FMO DATABASE

FMODB ID: MLV4Z

Calculation Name: 1V30-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-[n-cyclohexylamino]ethane sulfonic acid

Ligand 3-letter code: NHE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V30

Chain ID: A

ChEMBL ID:

UniProt ID: O58558

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1060607.257501
FMO2-HF: Nuclear repulsion	1013159.295723
FMO2-HF: Total energy	-47447.961778
FMO2-MP2: Total energy	-47591.772341

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:7:SER)

Summations of interaction energy for fragment #1(A:7:SER)

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.
3.77	10.654	8.298	-7.616	-7.564	-0.079

Interaction energy analysis for fragmet #1(A:7:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.772 / q_NPA : 0.880

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	9	ARG	1	0.902	0.965	3.838	38.707	39.914	-0.015	-0.430	-0.763	0.000
4	A	10	ILE	0	0.020	0.010	5.671	1.908	1.934	-0.001	-0.002	-0.023	0.000
24	A	30	LYS	1	0.857	0.929	3.576	45.871	45.996	-0.001	-0.043	-0.080	0.000
57	A	63	GLU	-1	-0.839	-0.912	2.038	-70.633	-67.640	4.475	-3.727	-3.740	-0.041
58	A	64	VAL	0	0.026	0.017	4.155	3.457	3.795	0.000	-0.097	-0.240	0.000
59	A	65	ASP	-1	-0.783	-0.875	2.265	-63.079	-61.124	3.842	-3.279	-2.518	-0.037
60	A	66	LYS	1	0.933	0.956	3.480	35.647	35.855	-0.001	-0.027	-0.180	-0.001
61	A	67	GLU	-1	-0.794	-0.873	4.715	-21.588	-21.556	-0.001	-0.011	-0.020	0.000
5	A	11	ALA	0	0.011	0.001	8.931	0.613	0.613	0.000	0.000	0.000	0.000
6	A	12	VAL	0	0.000	-0.003	12.278	0.887	0.887	0.000	0.000	0.000	0.000
7	A	13	TYR	0	0.046	-0.004	14.773	0.702	0.702	0.000	0.000	0.000	0.000
8	A	14	GLY	0	0.024	0.003	18.501	0.749	0.749	0.000	0.000	0.000	0.000
9	A	15	THR	0	0.020	-0.018	19.472	-0.094	-0.094	0.000	0.000	0.000	0.000
10	A	16	LEU	0	0.036	0.021	13.531	0.131	0.131	0.000	0.000	0.000	0.000
11	A	17	ARG	1	0.770	0.884	15.432	13.581	13.581	0.000	0.000	0.000	0.000
12	A	18	LYS	1	1.002	0.970	17.106	14.919	14.919	0.000	0.000	0.000	0.000
13	A	19	GLY	0	-0.043	-0.030	18.249	0.739	0.739	0.000	0.000	0.000	0.000
14	A	20	LYS	1	0.815	0.927	19.983	14.165	14.165	0.000	0.000	0.000	0.000
15	A	21	PRO	0	0.027	-0.006	20.411	-0.564	-0.564	0.000	0.000	0.000	0.000
16	A	22	LEU	0	0.048	0.029	17.149	0.076	0.076	0.000	0.000	0.000	0.000
17	A	23	HIS	0	-0.018	-0.004	14.619	-0.264	-0.264	0.000	0.000	0.000	0.000
18	A	24	TRP	0	-0.050	-0.034	15.494	-1.062	-1.062	0.000	0.000	0.000	0.000
19	A	25	TYR	0	0.077	0.039	12.518	-0.483	-0.483	0.000	0.000	0.000	0.000
20	A	26	LEU	0	-0.039	-0.021	9.941	-2.004	-2.004	0.000	0.000	0.000	0.000
21	A	27	LYS	1	0.905	0.947	11.953	16.259	16.259	0.000	0.000	0.000	0.000
22	A	28	GLY	0	0.035	0.037	10.368	0.881	0.881	0.000	0.000	0.000	0.000
23	A	29	ALA	0	-0.058	-0.014	7.632	-2.695	-2.695	0.000	0.000	0.000	0.000
25	A	31	PHE	0	-0.010	-0.005	7.141	-1.217	-1.217	0.000	0.000	0.000	0.000
26	A	32	LEU	0	-0.048	-0.023	6.033	-0.188	-0.188	0.000	0.000	0.000	0.000
27	A	33	GLY	0	0.046	0.019	10.027	1.395	1.395	0.000	0.000	0.000	0.000
28	A	34	GLU	-1	-0.846	-0.921	13.359	-15.003	-15.003	0.000	0.000	0.000	0.000
