FMO DATABASE

FMODB ID: QMZYY

Calculation Name: 5HDK-D-Xray547

Preferred Name: Heat shock factor protein

Target Type: PROTEIN FAMILY

Ligand Name: potassium ion

Ligand 3-letter code: K

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5HDK

Chain ID: D

ChEMBL ID: CHEMBL3988631

UniProt ID: Q03933

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	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-912447.565553
FMO2-HF: Nuclear repulsion	867953.131276
FMO2-HF: Total energy	-44494.434277
FMO2-MP2: Total energy	-44626.63966

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:4:HIS)

Summations of interaction energy for fragment #1(A:4:HIS)

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.
-109.46	-103.459	27.102	-14.071	-19.03	-0.039

Interaction energy analysis for fragmet #1(A:4:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.893 / q_NPA : 0.963

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	6	HIS	0	0.060	0.037	3.847	5.970	7.728	-0.013	-0.781	-0.963	0.000
4	A	7	VAL	0	-0.010	0.010	2.533	4.247	5.982	0.536	-0.812	-1.460	-0.002
5	A	8	PRO	0	0.008	0.001	4.440	2.165	2.219	-0.001	-0.005	-0.048	0.000
9	A	12	SER	0	-0.016	-0.005	1.834	-15.710	-20.101	16.304	-6.427	-5.485	0.044
10	A	13	LYS	1	0.914	0.967	3.328	18.594	18.363	0.026	0.992	-0.787	-0.001
12	A	15	TRP	0	0.032	0.003	2.399	-10.330	-7.436	2.104	-1.851	-3.147	-0.025
13	A	16	THR	0	-0.013	-0.019	3.551	-0.722	-0.338	0.009	-0.125	-0.268	0.000
14	A	17	LEU	0	-0.052	-0.035	5.042	2.407	2.434	-0.001	-0.002	-0.024	0.000
98	A	101	ASP	-1	-0.889	-0.958	2.189	-90.721	-87.994	7.592	-4.701	-5.617	-0.055
99	A	102	ASP	-1	-0.903	-0.954	4.178	-41.772	-41.536	-0.001	-0.042	-0.193	0.000
101	A	104	LEU	0	-0.005	-0.005	2.833	2.863	3.671	0.547	-0.317	-1.038	0.000
6	A	9	ALA	0	0.062	0.014	6.028	-0.265	-0.265	0.000	0.000	0.000	0.000
7	A	10	PHE	0	-0.058	-0.030	7.108	0.643	0.643	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.067	0.027	6.266	0.724	0.724	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.021	0.000	6.138	0.453	0.453	0.000	0.000	0.000	0.000
15	A	18	VAL	0	-0.039	-0.022	7.588	1.815	1.815	0.000	0.000	0.000	0.000
16	A	19	GLU	-1	-0.803	-0.896	5.563	-29.424	-29.424	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.910	-0.943	8.608	-19.894	-19.894	0.000	0.000	0.000	0.000
18	A	21	THR	0	0.018	0.007	10.584	1.797	1.797	0.000	0.000	0.000	0.000
19	A	22	HIS	0	-0.049	-0.026	13.134	1.472	1.472	0.000	0.000	0.000	0.000
20	A	23	THR	0	0.019	-0.011	12.587	0.455	0.455	0.000	0.000	0.000	0.000
21	A	24	ASN	0	0.077	0.047	14.292	-0.193	-0.193	0.000	0.000	0.000	0.000
22	A	25	GLU	-1	-0.931	-0.962	16.193	-13.857	-13.857	0.000	0.000	0.000	0.000
23	A	26	PHE	0	-0.088	-0.049	16.991	0.661	0.661	0.000	0.000	0.000	0.000
24	A	27	ILE	0	-0.083	-0.055	11.985	0.296	0.296	0.000	0.000	0.000	0.000
25	A	28	THR	0	0.052	0.036	13.615	-0.585	-0.585	0.000	0.000	0.000	0.000
26	A	29	TRP	0	-0.013	-0.006	7.367	1.148	1.148	0.000	0.000	0.000	0.000
