FMO DATABASE

FMODB ID: 89QGY

Calculation Name: 2PN0-A-Xray372

Preferred Name:

Target Type:

Ligand Name: cysteinesulfonic acid

ligand 3-letter code: OCS

PDB ID: 2PN0

Chain ID: A

ChEMBL ID:

UniProt ID: Q82T10

Base Structure: X-ray

Registration Date: 2023-09-23

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

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
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	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge	OCS=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-984765.651601
FMO2-HF: Nuclear repulsion	937250.583718
FMO2-HF: Total energy	-47515.067884
FMO2-MP2: Total energy	-47654.337369

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:4:LYS)

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

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.
-133.005	-129.76	0.527	-1.195	-2.577	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.977 / q_NPA : 0.978

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	6	LYS	1	0.916	0.971	3.561	51.678	53.329	0.007	-0.545	-1.113	-0.001
4	A	7	ILE	0	0.099	0.075	6.310	-0.091	-0.091	0.000	0.000	0.000	0.000
5	A	8	MET	0	-0.010	-0.001	8.974	-0.528	-0.528	0.000	0.000	0.000	0.000
6	A	9	ILE	0	0.019	0.020	12.571	1.122	1.122	0.000	0.000	0.000	0.000
7	A	10	SER	0	0.014	0.018	15.465	-0.132	-0.132	0.000	0.000	0.000	0.000
8	A	11	SER	0	0.058	0.001	18.794	-0.225	-0.225	0.000	0.000	0.000	0.000
9	A	12	LEU	0	-0.027	-0.001	20.585	0.220	0.220	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.799	-0.922	18.969	-13.229	-13.229	0.000	0.000	0.000	0.000
11	A	14	ALA	0	0.017	0.021	17.173	0.049	0.049	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.937	-0.956	18.410	-11.982	-11.982	0.000	0.000	0.000	0.000
13	A	16	ARG	1	0.840	0.920	21.804	11.819	11.819	0.000	0.000	0.000	0.000
14	A	17	LEU	0	-0.017	-0.016	16.786	0.486	0.486	0.000	0.000	0.000	0.000
15	A	18	GLU	-1	-0.881	-0.922	18.856	-14.587	-14.587	0.000	0.000	0.000	0.000
16	A	19	ILE	0	0.029	0.015	20.515	0.490	0.490	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.076	-0.035	21.717	0.547	0.547	0.000	0.000	0.000	0.000
18	A	21	LEU	0	0.007	-0.006	17.419	0.467	0.467	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.909	-0.940	21.930	-11.983	-11.983	0.000	0.000	0.000	0.000
20	A	23	THR	0	-0.091	-0.056	24.291	0.579	0.579	0.000	0.000	0.000	0.000
21	A	24	LEU	0	-0.070	-0.026	24.251	0.431	0.431	0.000	0.000	0.000	0.000
22	A	25	SER	0	0.028	0.033	24.301	-0.075	-0.075	0.000	0.000	0.000	0.000
23	A	26	GLN	0	-0.035	-0.021	24.595	-0.144	-0.144	0.000	0.000	0.000	0.000
24	A	27	ASN	0	-0.066	-0.039	25.245	0.222	0.222	0.000	0.000	0.000	0.000
25	A	28	ALA	0	0.038	0.027	22.433	-0.421	-0.421	0.000	0.000	0.000	0.000
26	A	29	PHE	0	-0.008	0.002	17.977	0.355	0.355	0.000	0.000	0.000	0.000
27	A	30	PRO	0	-0.008	-0.022	19.535	-0.389	-0.389	0.000	0.000	0.000	0.000
28	A	31	GLY	0	0.050	0.025	15.407	-0.023	-0.023	0.000	0.000	0.000	0.000
29	A	32	ARG	1	0.757	0.871	14.816	12.238	12.238	0.000	0.000	0.000	0.000
30	A	33	ASP	-1	-0.876	-0.937	14.467	-15.354	-15.354	0.000	0.000	0.000	0.000
31	A	34	ASP	-1	-0.961	-0.990	10.806	-18.895	-18.895	0.000	0.000	0.000	0.000
32	A	35	LEU	0	0.023	0.014	10.574	-1.097	-1.097	0.000	0.000	0.000	0.000
33	A	36	GLU	-1	-0.846	-0.929	12.476	-15.567	-15.567	0.000	0.000	0.000	0.000
