FMO DATABASE

FMODB ID: NNLZQ

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	OptHSide
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	-984756.778811
FMO2-HF: Nuclear repulsion	937240.996458
FMO2-HF: Total energy	-47515.782353
FMO2-MP2: Total energy	-47655.002995

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.
-148.048	-145.299	0.508	-1.076	-2.183	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 : 0.968 / q_NPA : 0.969

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].
3	A	6	LYS	1	0.857	0.934	3.677	38.253	39.856	-0.002	-0.573	-1.029
4	A	7	ILE	0	0.085	0.066	6.310	0.020	0.020	0.000	0.000	0.000
5	A	8	MET	0	-0.010	-0.002	8.985	-0.511	-0.511	0.000	0.000	0.000
6	A	9	ILE	0	-0.011	0.001	12.586	1.114	1.114	0.000	0.000	0.000
7	A	10	SER	0	0.039	0.012	15.476	-0.097	-0.097	0.000	0.000	0.000
8	A	11	SER	0	0.060	0.001	18.805	-0.230	-0.230	0.000	0.000	0.000
9	A	12	LEU	0	-0.017	0.000	20.627	0.206	0.206	0.000	0.000	0.000
10	A	13	ASP	-1	-0.799	-0.886	18.893	-13.200	-13.200	0.000	0.000	0.000
11	A	14	ALA	0	0.016	0.017	17.258	0.046	0.046	0.000	0.000	0.000
12	A	15	GLU	-1	-0.953	-0.965	18.421	-11.778	-11.778	0.000	0.000	0.000
13	A	16	ARG	1	0.865	0.931	21.804	11.751	11.751	0.000	0.000	0.000
14	A	17	LEU	0	-0.019	-0.018	16.866	0.448	0.448	0.000	0.000	0.000
15	A	18	GLU	-1	-0.877	-0.922	18.469	-14.833	-14.833	0.000	0.000	0.000
16	A	19	ILE	0	0.024	0.013	20.515	0.466	0.466	0.000	0.000	0.000
17	A	20	LEU	0	-0.072	-0.026	21.810	0.532	0.532	0.000	0.000	0.000
18	A	21	LEU	0	0.007	-0.007	17.553	0.456	0.456	0.000	0.000	0.000
19	A	22	GLU	-1	-0.918	-0.949	21.931	-11.658	-11.658	0.000	0.000	0.000
20	A	23	THR	0	-0.103	-0.066	24.291	0.567	0.567	0.000	0.000	0.000
21	A	24	LEU	0	-0.069	-0.029	24.246	0.433	0.433	0.000	0.000	0.000
22	A	25	SER	0	0.035	0.041	24.295	-0.088	-0.088	0.000	0.000	0.000
23	A	26	GLN	0	-0.044	-0.025	24.595	-0.093	-0.093	0.000	0.000	0.000
24	A	27	ASN	0	-0.059	-0.036	25.126	0.198	0.198	0.000	0.000	0.000
25	A	28	ALA	0	0.037	0.027	22.436	-0.417	-0.417	0.000	0.000	0.000
26	A	29	PHE	0	-0.007	0.004	17.984	0.342	0.342	0.000	0.000	0.000
27	A	30	PRO	0	-0.005	-0.021	19.568	-0.378	-0.378	0.000	0.000	0.000
28	A	31	GLY	0	0.045	0.022	15.412	-0.021	-0.021	0.000	0.000	0.000
29	A	32	ARG	1	0.728	0.853	14.821	12.217	12.217	0.000	0.000	0.000
30	A	33	ASP	-1	-0.890	-0.947	14.688	-15.168	-15.168	0.000	0.000	0.000
31	A	34	ASP	-1	-0.939	-0.979	10.779	-18.828	-18.828	0.000	0.000	0.000
32	A	35	LEU	0	0.028	0.016	10.580	-1.114	-1.114	0.000	0.000	0.000
33	A	36	GLU	-1	-0.806	-0.904	12.484	-15.165	-15.165	0.000	0.000	0.000
34	A	37	ALA	0	-0.042	-0.013	9.266	-0.886	-0.886	0.000	0.000	0.000
35	A	38	GLU	-1	-0.984	-1.006	7.847	-24.544	-24.544	0.000	0.000	0.000
36	A	39	LEU	0	0.013	-0.010	9.039	-1.113	-1.113	0.000	0.000	0.000
37	A	40	ALA	0	-0.016	0.009	11.420	-0.335	-0.335	0.000	0.000	0.000
38	A	41	ARG	1	0.785	0.891	2.635	41.530	42.676	0.510	-0.503	-1.154
