FMO DATABASE

FMODB ID: MLKZZ

Calculation Name: 6HPI-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6HPI

Chain ID: A

ChEMBL ID:

UniProt ID: Q9UHA7

Base Structure: SolutionNMR

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	158
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1531699.432496
FMO2-HF: Nuclear repulsion	1468674.4441
FMO2-HF: Total energy	-63024.988396
FMO2-MP2: Total energy	-63204.753407

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:MET)

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

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.
-44.294	-39.379	2.266	-3.243	-3.939	-0.029

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.806 / q_NPA : 0.900

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	LYS	1	0.803	0.899	2.648	36.221	39.164	1.366	-2.047	-2.262	-0.020
4	A	4	ALA	0	0.019	-0.004	3.948	0.532	0.824	0.001	-0.071	-0.222	0.000
50	A	50	ARG	1	0.862	0.922	2.471	49.890	51.388	0.899	-0.927	-1.470	-0.008
51	A	51	HIS	0	0.016	0.002	3.706	-20.103	-19.921	0.000	-0.198	0.015	-0.001
5	A	5	LEU	0	-0.042	-0.002	6.446	3.072	3.072	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.931	0.947	8.880	18.461	18.461	0.000	0.000	0.000	0.000
7	A	7	ILE	0	0.048	0.022	10.663	1.436	1.436	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.839	-0.884	6.230	-40.571	-40.571	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.012	0.011	9.362	0.032	0.032	0.000	0.000	0.000	0.000
10	A	10	PRO	0	-0.016	-0.008	11.600	0.718	0.718	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.001	0.001	13.393	1.510	1.510	0.000	0.000	0.000	0.000
12	A	12	GLN	0	-0.040	-0.039	17.049	0.397	0.397	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.015	0.014	19.979	0.332	0.332	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.037	-0.009	23.752	0.025	0.025	0.000	0.000	0.000	0.000
15	A	15	ILE	0	0.050	0.006	24.721	-0.334	-0.334	0.000	0.000	0.000	0.000
16	A	16	GLN	0	-0.012	0.014	28.036	0.160	0.160	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.838	-0.936	30.621	-9.982	-9.982	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.046	0.003	28.948	0.286	0.286	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.055	-0.047	33.203	0.464	0.464	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.053	0.022	35.633	0.128	0.128	0.000	0.000	0.000	0.000
21	A	21	ARG	1	0.780	0.906	33.725	8.615	8.615	0.000	0.000	0.000	0.000
22	A	22	VAL	0	0.019	0.007	32.906	-0.322	-0.322	0.000	0.000	0.000	0.000
23	A	23	TRP	0	0.014	0.010	28.603	0.260	0.260	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.014	-0.010	31.479	-0.085	-0.085	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.010	0.020	28.494	0.035	0.035	0.000	0.000	0.000	0.000
26	A	26	GLN	0	-0.046	-0.039	31.617	0.225	0.225	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.859	-0.938	35.032	-8.628	-8.628	0.000	0.000	0.000	0.000
28	A	28	GLN	0	-0.056	-0.031	31.498	-0.220	-0.220	0.000	0.000	0.000	0.000
29	A	29	THR	0	0.022	0.020	31.123	-0.324	-0.324	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.011	0.001	26.804	0.109	0.109	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.004	-0.012	31.198	0.127	0.127	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.021	0.031	34.025	-0.108	-0.108	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.053	-0.035	35.164	0.321	0.321	0.000	0.000	0.000	0.000
34	A	34	PRO	0	0.015	0.000	37.677	0.055	0.055	0.000	0.000	0.000	0.000
35	A	35	ARG	1	0.931	0.970	39.130	7.068	7.068	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.957	0.963	40.924	7.533	7.533	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.848	-0.914	41.264	-7.149	-7.149	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.854	0.928	40.428	7.605	7.605	0.000	0.000	0.000	0.000
39	A	39	MET	0	0.022	0.026	36.928	-0.204	-0.204	0.000	0.000	0.000	0.000
40	A	40	SER	0	0.004	-0.011	32.480	0.152	0.152	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.012	0.009	31.155	-0.112	-0.112	0.000	0.000	0.000	0.000
42	A	42	VAL	0	0.007	-0.003	27.295	-0.040	-0.040	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.006	0.014	22.598	0.115	0.115	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.035	-0.014	21.564	-0.131	-0.131	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.014	-0.003	17.317	-0.017	-0.017	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.005	-0.001	15.154	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.030	0.011	9.761	-0.193	-0.193	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.025	0.011	8.494	1.868	1.868	0.000	0.000	0.000	0.000