34	A	37	ALA	0	-0.043	-0.015	9.222	-0.932	-0.932	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.973	-1.002	7.997	-24.320	-24.320	0.000	0.000	0.000	0.000
36	A	39	LEU	0	0.006	-0.013	9.030	-1.163	-1.163	0.000	0.000	0.000	0.000
37	A	40	ALA	0	-0.017	0.007	11.387	-0.360	-0.360	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.764	0.874	2.715	42.785	44.379	0.520	-0.650	-1.464	0.001
39	A	42	ALA	0	0.012	0.003	8.410	-3.844	-3.844	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-1.012	-1.007	9.171	-28.969	-28.969	0.000	0.000	0.000	0.000
41	A	44	VAL	0	-0.008	-0.003	11.427	1.144	1.144	0.000	0.000	0.000	0.000
42	A	45	VAL	0	-0.002	0.004	14.096	0.240	0.240	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.856	-0.955	16.843	-12.711	-12.711	0.000	0.000	0.000	0.000
44	A	47	PRO	0	-0.042	-0.054	19.525	-0.579	-0.579	0.000	0.000	0.000	0.000
45	A	48	GLU	-1	-0.957	-0.963	21.093	-12.448	-12.448	0.000	0.000	0.000	0.000
46	A	49	GLU	-1	-0.995	-0.978	17.394	-15.382	-15.382	0.000	0.000	0.000	0.000
47	A	50	ILE	0	-0.052	-0.025	15.966	-1.396	-1.396	0.000	0.000	0.000	0.000
48	A	51	PRO	0	-0.012	-0.008	14.891	0.925	0.925	0.000	0.000	0.000	0.000
49	A	52	PRO	0	0.030	0.004	18.009	-0.100	-0.100	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.018	-0.009	16.858	0.326	0.326	0.000	0.000	0.000	0.000
51	A	54	VAL	0	0.012	0.012	13.745	-0.421	-0.421	0.000	0.000	0.000	0.000
52	A	55	VAL	0	-0.019	0.000	15.257	0.998	0.998	0.000	0.000	0.000	0.000
53	A	56	THR	0	0.040	0.019	15.553	-0.673	-0.673	0.000	0.000	0.000	0.000
54	A	57	MET	0	-0.017	-0.020	18.003	0.361	0.361	0.000	0.000	0.000	0.000
55	A	58	ASN	0	-0.077	-0.053	20.374	0.356	0.356	0.000	0.000	0.000	0.000
56	A	59	SER	0	0.019	0.036	20.214	0.236	0.236	0.000	0.000	0.000	0.000
57	A	60	THR	0	-0.026	-0.039	22.317	0.067	0.067	0.000	0.000	0.000	0.000
58	A	61	VAL	0	-0.029	-0.017	19.174	-0.277	-0.277	0.000	0.000	0.000	0.000
59	A	62	ARG	1	0.994	1.001	22.194	10.376	10.376	0.000	0.000	0.000	0.000
60	A	63	PHE	0	0.019	-0.013	18.914	-0.575	-0.575	0.000	0.000	0.000	0.000
61	A	64	ARG	1	0.914	0.970	23.384	11.174	11.174	0.000	0.000	0.000	0.000
62	A	65	VAL	0	-0.065	-0.011	23.867	-0.522	-0.522	0.000	0.000	0.000	0.000
63	A	66	GLU	-1	-0.933	-0.986	23.285	-11.240	-11.240	0.000	0.000	0.000	0.000
64	A	67	SER	0	-0.047	-0.034	25.684	0.236	0.236	0.000	0.000	0.000	0.000
65	A	68	SER	0	-0.104	-0.138	28.928	0.239	0.239	0.000	0.000	0.000	0.000
66	A	69	ALA	0	-0.035	-0.010	28.894	0.211	0.211	0.000	0.000	0.000	0.000
67	A	70	GLU	-1	-0.828	-0.831	29.231	-8.960	-8.960	0.000	0.000	0.000	0.000
68	A	71	GLU	-1	-0.925	-0.995	27.804	-10.355	-10.355	0.000	0.000	0.000	0.000
69	A	72	PHE	0	-0.073	-0.029	23.930	0.347	0.347	0.000	0.000	0.000	0.000
70	A	73	OCS	-1	-0.859	-0.918	25.690	-10.535	-10.535	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.034	-0.015	22.333	0.185	0.185	0.000	0.000	0.000	0.000
72	A	75	THR	0	0.016	0.025	23.398	-0.412	-0.412	0.000	0.000	0.000	0.000
73	A	76	LEU	0	-0.028	0.006	17.668	0.314	0.314	0.000	0.000	0.000	0.000
74	A	77	VAL	0	0.016	0.013	21.925	0.012	0.012	0.000	0.000	0.000	0.000
75	A	78	TYR	0	0.018	-0.035	21.879	-0.123	-0.123	0.000	0.000	0.000	0.000
76	A	79	PRO	0	0.030	0.002	23.998	0.314	0.314	0.000	0.000	0.000	0.000
77	A	80	LYS	1	0.816	0.905	26.930	10.411	10.411	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.834	-0.913	27.967	-9.475	-9.475	0.000	0.000	0.000	0.000
79	A	82	VAL	0	-0.043	-0.002	26.746	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	83	ASP	-1	-0.788	-0.876	29.359	-8.580	-8.580	0.000	0.000	0.000	0.000