39	A	42	ALA	0	0.039	0.023	8.401	-3.820	-3.820	0.000	0.000	0.000
40	A	43	GLU	-1	-0.998	-1.002	8.718	-30.122	-30.122	0.000	0.000	0.000
41	A	44	VAL	0	-0.012	-0.004	11.584	1.057	1.057	0.000	0.000	0.000
42	A	45	VAL	0	-0.008	-0.003	14.297	0.187	0.187	0.000	0.000	0.000
43	A	46	ASP	-1	-0.875	-0.958	17.041	-12.593	-12.593	0.000	0.000	0.000
44	A	47	PRO	0	-0.017	-0.040	19.744	-0.556	-0.556	0.000	0.000	0.000
45	A	48	GLU	-1	-0.962	-0.970	21.248	-12.242	-12.242	0.000	0.000	0.000
46	A	49	GLU	-1	-1.002	-0.984	17.461	-15.398	-15.398	0.000	0.000	0.000
47	A	50	ILE	0	-0.043	-0.016	15.919	-1.347	-1.347	0.000	0.000	0.000
48	A	51	PRO	0	-0.004	-0.005	15.037	0.875	0.875	0.000	0.000	0.000
49	A	52	PRO	0	0.022	0.002	18.114	-0.094	-0.094	0.000	0.000	0.000
50	A	53	THR	0	-0.019	-0.010	17.183	0.294	0.294	0.000	0.000	0.000
51	A	54	VAL	0	0.007	0.008	13.547	-0.425	-0.425	0.000	0.000	0.000
52	A	55	VAL	0	-0.021	-0.002	15.265	0.990	0.990	0.000	0.000	0.000
53	A	56	THR	0	0.058	0.029	15.563	-0.738	-0.738	0.000	0.000	0.000
54	A	57	MET	0	-0.028	-0.022	18.013	0.353	0.353	0.000	0.000	0.000
55	A	58	ASN	0	-0.057	-0.049	20.388	0.143	0.143	0.000	0.000	0.000
56	A	59	SER	0	0.019	0.029	20.239	0.259	0.259	0.000	0.000	0.000
57	A	60	THR	0	-0.029	-0.036	22.326	0.074	0.074	0.000	0.000	0.000
58	A	61	VAL	0	-0.019	-0.009	19.214	-0.258	-0.258	0.000	0.000	0.000
59	A	62	ARG	1	0.916	0.952	22.201	10.248	10.248	0.000	0.000	0.000
60	A	63	PHE	0	0.021	-0.009	18.920	-0.580	-0.580	0.000	0.000	0.000
61	A	64	ARG	1	0.813	0.899	23.393	11.000	11.000	0.000	0.000	0.000
62	A	65	VAL	0	-0.033	-0.006	23.869	-0.495	-0.495	0.000	0.000	0.000
63	A	66	GLU	-1	-0.912	-0.974	22.799	-11.431	-11.431	0.000	0.000	0.000
64	A	67	SER	0	-0.056	-0.036	25.684	0.216	0.216	0.000	0.000	0.000
65	A	68	SER	0	-0.092	-0.097	28.928	0.225	0.225	0.000	0.000	0.000
66	A	69	ALA	0	-0.028	-0.004	28.882	0.220	0.220	0.000	0.000	0.000
67	A	70	GLU	-1	-0.875	-0.887	29.548	-8.887	-8.887	0.000	0.000	0.000
68	A	71	GLU	-1	-0.778	-0.881	27.889	-10.406	-10.406	0.000	0.000	0.000
69	A	72	PHE	0	-0.057	-0.019	23.618	0.346	0.346	0.000	0.000	0.000
70	A	73	OCS	-1	-0.860	-0.930	25.719	-10.378	-10.378	0.000	0.000	0.000
71	A	74	LEU	0	-0.034	-0.016	22.416	0.202	0.202	0.000	0.000	0.000
72	A	75	THR	0	0.012	0.007	23.405	-0.436	-0.436	0.000	0.000	0.000
73	A	76	LEU	0	-0.031	0.005	17.633	0.308	0.308	0.000	0.000	0.000
74	A	77	VAL	0	0.011	0.006	21.933	0.023	0.023	0.000	0.000	0.000
75	A	78	TYR	0	0.012	-0.033	22.021	-0.121	-0.121	0.000	0.000	0.000
76	A	79	PRO	0	0.031	0.005	24.041	0.313	0.313	0.000	0.000	0.000
77	A	80	LYS	1	0.741	0.843	26.939	10.093	10.093	0.000	0.000	0.000
78	A	81	ASP	-1	-0.776	-0.869	28.036	-9.611	-9.611	0.000	0.000	0.000
79	A	82	VAL	0	-0.002	0.018	26.775	-0.003	-0.003	0.000	0.000	0.000
80	A	83	ASP	-1	-0.757	-0.838	29.368	-8.553	-8.553	0.000	0.000	0.000
81	A	84	THR	0	-0.049	-0.045	31.920	-0.096	-0.096	0.000	0.000	0.000
82	A	85	SER	0	-0.093	-0.072	32.173	0.072	0.072	0.000	0.000	0.000