49	A	49	CYS	0	0.005	0.016	8.941	-0.973	-0.973	0.000	0.000	0.000	0.000
52	A	52	VAL	0	0.017	-0.005	5.701	4.704	4.704	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.854	-0.895	6.247	-41.066	-41.066	0.000	0.000	0.000	0.000
54	A	54	THR	0	-0.027	-0.018	8.443	3.871	3.871	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.072	-0.021	10.074	2.442	2.442	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.862	-0.940	12.828	-16.245	-16.245	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.820	0.903	11.678	23.698	23.698	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.888	-0.932	16.746	-15.215	-15.215	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.815	0.918	19.196	15.697	15.697	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.041	0.028	19.238	0.540	0.540	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.019	-0.021	14.602	-1.493	-1.493	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.014	0.004	12.610	0.719	0.719	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.042	-0.029	12.711	-2.319	-2.319	0.000	0.000	0.000	0.000
64	A	64	TYR	0	0.002	-0.030	13.461	0.967	0.967	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.024	0.011	14.967	-0.169	-0.169	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.010	-0.016	17.751	0.239	0.239	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.011	-0.003	19.769	0.224	0.224	0.000	0.000	0.000	0.000
68	A	68	ASN	0	-0.035	-0.014	20.166	-0.200	-0.200	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.029	-0.004	21.921	0.606	0.606	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.032	-0.022	24.750	0.039	0.039	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.002	0.005	20.161	-0.372	-0.372	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.065	0.047	22.418	0.185	0.185	0.000	0.000	0.000	0.000
73	A	73	CYS	0	-0.075	-0.010	18.730	-0.345	-0.345	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.009	0.008	19.557	0.655	0.655	0.000	0.000	0.000	0.000
75	A	75	MET	0	0.019	0.013	20.149	-0.876	-0.876	0.000	0.000	0.000	0.000
76	A	76	CYS	0	-0.031	-0.006	21.889	0.707	0.707	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.014	0.001	24.278	-0.121	-0.121	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.890	0.935	27.401	9.681	9.681	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.007	0.022	30.676	0.082	0.082	0.000	0.000	0.000	0.000
80	A	80	GLY	0	0.015	0.013	33.784	0.317	0.317	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.952	-0.968	35.500	-8.407	-8.407	0.000	0.000	0.000	0.000
82	A	82	GLN	0	0.024	-0.001	33.600	-0.265	-0.265	0.000	0.000	0.000	0.000
83	A	83	PRO	0	-0.002	-0.008	28.291	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	84	THR	0	-0.007	-0.006	28.843	0.240	0.240	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.004	-0.008	23.874	-0.460	-0.460	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.003	-0.006	25.969	0.294	0.294	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.012	0.006	23.548	-0.351	-0.351	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.813	0.905	25.263	11.473	11.473	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.825	-0.906	24.129	-11.486	-11.486	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.906	0.946	16.948	17.304	17.304	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.823	-0.900	16.127	-18.031	-18.031	0.000	0.000	0.000	0.000
92	A	92	ILE	0	0.015	-0.005	14.405	-0.784	-0.784	0.000	0.000	0.000	0.000
93	A	93	MET	0	-0.008	-0.004	9.704	-1.631	-1.631	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.910	-0.958	10.716	-24.453	-24.453	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.013	-0.018	10.779	-1.593	-1.593	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.080	-0.044	5.431	-4.037	-4.037	0.000	0.000	0.000	0.000
97	A	97	ASN	0	-0.028	-0.010	6.328	-8.873	-8.873	0.000	0.000	0.000	0.000
98	A	98	GLN	0	0.013	0.018	6.900	-4.937	-4.937	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.034	-0.013	6.021	-0.992	-0.992	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.900	-0.951	7.598	-19.367	-19.367	0.000	0.000	0.000	0.000
101	A	101	PRO	0	-0.021	-0.006	9.113	0.966	0.966	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.011	-0.007	11.347	1.451	1.451	0.000	0.000	0.000	0.000
