FMO DATABASE

FMODB ID: KGRY3

Calculation Name: 4K2E-A-Xray372

Preferred Name:

Target Type:

Ligand Name: s-hydroxycysteine

ligand 3-letter code: CSO

PDB ID: 4K2E

Chain ID: A

ChEMBL ID:

UniProt ID: P52695

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	95
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-687351.75823
FMO2-HF: Nuclear repulsion	648368.408264
FMO2-HF: Total energy	-38983.349966
FMO2-MP2: Total energy	-39094.077618

3D Structure

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:11:LEU)

Summations of interaction energy for fragment #1(A:11:LEU)

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.
-15.917	-12.797	14.698	-7.966	-9.852	-0.061

Interaction energy analysis for fragmet #1(A:11:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.015 / q_NPA : 0.016

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

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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	13	GLU	-1	-0.854	-0.913	1.901	-14.991	-16.817	12.305	-5.501	-4.978	-0.047
4	A	14	MET	0	0.017	0.000	2.494	0.453	1.896	1.451	-0.716	-2.178	0.001
5	A	15	GLU	-1	-0.851	-0.902	2.662	-6.231	-2.837	0.943	-1.742	-2.594	-0.015
6	A	16	LYS	1	0.892	0.948	4.979	2.372	2.481	-0.001	-0.007	-0.102	0.000
7	A	17	ASN	0	-0.029	-0.021	7.697	0.504	0.504	0.000	0.000	0.000	0.000
8	A	18	SER	0	-0.032	-0.036	6.100	0.390	0.390	0.000	0.000	0.000	0.000
9	A	19	ALA	0	0.032	0.019	8.750	0.230	0.230	0.000	0.000	0.000	0.000
10	A	20	LYS	1	0.918	0.948	10.647	0.613	0.613	0.000	0.000	0.000	0.000
11	A	21	ALA	0	0.011	0.007	11.601	0.096	0.096	0.000	0.000	0.000	0.000
12	A	22	VAL	0	0.028	0.004	10.702	0.098	0.098	0.000	0.000	0.000	0.000
13	A	23	VAL	0	-0.025	-0.005	13.553	0.061	0.061	0.000	0.000	0.000	0.000
14	A	24	LEU	0	0.020	0.012	16.548	0.045	0.045	0.000	0.000	0.000	0.000
15	A	25	LEU	0	0.046	0.011	14.059	0.039	0.039	0.000	0.000	0.000	0.000
16	A	26	LYS	1	0.943	0.972	14.541	0.362	0.362	0.000	0.000	0.000	0.000
17	A	27	ALA	0	-0.018	0.009	18.991	0.028	0.028	0.000	0.000	0.000	0.000
18	A	28	MET	0	0.007	0.002	20.945	0.015	0.015	0.000	0.000	0.000	0.000
19	A	29	ALA	0	-0.018	0.013	20.045	0.019	0.019	0.000	0.000	0.000	0.000
20	A	30	ASN	0	-0.055	-0.052	22.166	0.007	0.007	0.000	0.000	0.000	0.000
21	A	31	GLU	-1	-0.842	-0.913	25.776	-0.048	-0.048	0.000	0.000	0.000	0.000
22	A	32	ARG	1	0.856	0.924	28.844	0.056	0.056	0.000	0.000	0.000	0.000
23	A	33	ARG	1	0.849	0.916	23.117	0.145	0.145	0.000	0.000	0.000	0.000
24	A	34	LEU	0	0.040	0.020	25.283	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	35	GLN	0	0.049	0.021	27.722	0.000	0.000	0.000	0.000	0.000	0.000
26	A	36	ILE	0	-0.016	-0.011	30.675	0.001	0.001	0.000	0.000	0.000	0.000
27	A	37	LEU	0	-0.022	-0.021	25.330	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	38	CSO	0	0.019	-0.001	28.918	0.001	0.001	0.000	0.000	0.000	0.000
29	A	39	MET	0	-0.035	-0.005	30.819	0.005	0.005	0.000	0.000	0.000	0.000
30	A	40	LEU	0	-0.044	-0.021	31.738	0.001	0.001	0.000	0.000	0.000	0.000
31	A	41	LEU	0	0.001	0.005	29.623	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	42	ASP	-1	-0.943	-0.955	32.222	-0.079	-0.079	0.000	0.000	0.000	0.000
33	A	43	ASN	0	-0.056	-0.033	34.628	0.008	0.008	0.000	0.000	0.000	0.000
34	A	44	GLU	-1	-0.854	-0.906	35.627	-0.094	-0.094	0.000	0.000	0.000	0.000
35	A	45	LEU	0	0.012	0.021	36.980	0.005	0.005	0.000	0.000	0.000	0.000
36	A	46	SER	0	0.029	0.010	38.682	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	47	VAL	0	-0.003	-0.012	38.057	0.001	0.001	0.000	0.000	0.000	0.000
38	A	48	GLY	0	0.010	0.004	39.914	0.002	0.002	0.000	0.000	0.000	0.000
39	A	49	GLU	-1	-0.807	-0.882	41.259	-0.053	-0.053	0.000	0.000	0.000	0.000
40	A	50	LEU	0	0.022	-0.004	35.011	0.002	0.002	0.000	0.000	0.000	0.000
41	A	51	SER	0	-0.104	-0.073	38.705	0.002	0.002	0.000	0.000	0.000	0.000
42	A	52	SER	0	0.003	-0.017	40.512	0.003	0.003	0.000	0.000	0.000	0.000
43	A	53	ARG	1	0.849	0.913	39.651	0.051	0.051	0.000	0.000	0.000	0.000