27	A	30	SER	0	-0.001	-0.009	13.576	0.897	0.897	0.000	0.000	0.000	0.000
28	A	31	GLN	0	0.015	-0.014	16.211	-0.439	-0.439	0.000	0.000	0.000	0.000
29	A	32	ASN	0	0.018	0.019	17.939	-0.559	-0.559	0.000	0.000	0.000	0.000
30	A	33	GLY	0	0.071	0.044	13.775	-0.365	-0.365	0.000	0.000	0.000	0.000
31	A	34	GLN	0	-0.051	-0.033	12.990	-1.478	-1.478	0.000	0.000	0.000	0.000
32	A	35	SER	0	-0.056	-0.037	14.372	-0.588	-0.588	0.000	0.000	0.000	0.000
33	A	36	PHE	0	0.019	0.007	11.860	-0.520	-0.520	0.000	0.000	0.000	0.000
34	A	37	LEU	0	0.015	0.002	14.021	0.748	0.748	0.000	0.000	0.000	0.000
35	A	38	VAL	0	-0.019	0.000	15.632	-0.622	-0.622	0.000	0.000	0.000	0.000
36	A	39	LEU	0	0.003	-0.006	17.665	0.657	0.657	0.000	0.000	0.000	0.000
37	A	40	ASP	-1	-0.791	-0.885	20.814	-10.351	-10.351	0.000	0.000	0.000	0.000
38	A	41	GLU	-1	-0.879	-0.955	20.866	-12.482	-12.482	0.000	0.000	0.000	0.000
39	A	42	GLN	0	-0.005	0.008	21.762	-0.165	-0.165	0.000	0.000	0.000	0.000
40	A	43	ARG	1	0.917	0.938	22.994	10.635	10.635	0.000	0.000	0.000	0.000
41	A	44	PHE	0	0.050	0.016	14.055	-0.264	-0.264	0.000	0.000	0.000	0.000
42	A	45	ALA	0	-0.025	-0.021	18.746	-0.474	-0.474	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.871	0.924	20.458	10.620	10.620	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.885	-0.942	20.796	-11.250	-11.250	0.000	0.000	0.000	0.000
45	A	48	ILE	0	-0.008	0.012	14.355	-0.461	-0.461	0.000	0.000	0.000	0.000
46	A	49	LEU	0	-0.040	-0.003	14.832	-0.806	-0.806	0.000	0.000	0.000	0.000
47	A	50	PRO	0	0.023	0.011	16.255	-0.611	-0.611	0.000	0.000	0.000	0.000
48	A	51	LYS	1	0.896	0.968	14.030	17.035	17.035	0.000	0.000	0.000	0.000
49	A	52	TYR	0	0.033	0.018	10.132	-0.639	-0.639	0.000	0.000	0.000	0.000
50	A	53	PHE	0	-0.072	-0.061	9.453	-1.071	-1.071	0.000	0.000	0.000	0.000
51	A	54	LYS	1	0.849	0.934	14.407	16.906	16.906	0.000	0.000	0.000	0.000
52	A	55	HIS	0	0.017	0.024	16.482	1.148	1.148	0.000	0.000	0.000	0.000
53	A	56	ASN	0	0.050	0.019	19.140	-0.473	-0.473	0.000	0.000	0.000	0.000
54	A	57	ASN	0	0.036	0.020	20.576	0.290	0.290	0.000	0.000	0.000	0.000
55	A	58	MET	0	0.080	0.035	17.730	-0.812	-0.812	0.000	0.000	0.000	0.000
56	A	59	ALA	0	0.043	0.026	19.484	-0.457	-0.457	0.000	0.000	0.000	0.000
57	A	60	SER	0	-0.037	-0.027	19.144	-0.183	-0.183	0.000	0.000	0.000	0.000
58	A	61	PHE	0	0.017	0.004	11.793	-0.597	-0.597	0.000	0.000	0.000	0.000
59	A	62	VAL	0	0.048	0.016	15.574	-0.766	-0.766	0.000	0.000	0.000	0.000
60	A	63	ARG	1	0.935	0.974	17.882	13.530	13.530	0.000	0.000	0.000	0.000
61	A	64	GLN	0	-0.016	-0.012	13.595	0.718	0.718	0.000	0.000	0.000	0.000
62	A	65	LEU	0	0.044	0.029	12.124	-0.864	-0.864	0.000	0.000	0.000	0.000
63	A	66	ASN	0	0.002	0.004	14.564	-0.414	-0.414	0.000	0.000	0.000	0.000
64	A	67	MET	0	-0.045	-0.012	16.018	-0.132	-0.132	0.000	0.000	0.000	0.000
65	A	68	TYR	0	0.026	0.013	11.214	-0.195	-0.195	0.000	0.000	0.000	0.000
66	A	69	GLY	0	-0.037	-0.011	14.277	-0.512	-0.512	0.000	0.000	0.000	0.000
