FMO DATABASE

FMODB ID: NZM7Q

Calculation Name: 2FRH-A-Xray547

Preferred Name:

Target Type:

Ligand Name: calcium ion

Ligand 3-letter code: CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FRH

Chain ID: A

ChEMBL ID:

UniProt ID: Q7A1N5

Base Structure: X-ray

Registration Date: 2025-10-04

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1112809.410237
FMO2-HF: Nuclear repulsion	1060684.012449
FMO2-HF: Total energy	-52125.397789
FMO2-MP2: Total energy	-52278.876692

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:98:GLY)

Summations of interaction energy for fragment #1(A:98: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.
-58.096	-53.944	1.289	-3.132	-2.308	-0.041

Interaction energy analysis for fragmet #1(A:98:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.816 / q_NPA : 0.895

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	100	HIS	0	-0.031	-0.039	2.317	-22.535	-18.514	1.289	-3.036	-2.273	-0.040
4	A	101	MET	0	0.000	0.017	3.961	-10.890	-10.759	0.000	-0.096	-0.035	-0.001
5	A	102	ALA	0	-0.006	-0.002	5.716	1.003	1.003	0.000	0.000	0.000	0.000
6	A	103	ILE	0	0.012	0.001	6.923	3.516	3.516	0.000	0.000	0.000	0.000
7	A	104	THR	0	-0.002	0.001	10.522	-0.087	-0.087	0.000	0.000	0.000	0.000
8	A	105	LYS	1	0.907	0.946	12.480	24.116	24.116	0.000	0.000	0.000	0.000
9	A	106	ILE	0	0.024	0.028	15.521	0.097	0.097	0.000	0.000	0.000	0.000
10	A	107	ASN	0	-0.069	-0.046	19.172	0.035	0.035	0.000	0.000	0.000	0.000
11	A	108	ASP	-1	-0.793	-0.874	21.938	-11.841	-11.841	0.000	0.000	0.000	0.000
12	A	109	CYS	0	-0.003	-0.037	24.279	-0.412	-0.412	0.000	0.000	0.000	0.000
13	A	110	PHE	0	0.013	0.025	26.656	0.087	0.087	0.000	0.000	0.000	0.000
14	A	111	GLU	-1	-0.785	-0.896	21.584	-15.008	-15.008	0.000	0.000	0.000	0.000
15	A	112	LEU	0	-0.044	-0.021	21.808	-0.501	-0.501	0.000	0.000	0.000	0.000
16	A	113	LEU	0	0.012	0.004	22.880	-0.251	-0.251	0.000	0.000	0.000	0.000
17	A	114	SER	0	0.016	0.012	23.165	0.196	0.196	0.000	0.000	0.000	0.000
18	A	115	MET	0	-0.016	-0.008	15.938	-0.316	-0.316	0.000	0.000	0.000	0.000
19	A	116	VAL	0	-0.034	-0.018	20.530	-0.378	-0.378	0.000	0.000	0.000	0.000
20	A	117	THR	0	-0.007	-0.014	22.694	0.203	0.203	0.000	0.000	0.000	0.000
21	A	118	TYR	0	-0.051	-0.042	16.803	-0.225	-0.225	0.000	0.000	0.000	0.000
22	A	119	ALA	0	0.021	0.003	18.993	-0.109	-0.109	0.000	0.000	0.000	0.000
23	A	120	ASP	-1	-0.856	-0.945	20.409	-12.937	-12.937	0.000	0.000	0.000	0.000
24	A	121	LYS	1	0.894	0.974	23.942	12.149	12.149	0.000	0.000	0.000	0.000
25	A	122	LEU	0	0.049	0.037	18.112	0.275	0.275	0.000	0.000	0.000	0.000