83	A	86	GLY	0	-0.004	-0.005	30.224	0.102	0.102	0.000	0.000	0.000
84	A	87	GLU	-1	-0.814	-0.876	28.282	-9.925	-9.925	0.000	0.000	0.000
85	A	88	LYS	1	0.795	0.911	26.638	8.965	8.965	0.000	0.000	0.000
86	A	89	ILE	0	-0.004	-0.006	21.336	0.128	0.128	0.000	0.000	0.000
87	A	90	SER	0	0.010	0.007	22.951	-0.396	-0.396	0.000	0.000	0.000
88	A	91	ILE	0	0.057	0.022	16.293	-0.099	-0.099	0.000	0.000	0.000
89	A	92	LEU	0	-0.019	-0.017	18.765	-0.367	-0.367	0.000	0.000	0.000
90	A	93	ALA	0	-0.043	-0.004	21.152	0.148	0.148	0.000	0.000	0.000
91	A	94	PRO	0	0.018	-0.003	19.290	-0.478	-0.478	0.000	0.000	0.000
92	A	95	VAL	0	0.008	0.010	17.602	0.413	0.413	0.000	0.000	0.000
93	A	96	GLY	0	0.066	0.027	17.119	-0.532	-0.532	0.000	0.000	0.000
94	A	97	SER	0	-0.040	-0.031	15.842	-0.490	-0.490	0.000	0.000	0.000
95	A	98	ALA	0	-0.012	-0.006	12.915	-0.692	-0.692	0.000	0.000	0.000
96	A	99	LEU	0	-0.023	-0.017	12.914	-0.630	-0.630	0.000	0.000	0.000
97	A	100	LEU	0	-0.008	-0.004	13.650	-0.134	-0.134	0.000	0.000	0.000
98	A	101	GLY	0	0.005	0.002	11.104	-0.851	-0.851	0.000	0.000	0.000
99	A	102	LEU	0	-0.045	0.001	10.527	-1.242	-1.242	0.000	0.000	0.000
100	A	103	ALA	0	0.002	-0.010	12.377	0.565	0.565	0.000	0.000	0.000
101	A	104	GLN	0	-0.073	-0.062	14.441	-0.060	-0.060	0.000	0.000	0.000
102	A	105	GLY	0	-0.055	-0.022	16.607	-0.574	-0.574	0.000	0.000	0.000
103	A	106	ASP	-1	-0.844	-0.906	12.071	-20.290	-20.290	0.000	0.000	0.000
104	A	107	GLU	-1	-0.841	-0.906	14.603	-13.004	-13.004	0.000	0.000	0.000
105	A	108	ILE	0	-0.020	0.005	13.819	-0.773	-0.773	0.000	0.000	0.000
106	A	109	GLU	-1	-0.875	-0.941	16.332	-12.724	-12.724	0.000	0.000	0.000
107	A	110	TRP	0	0.021	0.010	18.478	-0.390	-0.390	0.000	0.000	0.000
108	A	111	PRO	0	0.004	-0.007	21.115	0.307	0.307	0.000	0.000	0.000
109	A	112	LYS	1	0.967	1.002	24.369	9.427	9.427	0.000	0.000	0.000
110	A	113	PRO	0	0.013	-0.004	27.658	0.108	0.108	0.000	0.000	0.000
111	A	114	GLY	0	-0.030	-0.009	30.729	0.127	0.127	0.000	0.000	0.000
112	A	115	GLY	0	-0.009	0.002	29.212	0.129	0.129	0.000	0.000	0.000
113	A	116	GLY	0	-0.022	-0.018	27.220	0.136	0.136	0.000	0.000	0.000
114	A	117	VAL	0	-0.010	-0.004	21.779	0.041	0.041	0.000	0.000	0.000
115	A	118	LEU	0	-0.026	-0.009	23.809	0.329	0.329	0.000	0.000	0.000
116	A	119	ARG	1	0.873	0.916	16.119	13.998	13.998	0.000	0.000	0.000
117	A	120	VAL	0	-0.003	-0.007	19.856	0.505	0.505	0.000	0.000	0.000
118	A	121	ARG	1	0.823	0.904	18.862	12.605	12.605	0.000	0.000	0.000
119	A	122	ILE	0	0.028	0.028	16.008	0.758	0.758	0.000	0.000	0.000
120	A	123	VAL	0	-0.073	-0.046	19.796	-0.292	-0.292	0.000	0.000	0.000
121	A	124	GLU	-1	-0.951	-0.978	22.531	-10.751	-10.751	0.000	0.000	0.000
122	A	125	VAL	0	0.006	0.011	18.375	0.017	0.017	0.000	0.000	0.000
123	A	126	THR	0	0.014	0.014	21.859	0.232	0.232	0.000	0.000	0.000
124	A	127	TYR	0	-0.005	0.020	22.918	0.576	0.576	0.000	0.000	0.000

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