29	A	35	ASP	-1	-0.825	-0.916	14.995	-16.583	-16.583	0.000	0.000	0.000	0.000
30	A	36	TRP	0	-0.009	-0.001	16.975	0.381	0.381	0.000	0.000	0.000	0.000
31	A	37	ILE	0	0.000	0.011	15.646	-0.346	-0.346	0.000	0.000	0.000	0.000
32	A	38	GLU	-1	-0.875	-0.957	19.761	-11.235	-11.235	0.000	0.000	0.000	0.000
33	A	39	GLY	0	-0.007	0.003	22.644	-0.375	-0.375	0.000	0.000	0.000	0.000
34	A	40	TYR	0	-0.040	-0.042	20.722	-0.214	-0.214	0.000	0.000	0.000	0.000
35	A	41	GLN	0	-0.079	-0.033	24.402	0.455	0.455	0.000	0.000	0.000	0.000
36	A	42	LEU	0	0.016	0.013	23.206	-0.388	-0.388	0.000	0.000	0.000	0.000
37	A	43	TYR	0	-0.031	-0.026	26.042	0.582	0.582	0.000	0.000	0.000	0.000
38	A	44	PHE	0	0.035	0.007	26.966	-0.587	-0.587	0.000	0.000	0.000	0.000
39	A	45	GLU	-1	-0.762	-0.845	29.041	-9.019	-9.019	0.000	0.000	0.000	0.000
40	A	46	TYR	0	0.020	0.023	29.979	0.060	0.060	0.000	0.000	0.000	0.000
41	A	47	LEU	0	-0.003	0.005	24.043	-0.320	-0.320	0.000	0.000	0.000	0.000
42	A	48	PRO	0	-0.032	0.011	22.310	0.294	0.294	0.000	0.000	0.000	0.000
43	A	49	TYR	0	0.026	0.004	23.660	-0.360	-0.360	0.000	0.000	0.000	0.000
44	A	50	ALA	0	0.030	0.028	20.890	0.341	0.341	0.000	0.000	0.000	0.000
45	A	51	VAL	0	0.021	0.003	22.979	-0.212	-0.212	0.000	0.000	0.000	0.000
46	A	52	LYS	1	0.908	0.935	22.158	13.965	13.965	0.000	0.000	0.000	0.000
47	A	53	GLY	0	0.003	-0.005	25.700	0.464	0.464	0.000	0.000	0.000	0.000
48	A	54	LYS	1	0.941	0.964	27.774	9.421	9.421	0.000	0.000	0.000	0.000
49	A	55	GLY	0	0.013	0.000	28.113	0.320	0.320	0.000	0.000	0.000	0.000
50	A	56	LYS	1	0.956	1.011	23.563	11.090	11.090	0.000	0.000	0.000	0.000
51	A	57	LEU	0	-0.006	0.002	19.345	0.375	0.375	0.000	0.000	0.000	0.000
52	A	58	LYS	1	0.816	0.923	19.523	12.818	12.818	0.000	0.000	0.000	0.000
53	A	59	VAL	0	-0.034	-0.028	14.916	-0.168	-0.168	0.000	0.000	0.000	0.000
54	A	60	GLU	-1	-0.772	-0.840	13.788	-16.726	-16.726	0.000	0.000	0.000	0.000
55	A	61	VAL	0	-0.014	-0.009	8.876	-0.724	-0.724	0.000	0.000	0.000	0.000
56	A	62	TYR	0	0.018	-0.019	7.992	0.711	0.711	0.000	0.000	0.000	0.000
62	A	68	THR	0	-0.015	-0.044	6.774	4.644	4.644	0.000	0.000	0.000	0.000
63	A	69	PHE	0	-0.055	-0.033	6.022	2.355	2.355	0.000	0.000	0.000	0.000
64	A	70	GLU	-1	-0.909	-0.967	7.894	-27.631	-27.631	0.000	0.000	0.000	0.000
65	A	71	ARG	1	0.894	0.936	10.473	27.182	27.182	0.000	0.000	0.000	0.000
66	A	72	ILE	0	-0.063	-0.037	9.521	1.712	1.712	0.000	0.000	0.000	0.000
67	A	73	ASN	0	-0.060	-0.034	12.080	1.793	1.793	0.000	0.000	0.000	0.000
68	A	74	GLU	-1	-0.900	-0.931	13.866	-18.162	-18.162	0.000	0.000	0.000	0.000
69	A	75	ILE	0	-0.090	-0.023	15.347	1.327	1.327	0.000	0.000	0.000	0.000
70	A	76	GLU	-1	-0.834	-0.910	18.236	-12.777	-12.777	0.000	0.000	0.000	0.000
71	A	77	ILE	0	-0.045	-0.023	20.247	0.328	0.328	0.000	0.000	0.000	0.000
72	A	78	GLY	0	-0.006	-0.013	18.948	0.235	0.235	0.000	0.000	0.000	0.000
73	A	79	THR	0	0.021	0.003	19.915	-0.120	-0.120	0.000	0.000	0.000	0.000
74	A	80	GLY	0	-0.035	-0.010	22.773	0.295	0.295	0.000	0.000	0.000	0.000
75	A	81	TYR	0	-0.111	-0.074	19.630	0.316	0.316	0.000	0.000	0.000	0.000
76	A	82	ARG	1	0.944	0.974	19.201	13.090	13.090	0.000	0.000	0.000	0.000