26	A	123	LYS	1	0.811	0.904	20.745	14.143	14.143	0.000	0.000	0.000	0.000
27	A	124	SER	0	-0.088	-0.046	22.703	0.484	0.484	0.000	0.000	0.000	0.000
28	A	125	LEU	0	0.026	0.009	24.292	0.393	0.393	0.000	0.000	0.000	0.000
29	A	126	ILE	0	-0.019	-0.018	19.384	0.191	0.191	0.000	0.000	0.000	0.000
30	A	127	LYS	1	0.896	0.967	23.755	12.541	12.541	0.000	0.000	0.000	0.000
31	A	128	LYS	1	0.928	0.976	26.632	10.419	10.419	0.000	0.000	0.000	0.000
32	A	129	GLU	-1	-0.843	-0.914	27.047	-11.085	-11.085	0.000	0.000	0.000	0.000
33	A	130	PHE	0	-0.046	-0.041	23.980	-0.365	-0.365	0.000	0.000	0.000	0.000
34	A	131	SER	0	-0.045	-0.005	27.252	0.184	0.184	0.000	0.000	0.000	0.000
35	A	132	ILE	0	0.009	0.023	22.889	0.079	0.079	0.000	0.000	0.000	0.000
36	A	133	SER	0	-0.052	-0.080	25.546	-0.207	-0.207	0.000	0.000	0.000	0.000
37	A	134	PHE	0	0.020	-0.022	17.533	-0.316	-0.316	0.000	0.000	0.000	0.000
38	A	135	GLU	-1	-0.830	-0.902	20.208	-13.665	-13.665	0.000	0.000	0.000	0.000
39	A	136	GLU	-1	-0.814	-0.871	21.015	-12.425	-12.425	0.000	0.000	0.000	0.000
40	A	137	PHE	0	0.051	0.025	16.144	-0.503	-0.503	0.000	0.000	0.000	0.000
41	A	138	ALA	0	-0.012	-0.006	16.486	-1.022	-1.022	0.000	0.000	0.000	0.000
42	A	139	VAL	0	-0.002	-0.005	16.367	-1.000	-1.000	0.000	0.000	0.000	0.000
43	A	140	LEU	0	0.017	0.005	17.843	-0.581	-0.581	0.000	0.000	0.000	0.000
44	A	141	THR	0	-0.020	-0.019	13.265	-1.030	-1.030	0.000	0.000	0.000	0.000
45	A	142	TYR	0	-0.029	-0.020	13.112	-1.290	-1.290	0.000	0.000	0.000	0.000
46	A	143	ILE	0	0.017	0.003	13.809	-0.858	-0.858	0.000	0.000	0.000	0.000
47	A	144	SER	0	-0.011	0.001	13.748	0.602	0.602	0.000	0.000	0.000	0.000
48	A	145	GLU	-1	-0.798	-0.895	7.096	-40.946	-40.946	0.000	0.000	0.000	0.000
49	A	146	ASN	0	-0.076	-0.030	10.438	-2.408	-2.408	0.000	0.000	0.000	0.000
50	A	147	LYS	1	0.827	0.926	10.688	27.564	27.564	0.000	0.000	0.000	0.000
51	A	148	GLU	-1	-0.829	-0.898	14.738	-19.709	-19.709	0.000	0.000	0.000	0.000
52	A	149	LYS	1	0.875	0.937	17.680	13.795	13.795	0.000	0.000	0.000	0.000
53	A	150	GLU	-1	-0.889	-0.949	20.863	-14.022	-14.022	0.000	0.000	0.000	0.000
54	A	151	TYR	0	0.027	-0.014	16.131	-0.180	-0.180	0.000	0.000	0.000	0.000
55	A	152	TYR	0	0.025	0.011	20.965	1.154	1.154	0.000	0.000	0.000	0.000
56	A	153	LEU	0	0.002	0.006	21.505	-0.622	-0.622	0.000	0.000	0.000	0.000
57	A	154	LYS	1	0.891	0.932	21.339	13.995	13.995	0.000	0.000	0.000	0.000
58	A	155	ASP	-1	-0.822	-0.911	17.867	-15.642	-15.642	0.000	0.000	0.000	0.000
59	A	156	ILE	0	0.013	0.007	18.155	-0.756	-0.756	0.000	0.000	0.000	0.000