67	A	70	PHE	0	-0.016	-0.011	9.405	0.405	0.405	0.000	0.000	0.000	0.000
68	A	71	ARG	1	0.893	0.954	15.636	15.124	15.124	0.000	0.000	0.000	0.000
69	A	72	LYS	1	0.971	0.989	17.706	11.600	11.600	0.000	0.000	0.000	0.000
70	A	73	VAL	0	-0.012	-0.004	19.009	0.183	0.183	0.000	0.000	0.000	0.000
71	A	74	VAL	0	-0.023	-0.018	21.654	0.093	0.093	0.000	0.000	0.000	0.000
72	A	75	HIS	0	0.029	0.015	25.292	0.141	0.141	0.000	0.000	0.000	0.000
73	A	76	ILE	0	0.008	0.004	28.287	0.064	0.064	0.000	0.000	0.000	0.000
74	A	77	ASP	-1	-0.859	-0.939	31.431	-8.910	-8.910	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.040	-0.024	34.148	0.256	0.256	0.000	0.000	0.000	0.000
76	A	79	GLY	0	0.000	-0.004	37.039	0.052	0.052	0.000	0.000	0.000	0.000
77	A	80	ILE	0	-0.048	-0.014	35.037	0.178	0.178	0.000	0.000	0.000	0.000
78	A	81	VAL	0	0.020	0.007	38.145	-0.108	-0.108	0.000	0.000	0.000	0.000
79	A	82	LYS	1	0.857	0.943	30.698	9.202	9.202	0.000	0.000	0.000	0.000
80	A	83	GLN	0	0.028	0.010	34.561	-0.024	-0.024	0.000	0.000	0.000	0.000
81	A	84	GLU	-1	-0.919	-0.958	30.754	-8.853	-8.853	0.000	0.000	0.000	0.000
82	A	85	ARG	1	0.901	0.949	30.454	9.063	9.063	0.000	0.000	0.000	0.000
83	A	86	ASP	-1	-0.894	-0.941	27.740	-9.869	-9.869	0.000	0.000	0.000	0.000
84	A	87	GLY	0	-0.042	-0.032	26.263	0.307	0.307	0.000	0.000	0.000	0.000
85	A	88	PRO	0	-0.020	-0.002	21.774	-0.231	-0.231	0.000	0.000	0.000	0.000
86	A	89	VAL	0	-0.027	-0.004	19.077	0.285	0.285	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.829	-0.877	17.994	-14.577	-14.577	0.000	0.000	0.000	0.000
88	A	91	PHE	0	-0.020	-0.026	14.801	0.587	0.587	0.000	0.000	0.000	0.000
89	A	92	GLN	0	0.030	0.003	14.364	-0.943	-0.943	0.000	0.000	0.000	0.000
90	A	93	HIS	0	0.024	0.018	11.987	0.186	0.186	0.000	0.000	0.000	0.000
91	A	94	PRO	0	-0.011	-0.005	13.301	-0.626	-0.626	0.000	0.000	0.000	0.000
92	A	95	TYR	0	0.035	0.006	10.919	0.415	0.415	0.000	0.000	0.000	0.000
93	A	96	PHE	0	-0.034	-0.010	6.251	-3.133	-3.133	0.000	0.000	0.000	0.000
94	A	97	LYS	1	0.830	0.914	8.611	23.021	23.021	0.000	0.000	0.000	0.000
95	A	98	GLN	0	0.046	0.027	8.260	-2.176	-2.176	0.000	0.000	0.000	0.000
96	A	99	GLY	0	-0.031	-0.021	7.401	1.205	1.205	0.000	0.000	0.000	0.000
97	A	100	GLN	0	-0.044	-0.018	7.145	0.675	0.675	0.000	0.000	0.000	0.000
100	A	103	LEU	0	0.018	0.015	6.482	3.043	3.043	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.946	-0.960	5.503	-36.231	-36.231	0.000	0.000	0.000	0.000
103	A	106	ASN	0	-0.053	-0.024	7.111	5.449	5.449	0.000	0.000	0.000	0.000
104	A	107	ILE	0	-0.070	-0.024	7.850	3.128	3.128	0.000	0.000	0.000	0.000
105	A	108	LYS	1	0.878	0.934	10.128	25.652	25.652	0.000	0.000	0.000	0.000
106	A	109	ARG	1	0.886	0.930	12.851	17.267	17.267	0.000	0.000	0.000	0.000
107	A	110	LYS	1	0.887	0.937	14.549	15.257	15.257	0.000	0.000	0.000	0.000
108	A	111	VAL	-1	-0.903	-0.937	18.328	-13.488	-13.488	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:HIS)