
34	A	35	GLY	0	0.112	0.068	21.471	0.025	0.025	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.033	-0.008	23.787	-0.447	-0.447	0.000	0.000	0.000	0.000
36	A	37	PRO	0	-0.054	-0.022	21.473	-0.024	-0.024	0.000	0.000	0.000	0.000
37	A	38	ILE	0	-0.022	-0.005	23.279	0.488	0.488	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.786	-0.852	22.273	-13.106	-13.106	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.805	-0.906	22.411	-13.015	-13.015	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.014	0.004	16.564	-0.806	-0.806	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.703	-0.870	17.647	-16.296	-16.296	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.848	0.920	18.402	12.759	12.759	0.000	0.000	0.000	0.000
43	A	44	CYS	0	-0.077	-0.025	14.435	1.229	1.229	0.000	0.000	0.000	0.000
44	A	46	GLN	0	0.042	0.033	14.238	-0.998	-0.998	0.000	0.000	0.000	0.000
45	A	47	VAL	0	-0.035	-0.018	14.457	-0.277	-0.277	0.000	0.000	0.000	0.000
46	A	48	HIS	0	-0.061	-0.032	6.677	1.995	1.995	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.849	-0.927	11.094	-24.943	-24.943	0.000	0.000	0.000	0.000
48	A	50	ASN	0	-0.011	-0.012	12.741	-0.524	-0.524	0.000	0.000	0.000	0.000
49	A	51	CYS	0	-0.027	0.021	7.242	1.974	1.974	0.000	0.000	0.000	0.000
51	A	53	ASN	0	-0.022	-0.014	10.022	-1.948	-1.948	0.000	0.000	0.000	0.000
52	A	54	SER	0	0.064	0.028	13.115	0.614	0.614	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.051	-0.024	9.433	-0.059	-0.059	0.000	0.000	0.000	0.000
54	A	56	ARG	1	0.833	0.900	8.973	26.490	26.490	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.888	-0.922	12.113	-17.135	-17.135	0.000	0.000	0.000	0.000
56	A	58	GLN	0	-0.047	-0.011	10.808	1.271	1.271	0.000	0.000	0.000	0.000
57	A	59	GLY	0	0.079	0.031	13.158	-1.338	-1.338	0.000	0.000	0.000	0.000
58	A	60	GLY	0	-0.006	-0.007	12.774	-0.568	-0.568	0.000	0.000	0.000	0.000
59	A	61	CYS	0	-0.090	-0.003	8.199	-6.766	-6.766	0.000	0.000	0.000	0.000
60	A	62	ARG	1	1.007	0.994	7.464	29.373	29.373	0.000	0.000	0.000	0.000
68	A	70	TYR	0	0.011	-0.006	6.076	-0.759	-0.759	0.000	0.000	0.000	0.000
69	A	71	GLU	-1	-0.886	-0.931	8.920	-18.693	-18.693	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.923	0.952	13.209	18.514	18.514	0.000	0.000	0.000	0.000
71	A	74	ALA	0	-0.006	-0.001	17.039	0.041	0.041	0.000	0.000	0.000	0.000
72	A	75	GLY	0	0.083	0.057	16.399	0.580	0.580	0.000	0.000	0.000	0.000
73	A	76	THR	0	-0.083	-0.045	15.785	-0.545	-0.545	0.000	0.000	0.000	0.000
74	A	77	LEU	0	0.001	-0.010	9.832	-0.539	-0.539	0.000	0.000	0.000	0.000
75	A	78	SER	0	0.020	0.011	12.423	0.893	0.893	0.000	0.000	0.000	0.000