60	A	157	ILE	0	-0.041	-0.038	19.012	-0.227	-0.227	0.000	0.000	0.000	0.000
61	A	158	ASN	0	-0.064	-0.024	19.180	0.146	0.146	0.000	0.000	0.000	0.000
62	A	159	HIS	0	0.037	0.038	13.450	-1.308	-1.308	0.000	0.000	0.000	0.000
63	A	160	LEU	0	-0.027	0.008	15.097	-0.952	-0.952	0.000	0.000	0.000	0.000
64	A	161	ASN	0	-0.017	-0.014	16.490	1.181	1.181	0.000	0.000	0.000	0.000
65	A	162	TYR	0	0.047	0.015	18.294	0.713	0.713	0.000	0.000	0.000	0.000
66	A	163	LYS	1	0.971	0.984	22.812	12.725	12.725	0.000	0.000	0.000	0.000
67	A	164	GLN	0	0.071	0.033	25.256	0.066	0.066	0.000	0.000	0.000	0.000
68	A	165	PRO	0	0.005	0.000	26.950	-0.023	-0.023	0.000	0.000	0.000	0.000
69	A	166	GLN	0	-0.054	-0.026	25.816	0.434	0.434	0.000	0.000	0.000	0.000
70	A	167	VAL	0	0.042	0.026	22.022	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	168	VAL	0	0.029	0.004	24.537	0.022	0.022	0.000	0.000	0.000	0.000
72	A	169	LYS	1	0.932	0.974	27.578	10.401	10.401	0.000	0.000	0.000	0.000
73	A	170	ALA	0	0.045	0.012	24.203	0.210	0.210	0.000	0.000	0.000	0.000
74	A	171	VAL	0	0.024	0.005	23.808	0.021	0.021	0.000	0.000	0.000	0.000
75	A	172	LYS	1	0.925	0.967	26.122	9.383	9.383	0.000	0.000	0.000	0.000
76	A	173	ILE	0	0.001	0.009	28.420	0.281	0.281	0.000	0.000	0.000	0.000
77	A	174	LEU	0	0.038	0.009	22.865	0.091	0.091	0.000	0.000	0.000	0.000
78	A	175	SER	0	-0.047	-0.016	27.024	0.067	0.067	0.000	0.000	0.000	0.000
79	A	176	GLN	0	-0.032	-0.025	29.150	0.239	0.239	0.000	0.000	0.000	0.000
80	A	177	GLU	-1	-0.934	-0.957	28.700	-10.088	-10.088	0.000	0.000	0.000	0.000
81	A	178	ASP	-1	-0.896	-0.938	29.620	-10.766	-10.766	0.000	0.000	0.000	0.000
82	A	179	TYR	0	-0.025	-0.021	23.924	-0.348	-0.348	0.000	0.000	0.000	0.000
83	A	180	PHE	0	-0.018	-0.034	22.504	-0.680	-0.680	0.000	0.000	0.000	0.000
84	A	181	ASP	-1	-0.862	-0.895	26.029	-10.525	-10.525	0.000	0.000	0.000	0.000
85	A	182	LYS	0	-0.031	0.016	26.991	0.214	0.214	0.000	0.000	0.000	0.000
86	A	183	LYS	1	0.955	0.985	28.557	9.893	9.893	0.000	0.000	0.000	0.000
87	A	184	ARG	1	0.894	0.917	30.530	9.782	9.782	0.000	0.000	0.000	0.000
88	A	185	ASN	0	-0.010	-0.013	31.730	-0.240	-0.240	0.000	0.000	0.000	0.000
89	A	186	GLU	-1	-0.934	-0.951	35.220	-7.684	-7.684	0.000	0.000	0.000	0.000
90	A	187	HIS	0	0.052	0.002	37.735	0.127	0.127	0.000	0.000	0.000	0.000
91	A	188	ASP	-1	-0.849	-0.905	33.553	-9.676	-9.676	0.000	0.000	0.000	0.000
92	A	189	GLU	-1	-0.896	-0.960	33.100	-8.932	-8.932	0.000	0.000	0.000	0.000
93	A	190	ARG	1	0.856	0.948	26.571	10.896	10.896	0.000	0.000	0.000	0.000
94	A	191	THR	0	-0.077	-0.042	28.508	-0.347	-0.347	0.000	0.000	0.000	0.000