77	A	83	LEU	0	-0.003	0.016	11.694	-0.049	-0.049	0.000	0.000	0.000	0.000
78	A	84	VAL	0	-0.026	-0.011	15.916	0.636	0.636	0.000	0.000	0.000	0.000
79	A	85	GLU	-1	-0.906	-0.953	12.910	-23.466	-23.466	0.000	0.000	0.000	0.000
80	A	86	VAL	0	-0.026	-0.012	13.858	1.544	1.544	0.000	0.000	0.000	0.000
81	A	87	SER	0	-0.026	-0.028	13.733	-1.679	-1.679	0.000	0.000	0.000	0.000
82	A	88	THR	0	0.006	0.004	11.678	0.632	0.632	0.000	0.000	0.000	0.000
83	A	89	LYS	1	0.845	0.904	14.008	15.853	15.853	0.000	0.000	0.000	0.000
84	A	90	PHE	0	0.005	-0.001	9.264	0.084	0.084	0.000	0.000	0.000	0.000
85	A	91	GLY	0	0.023	0.018	9.417	-2.438	-2.438	0.000	0.000	0.000	0.000
86	A	92	LYS	1	0.909	0.951	10.894	19.741	19.741	0.000	0.000	0.000	0.000
87	A	93	ALA	0	0.000	0.008	9.084	-3.235	-3.235	0.000	0.000	0.000	0.000
88	A	94	PHE	0	0.033	0.020	8.260	1.741	1.741	0.000	0.000	0.000	0.000
89	A	95	LEU	0	-0.010	-0.001	11.503	-0.171	-0.171	0.000	0.000	0.000	0.000
90	A	96	TRP	0	0.054	0.018	10.479	0.119	0.119	0.000	0.000	0.000	0.000
91	A	97	GLU	-1	-0.806	-0.853	16.903	-13.411	-13.411	0.000	0.000	0.000	0.000
92	A	98	TRP	0	-0.015	-0.018	20.369	-0.110	-0.110	0.000	0.000	0.000	0.000
93	A	99	GLY	0	-0.017	-0.014	23.496	0.197	0.197	0.000	0.000	0.000	0.000
94	A	100	SER	0	-0.015	-0.008	24.936	0.505	0.505	0.000	0.000	0.000	0.000
95	A	101	LYS	1	0.966	0.974	28.517	8.988	8.988	0.000	0.000	0.000	0.000
96	A	102	PRO	0	0.017	0.028	28.635	-0.119	-0.119	0.000	0.000	0.000	0.000
97	A	103	ARG	1	0.802	0.866	30.017	9.708	9.708	0.000	0.000	0.000	0.000
98	A	104	GLY	0	0.040	0.022	31.089	-0.250	-0.250	0.000	0.000	0.000	0.000
99	A	105	LYS	0	0.034	0.004	33.031	0.086	0.086	0.000	0.000	0.000	0.000
100	A	106	ARG	1	0.873	0.950	29.823	9.642	9.642	0.000	0.000	0.000	0.000
101	A	107	ILE	0	-0.008	0.001	26.688	0.247	0.247	0.000	0.000	0.000	0.000
102	A	108	LYS	1	0.822	0.899	29.136	9.105	9.105	0.000	0.000	0.000	0.000
103	A	109	SER	0	-0.033	-0.039	27.910	-0.226	-0.226	0.000	0.000	0.000	0.000
104	A	110	GLY	0	0.015	0.012	25.342	-0.210	-0.210	0.000	0.000	0.000	0.000
105	A	111	ASP	-1	-0.787	-0.898	23.373	-13.262	-13.262	0.000	0.000	0.000	0.000
106	A	112	PHE	0	0.008	0.003	21.894	0.348	0.348	0.000	0.000	0.000	0.000
107	A	113	ASP	-1	-0.768	-0.859	23.042	-12.418	-12.418	0.000	0.000	0.000	0.000
108	A	114	GLU	-1	-0.760	-0.862	25.806	-9.528	-9.528	0.000	0.000	0.000	0.000
109	A	115	ILE	0	0.048	0.022	28.179	0.277	0.277	0.000	0.000	0.000	0.000
110	A	116	ARG	1	0.833	0.895	24.003	11.839	11.839	0.000	0.000	0.000	0.000
111	A	117	LEU	0	-0.017	0.000	29.694	0.241	0.241	0.000	0.000	0.000	0.000
112	A	118	GLU	-1	-0.908	-0.950	32.262	-8.949	-8.949	0.000	0.000	0.000	0.000
113	A	119	HIS	0	-0.033	-0.006	31.858	0.111	0.111	0.000	0.000	0.000	0.000
114	A	120	HIS	0	-0.003	-0.012	33.238	0.028	0.028	0.000	0.000	0.000	0.000
115	A	121	HIS	0	0.000	-0.004	35.098	0.127	0.127	0.000	0.000	0.000	0.000
116	A	122	HIS	0	-0.065	-0.035	37.399	0.368	0.368	0.000	0.000	0.000	0.000
117	A	123	HIS	0	-0.030	-0.013	37.031	-0.039	-0.039	0.000	0.000	0.000	0.000
118	A	124	HIS	0	-0.067	-0.010	34.186	0.743	0.743	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:SER)