76	A	79	CYS	0	-0.038	-0.008	5.140	-4.614	-4.614	0.000	0.000	0.000	0.000
77	A	80	SER	0	0.013	-0.002	10.558	1.565	1.565	0.000	0.000	0.000	0.000
78	A	81	GLY	0	0.035	0.010	12.141	-1.228	-1.228	0.000	0.000	0.000	0.000
79	A	82	SER	0	0.010	0.006	12.661	0.073	0.073	0.000	0.000	0.000	0.000
80	A	83	ASN	0	-0.052	-0.018	8.108	-4.124	-4.124	0.000	0.000	0.000	0.000
81	A	84	ASN	0	0.084	0.031	9.819	-0.953	-0.953	0.000	0.000	0.000	0.000
82	A	85	SER	0	0.059	0.011	10.260	-1.915	-1.915	0.000	0.000	0.000	0.000
83	A	87	ALA	0	0.008	-0.016	5.844	-4.475	-4.475	0.000	0.000	0.000	0.000
84	A	88	ALA	0	-0.006	-0.001	6.447	-4.224	-4.224	0.000	0.000	0.000	0.000
85	A	89	THR	0	0.023	0.007	9.112	0.086	0.086	0.000	0.000	0.000	0.000
87	A	92	ASP	-1	-0.791	-0.881	6.004	-22.305	-22.305	0.000	0.000	0.000	0.000
89	A	95	ARG	1	0.881	0.901	6.634	26.850	26.850	0.000	0.000	0.000	0.000
90	A	96	LEU	0	-0.041	-0.019	9.453	2.577	2.577	0.000	0.000	0.000	0.000
91	A	97	ALA	0	0.026	0.023	9.545	1.920	1.920	0.000	0.000	0.000	0.000
92	A	98	ALA	0	0.005	0.000	9.643	1.709	1.709	0.000	0.000	0.000	0.000
93	A	99	ILE	0	-0.004	0.006	11.550	1.763	1.763	0.000	0.000	0.000	0.000
94	A	101	PHE	0	0.004	-0.035	12.031	0.698	0.698	0.000	0.000	0.000	0.000
95	A	102	ALA	0	-0.020	-0.003	15.895	0.732	0.732	0.000	0.000	0.000	0.000
96	A	103	GLY	0	-0.030	-0.001	17.983	0.833	0.833	0.000	0.000	0.000	0.000
97	A	104	ALA	0	-0.010	0.002	19.381	0.752	0.752	0.000	0.000	0.000	0.000
98	A	105	PRO	0	-0.028	-0.019	21.142	-0.100	-0.100	0.000	0.000	0.000	0.000
99	A	106	TYR	0	-0.063	-0.041	19.048	-0.011	-0.011	0.000	0.000	0.000	0.000
100	A	107	ASN	0	0.005	-0.008	22.927	0.722	0.722	0.000	0.000	0.000	0.000
101	A	108	ASP	-1	-0.812	-0.923	24.955	-12.149	-12.149	0.000	0.000	0.000	0.000
102	A	109	ASN	0	-0.059	-0.022	26.235	0.028	0.028	0.000	0.000	0.000	0.000
103	A	110	ASN	0	-0.043	-0.046	23.847	0.558	0.558	0.000	0.000	0.000	0.000
104	A	111	TYR	0	-0.028	-0.017	18.536	-0.419	-0.419	0.000	0.000	0.000	0.000
105	A	112	ASN	0	-0.040	-0.011	21.831	0.628	0.628	0.000	0.000	0.000	0.000
106	A	113	ILE	0	-0.002	0.011	23.275	0.696	0.696	0.000	0.000	0.000	0.000
107	A	114	ASP	-1	-0.854	-0.933	24.813	-10.777	-10.777	0.000	0.000	0.000	0.000
108	A	115	LEU	0	0.047	-0.007	20.968	0.177	0.177	0.000	0.000	0.000	0.000
109	A	116	LYS	1	0.912	0.969	25.180	9.720	9.720	0.000	0.000	0.000	0.000
110	A	117	ALA	0	-0.048	-0.030	28.322	0.265	0.265	0.000	0.000	0.000	0.000
111	A	118	ARG	1	0.860	0.915	26.677	11.361	11.361	0.000	0.000	0.000	0.000
112	A	120	GLN	-1	-0.902	-0.941	25.714	-10.998	-10.998	0.000	0.000	0.000	0.000

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