95	A	192	VAL	0	-0.039	-0.035	27.083	-0.454	-0.454	0.000	0.000	0.000	0.000
96	A	193	LEU	0	-0.016	0.011	25.253	-0.428	-0.428	0.000	0.000	0.000	0.000
97	A	194	ILE	0	0.024	0.004	22.795	0.466	0.466	0.000	0.000	0.000	0.000
98	A	195	LEU	0	-0.016	-0.005	24.003	-0.249	-0.249	0.000	0.000	0.000	0.000
99	A	196	VAL	0	0.008	0.003	20.536	0.185	0.185	0.000	0.000	0.000	0.000
100	A	197	ASN	0	0.116	0.066	23.410	-0.635	-0.635	0.000	0.000	0.000	0.000
101	A	198	ALA	0	-0.033	-0.049	23.312	-0.382	-0.382	0.000	0.000	0.000	0.000
102	A	199	GLN	0	-0.068	-0.046	24.151	-0.380	-0.380	0.000	0.000	0.000	0.000
103	A	200	GLN	0	0.033	0.002	25.063	-0.575	-0.575	0.000	0.000	0.000	0.000
104	A	201	ARG	1	0.866	0.953	16.821	17.105	17.105	0.000	0.000	0.000	0.000
105	A	202	LYS	1	0.969	0.988	21.206	11.652	11.652	0.000	0.000	0.000	0.000
106	A	203	LYS	1	0.840	0.929	23.032	11.118	11.118	0.000	0.000	0.000	0.000
107	A	204	ILE	0	0.019	0.011	18.581	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	205	GLU	-1	-0.906	-0.960	16.897	-18.141	-18.141	0.000	0.000	0.000	0.000
109	A	206	SER	0	-0.043	-0.022	19.362	-0.265	-0.265	0.000	0.000	0.000	0.000
110	A	207	LEU	0	-0.024	-0.007	21.093	0.087	0.087	0.000	0.000	0.000	0.000
111	A	208	LEU	0	0.054	0.014	15.720	0.009	0.009	0.000	0.000	0.000	0.000
112	A	209	SER	0	-0.029	-0.006	18.243	-0.342	-0.342	0.000	0.000	0.000	0.000
113	A	210	ARG	1	0.907	0.949	19.175	12.510	12.510	0.000	0.000	0.000	0.000
114	A	211	VAL	0	0.037	0.025	18.646	0.226	0.226	0.000	0.000	0.000	0.000
115	A	212	ASN	0	0.024	0.004	14.533	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	213	LYS	1	0.914	0.975	18.002	14.215	14.215	0.000	0.000	0.000	0.000
117	A	214	ARG	1	0.850	0.917	21.182	12.418	12.418	0.000	0.000	0.000	0.000
118	A	215	ILE	0	-0.016	0.001	16.599	0.339	0.339	0.000	0.000	0.000	0.000
119	A	216	THR	0	-0.067	-0.043	18.840	-0.223	-0.223	0.000	0.000	0.000	0.000
120	A	217	GLU	-1	-0.842	-0.929	20.369	-11.623	-11.623	0.000	0.000	0.000	0.000
121	A	218	ALA	0	-0.010	-0.003	22.053	0.383	0.383	0.000	0.000	0.000	0.000
122	A	219	ASN	0	-0.003	0.005	17.578	0.475	0.475	0.000	0.000	0.000	0.000
123	A	220	ASN	0	-0.058	-0.024	21.967	-0.038	-0.038	0.000	0.000	0.000	0.000
124	A	221	GLU	-1	-0.906	-0.939	25.261	-10.174	-10.174	0.000	0.000	0.000	0.000
125	A	222	ILE	0	-0.126	-0.070	22.576	0.230	0.230	0.000	0.000	0.000	0.000
126	A	223	GLU	-1	-0.971	-0.993	24.887	-12.141	-12.141	0.000	0.000	0.000	0.000
127	A	224	LEU	-1	-0.944	-0.955	25.746	-11.649	-11.649	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:98:GLY)