103	A	103	LYS	1	1.005	0.991	15.117	18.940	18.940	0.000	0.000	0.000	0.000
104	A	104	SER	0	0.019	0.012	17.064	0.399	0.399	0.000	0.000	0.000	0.000
105	A	105	PHE	0	-0.013	-0.014	16.363	0.863	0.863	0.000	0.000	0.000	0.000
106	A	106	LEU	0	0.005	0.007	11.997	-0.055	-0.055	0.000	0.000	0.000	0.000
107	A	107	PHE	0	0.049	0.000	16.396	1.178	1.178	0.000	0.000	0.000	0.000
108	A	108	TYR	0	0.002	0.025	17.339	-1.214	-1.214	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.073	-0.028	15.489	1.000	1.000	0.000	0.000	0.000	0.000
110	A	110	SER	0	0.030	0.000	19.894	-0.304	-0.304	0.000	0.000	0.000	0.000
111	A	111	GLN	0	0.002	0.000	22.807	0.339	0.339	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.064	-0.027	25.612	0.197	0.197	0.000	0.000	0.000	0.000
113	A	113	GLY	0	0.027	0.029	29.088	0.389	0.389	0.000	0.000	0.000	0.000
114	A	114	ARG	1	0.906	0.930	28.698	9.959	9.959	0.000	0.000	0.000	0.000
115	A	115	ASN	0	0.002	0.026	28.614	-0.430	-0.430	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.015	-0.019	23.536	-0.336	-0.336	0.000	0.000	0.000	0.000
117	A	117	THR	0	0.038	0.018	24.477	0.331	0.331	0.000	0.000	0.000	0.000
118	A	118	PHE	0	0.016	-0.004	19.602	-0.718	-0.718	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.804	-0.891	22.244	-12.644	-12.644	0.000	0.000	0.000	0.000
120	A	120	SER	0	0.012	0.006	21.152	-0.714	-0.714	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.025	-0.012	16.328	0.186	0.186	0.000	0.000	0.000	0.000
122	A	122	ALA	0	-0.040	-0.027	19.585	0.181	0.181	0.000	0.000	0.000	0.000
123	A	123	PHE	0	-0.060	-0.021	21.338	0.486	0.486	0.000	0.000	0.000	0.000
124	A	124	PRO	0	0.033	0.013	23.350	0.082	0.082	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.004	0.005	25.236	0.432	0.432	0.000	0.000	0.000	0.000
126	A	126	TRP	0	-0.034	-0.016	27.098	0.312	0.312	0.000	0.000	0.000	0.000
127	A	127	PHE	0	0.028	-0.001	25.691	-0.640	-0.640	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.016	-0.011	22.479	0.411	0.411	0.000	0.000	0.000	0.000
129	A	129	ALA	0	-0.029	-0.008	27.055	0.132	0.132	0.000	0.000	0.000	0.000
130	A	130	VAL	0	0.005	-0.013	27.564	-0.063	-0.063	0.000	0.000	0.000	0.000
131	A	131	SER	0	-0.054	-0.043	30.179	0.168	0.168	0.000	0.000	0.000	0.000
132	A	132	SER	0	0.002	-0.024	32.719	0.156	0.156	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.884	-0.924	35.163	-8.037	-8.037	0.000	0.000	0.000	0.000
134	A	134	GLY	0	-0.025	-0.009	38.546	0.053	0.053	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.007	-0.014	38.094	0.047	0.047	0.000	0.000	0.000	0.000
136	A	136	CYS	0	-0.033	-0.005	36.405	0.215	0.215	0.000	0.000	0.000	0.000
137	A	137	PRO	0	0.075	0.026	33.869	-0.152	-0.152	0.000	0.000	0.000	0.000
138	A	138	LEU	0	-0.037	0.012	27.884	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	139	ILE	0	-0.036	-0.012	30.372	-0.058	-0.058	0.000	0.000	0.000	0.000
140	A	140	LEU	0	0.023	0.010	25.487	-0.309	-0.309	0.000	0.000	0.000	0.000
141	A	141	THR	0	-0.025	-0.028	29.541	0.421	0.421	0.000	0.000	0.000	0.000
142	A	142	GLN	0	-0.002	-0.009	30.616	-0.536	-0.536	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.905	-0.926	32.237	-8.603	-8.603	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.041	-0.021	34.146	0.117	0.117	0.000	0.000	0.000	0.000
145	A	145	GLY	0	0.028	0.020	37.669	0.029	0.029	0.000	0.000	0.000	0.000
146	A	146	LYS	1	0.890	0.935	38.375	8.360	8.360	0.000	0.000	0.000	0.000
147	A	147	ALA	0	0.043	0.030	39.827	0.084	0.084	0.000	0.000	0.000	0.000
148	A	148	ASN	0	0.001	-0.008	34.603	-0.084	-0.084	0.000	0.000	0.000	0.000
149	A	149	THR	0	0.038	0.014	32.901	0.001	0.001	0.000	0.000	0.000	0.000
150	A	150	THR	0	0.021	0.005	29.813	-0.075	-0.075	0.000	0.000	0.000	0.000
151	A	151	ASP	-1	-0.929	-0.955	28.743	-10.383	-10.383	0.000	0.000	0.000	0.000
152	A	152	PHE	0	0.004	-0.014	28.495	0.446	0.446	0.000	0.000	0.000	0.000
153	A	153	GLY	0	0.029	0.028	26.565	-0.411	-0.411	0.000	0.000	0.000	0.000
154	A	154	LEU	0	0.006	-0.014	21.252	0.013	0.013	0.000	0.000	0.000	0.000
155	A	155	THR	0	-0.036	-0.003	25.008	-0.090	-0.090	0.000	0.000	0.000	0.000
156	A	156	MET	0	-0.016	0.004	19.072	-0.114	-0.114	0.000	0.000	0.000	0.000
157	A	157	LEU	0	-0.006	-0.010	21.721	0.274	0.274	0.000	0.000	0.000	0.000
158	A	158	PHE	-1	-0.903	-0.946	17.464	-15.770	-15.770	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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