44	A	54	LEU	0	-0.024	0.000	33.711	0.001	0.001	0.000	0.000	0.000	0.000
45	A	55	GLU	-1	-0.908	-0.930	38.049	-0.034	-0.034	0.000	0.000	0.000	0.000
46	A	56	LEU	0	-0.046	-0.013	34.891	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	57	SER	0	0.051	0.038	39.639	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	58	GLN	0	0.064	0.006	39.697	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	59	SER	0	-0.017	0.004	39.214	-0.006	-0.006	0.000	0.000	0.000	0.000
50	A	60	ALA	0	0.061	0.044	36.821	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	61	LEU	0	0.008	0.012	34.581	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	62	SER	0	-0.040	-0.033	34.406	-0.009	-0.009	0.000	0.000	0.000	0.000
53	A	63	GLN	0	0.014	0.000	31.711	-0.005	-0.005	0.000	0.000	0.000	0.000
54	A	64	HIS	0	0.018	0.010	29.583	-0.017	-0.017	0.000	0.000	0.000	0.000
55	A	65	LEU	0	0.028	0.009	29.716	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	66	ALA	0	-0.041	-0.027	30.922	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	67	TRP	0	-0.020	-0.012	22.277	-0.001	-0.001	0.000	0.000	0.000	0.000
58	A	68	LEU	0	0.010	0.003	25.564	-0.017	-0.017	0.000	0.000	0.000	0.000
59	A	69	ARG	1	0.925	0.973	27.041	0.119	0.119	0.000	0.000	0.000	0.000
60	A	70	ARG	1	0.800	0.890	23.477	0.197	0.197	0.000	0.000	0.000	0.000
61	A	71	ASP	-1	-0.814	-0.892	21.876	-0.255	-0.255	0.000	0.000	0.000	0.000
62	A	72	GLY	0	0.024	0.019	22.549	-0.020	-0.020	0.000	0.000	0.000	0.000
63	A	73	LEU	0	-0.047	0.011	21.483	0.000	0.000	0.000	0.000	0.000	0.000
64	A	74	VAL	0	-0.031	-0.016	25.339	0.014	0.014	0.000	0.000	0.000	0.000
65	A	75	ASN	0	0.025	0.016	29.191	-0.016	-0.016	0.000	0.000	0.000	0.000
66	A	76	THR	0	-0.019	-0.026	31.928	0.006	0.006	0.000	0.000	0.000	0.000
67	A	77	ARG	1	0.762	0.850	35.453	0.078	0.078	0.000	0.000	0.000	0.000
68	A	78	LYS	1	0.825	0.906	39.101	0.077	0.077	0.000	0.000	0.000	0.000
69	A	79	GLU	-1	-0.821	-0.896	42.547	-0.068	-0.068	0.000	0.000	0.000	0.000
70	A	80	ALA	0	0.040	0.011	45.841	0.002	0.002	0.000	0.000	0.000	0.000
71	A	81	GLN	0	0.057	0.018	47.317	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	82	THR	0	0.005	0.030	43.238	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	83	VAL	0	-0.035	-0.010	38.571	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	84	PHE	0	0.052	0.014	39.448	0.003	0.003	0.000	0.000	0.000	0.000
75	A	85	TYR	0	0.012	-0.001	33.015	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	86	THR	0	0.091	0.043	33.634	0.003	0.003	0.000	0.000	0.000	0.000
77	A	87	LEU	0	0.025	0.027	27.817	-0.011	-0.011	0.000	0.000	0.000	0.000
78	A	88	SER	0	-0.024	-0.036	26.042	0.004	0.004	0.000	0.000	0.000	0.000
79	A	89	SER	0	-0.039	-0.042	22.344	0.012	0.012	0.000	0.000	0.000	0.000
80	A	90	THR	0	0.049	0.008	23.103	0.016	0.016	0.000	0.000	0.000	0.000
81	A	91	GLU	-1	-0.805	-0.872	18.554	-0.311	-0.311	0.000	0.000	0.000	0.000
82	A	92	VAL	0	-0.003	0.003	21.387	0.016	0.016	0.000	0.000	0.000	0.000
83	A	93	LYS	1	0.880	0.945	23.310	0.160	0.160	0.000	0.000	0.000	0.000
84	A	94	ALA	0	0.053	0.028	22.535	0.013	0.013	0.000	0.000	0.000	0.000
85	A	95	MET	0	-0.019	-0.010	17.905	0.023	0.023	0.000	0.000	0.000	0.000
86	A	96	ILE	0	-0.008	-0.009	22.552	0.018	0.018	0.000	0.000	0.000	0.000
87	A	97	GLU	-1	-0.798	-0.870	25.985	-0.069	-0.069	0.000	0.000	0.000	0.000
88	A	98	LEU	0	-0.031	-0.015	21.334	0.013	0.013	0.000	0.000	0.000	0.000
89	A	99	LEU	0	-0.012	-0.020	22.579	0.013	0.013	0.000	0.000	0.000	0.000
90	A	100	HIS	0	0.035	0.004	25.952	0.008	0.008	0.000	0.000	0.000	0.000
91	A	101	ARG	1	0.816	0.880	25.727	0.060	0.060	0.000	0.000	0.000	0.000
92	A	102	LEU	0	-0.064	-0.027	23.625	0.009	0.009	0.000	0.000	0.000	0.000
93	A	103	TYR	0	-0.052	-0.027	24.857	0.006	0.006	0.000	0.000	0.000	0.000
94	A	104	CYS	0	-0.059	-0.010	30.453	0.001	0.001	0.000	0.000	0.000	0.000
95	A	105	GLN	0	-0.014	0.013	32.310	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:11:LEU)