81	A	84	THR	0	-0.076	-0.059	31.913	-0.121	-0.121	0.000	0.000	0.000	0.000
82	A	85	SER	0	-0.064	-0.053	32.202	0.075	0.075	0.000	0.000	0.000	0.000
83	A	86	GLY	0	-0.008	-0.006	30.218	0.103	0.103	0.000	0.000	0.000	0.000
84	A	87	GLU	-1	-0.851	-0.926	27.680	-10.209	-10.209	0.000	0.000	0.000	0.000
85	A	88	LYS	1	0.913	1.000	26.622	9.097	9.097	0.000	0.000	0.000	0.000
86	A	89	ILE	0	-0.009	-0.004	21.444	0.131	0.131	0.000	0.000	0.000	0.000
87	A	90	SER	0	0.001	0.003	22.943	-0.413	-0.413	0.000	0.000	0.000	0.000
88	A	91	ILE	0	0.060	0.026	16.255	-0.073	-0.073	0.000	0.000	0.000	0.000
89	A	92	LEU	0	-0.021	-0.022	18.757	-0.365	-0.365	0.000	0.000	0.000	0.000
90	A	93	ALA	0	-0.042	-0.006	21.145	0.152	0.152	0.000	0.000	0.000	0.000
91	A	94	PRO	0	0.012	-0.006	19.298	-0.485	-0.485	0.000	0.000	0.000	0.000
92	A	95	VAL	0	0.014	0.016	17.603	0.415	0.415	0.000	0.000	0.000	0.000
93	A	96	GLY	0	0.062	0.025	17.113	-0.543	-0.543	0.000	0.000	0.000	0.000
94	A	97	SER	0	-0.047	-0.035	15.851	-0.514	-0.514	0.000	0.000	0.000	0.000
95	A	98	ALA	0	-0.011	-0.001	12.907	-0.705	-0.705	0.000	0.000	0.000	0.000
96	A	99	LEU	0	-0.023	-0.019	12.908	-0.649	-0.649	0.000	0.000	0.000	0.000
97	A	100	LEU	0	0.002	0.000	13.701	-0.114	-0.114	0.000	0.000	0.000	0.000
98	A	101	GLY	0	0.000	0.000	11.095	-0.872	-0.872	0.000	0.000	0.000	0.000
99	A	102	LEU	0	-0.047	-0.003	10.428	-1.283	-1.283	0.000	0.000	0.000	0.000
100	A	103	ALA	0	0.008	-0.005	12.370	0.557	0.557	0.000	0.000	0.000	0.000
101	A	104	GLN	0	-0.063	-0.051	14.434	-0.056	-0.056	0.000	0.000	0.000	0.000
102	A	105	GLY	0	-0.063	-0.026	16.603	-0.571	-0.571	0.000	0.000	0.000	0.000
103	A	106	ASP	-1	-0.844	-0.907	12.050	-20.310	-20.310	0.000	0.000	0.000	0.000
104	A	107	GLU	-1	-0.887	-0.960	14.600	-13.011	-13.011	0.000	0.000	0.000	0.000
105	A	108	ILE	0	-0.020	0.004	13.822	-0.791	-0.791	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.900	-0.962	16.330	-12.713	-12.713	0.000	0.000	0.000	0.000
107	A	110	TRP	0	0.019	0.007	18.477	-0.396	-0.396	0.000	0.000	0.000	0.000
108	A	111	PRO	0	0.009	-0.001	21.114	0.305	0.305	0.000	0.000	0.000	0.000
109	A	112	LYS	1	0.947	0.991	24.369	9.537	9.537	0.000	0.000	0.000	0.000
110	A	113	PRO	0	0.024	0.000	27.658	0.109	0.109	0.000	0.000	0.000	0.000
111	A	114	GLY	0	-0.028	-0.008	30.728	0.129	0.129	0.000	0.000	0.000	0.000
112	A	115	GLY	0	-0.010	0.002	29.214	0.130	0.130	0.000	0.000	0.000	0.000
113	A	116	GLY	0	-0.010	-0.012	27.223	0.130	0.130	0.000	0.000	0.000	0.000
114	A	117	VAL	0	0.001	0.000	21.800	0.025	0.025	0.000	0.000	0.000	0.000
115	A	118	LEU	0	-0.024	-0.009	23.787	0.338	0.338	0.000	0.000	0.000	0.000
116	A	119	ARG	1	0.916	0.967	15.984	14.020	14.020	0.000	0.000	0.000	0.000
117	A	120	VAL	0	-0.003	-0.008	19.767	0.495	0.495	0.000	0.000	0.000	0.000
118	A	121	ARG	1	0.841	0.925	19.079	12.507	12.507	0.000	0.000	0.000	0.000
119	A	122	ILE	0	0.028	0.028	15.964	0.759	0.759	0.000	0.000	0.000	0.000
120	A	123	VAL	0	-0.093	-0.053	19.792	-0.322	-0.322	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.951	-0.987	22.536	-10.824	-10.824	0.000	0.000	0.000	0.000
122	A	125	VAL	0	0.008	0.016	18.390	0.020	0.020	0.000	0.000	0.000	0.000
123	A	126	THR	0	-0.001	0.010	21.852	0.256	0.256	0.000	0.000	0.000	0.000
124	A	127	TYR	0	0.018	0.022	23.343	0.165	0.165	0.000	0.000	0.000	0.000

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