FMO DATABASE

FMODB ID: 89M1Y

Calculation Name: 4JG2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JG2

Chain ID: A

ChEMBL ID:

UniProt ID: Q73EI2

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:

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	185
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1811842.176879
FMO2-HF: Nuclear repulsion	1741901.653181
FMO2-HF: Total energy	-69940.523697
FMO2-MP2: Total energy	-70147.793384

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:LYS)

Summations of interaction energy for fragment #1(A:-11: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.
-101.173	-92.473	42.024	-24.083	-26.643	-0.225

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.853 / q_NPA : 0.916

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	-9	THR	0	0.018	-0.003	3.817	1.040	3.559	-0.014	-1.266	-1.240	0.008
4	A	-8	GLU	-1	-0.800	-0.843	1.658	-141.525	-142.140	22.865	-12.376	-9.875	-0.144
5	A	-7	ASN	0	0.054	0.016	4.599	3.784	3.906	-0.001	-0.012	-0.109	0.000
6	A	-6	LEU	0	0.046	0.013	4.780	-2.696	-2.616	-0.001	-0.002	-0.077	0.000
7	A	-5	TYR	0	-0.017	0.000	6.122	-0.133	-0.133	0.000	0.000	0.000	0.000
8	A	-4	PHE	0	-0.034	-0.026	7.631	0.908	0.908	0.000	0.000	0.000	0.000
9	A	-3	GLN	0	-0.063	-0.006	2.555	-4.592	-3.622	0.979	-0.674	-1.275	0.001
10	A	-2	SER	0	-0.007	-0.029	1.828	-17.974	-19.258	12.439	-5.816	-5.339	-0.061
11	A	-1	ASN	0	-0.004	-0.003	4.060	2.757	3.313	-0.001	-0.179	-0.376	-0.001
12	A	0	ALA	0	0.008	0.011	4.700	4.923	5.064	-0.001	-0.031	-0.109	0.000
13	A	4	GLN	0	0.056	0.016	2.498	-22.389	-17.127	4.011	-3.421	-5.853	-0.025
14	A	5	ASN	0	-0.030	-0.016	2.482	3.029	4.037	1.733	-0.512	-2.229	-0.003
15	A	6	ARG	1	0.884	0.911	3.436	25.291	25.232	0.015	0.206	-0.161	0.000
16	A	7	THR	0	0.065	0.044	6.850	2.052	2.052	0.000	0.000	0.000	0.000
17	A	8	LYS	1	0.915	0.973	5.017	42.494	42.494	0.000	0.000	0.000	0.000
18	A	9	VAL	0	-0.008	-0.003	6.889	-0.738	-0.738	0.000	0.000	0.000	0.000
19	A	10	VAL	0	-0.034	-0.021	7.936	0.372	0.372	0.000	0.000	0.000	0.000
20	A	11	THR	0	0.050	0.019	10.409	0.167	0.167	0.000	0.000	0.000	0.000
21	A	12	SER	0	0.051	0.009	13.791	-0.523	-0.523	0.000	0.000	0.000	0.000
22	A	13	VAL	0	0.000	-0.024	15.537	0.198	0.198	0.000	0.000	0.000	0.000
23	A	14	ASN	0	-0.014	-0.002	18.066	0.945	0.945	0.000	0.000	0.000	0.000
24	A	15	THR	0	-0.034	0.011	18.041	0.142	0.142	0.000	0.000	0.000	0.000
25	A	16	ARG	1	0.880	0.942	20.270	10.360	10.360	0.000	0.000	0.000	0.000
26	A	17	LEU	0	-0.007	0.004	20.503	-0.323	-0.323	0.000	0.000	0.000	0.000
27	A	18	SER	0	0.098	0.040	24.055	0.707	0.707	0.000	0.000	0.000	0.000
28	A	19	TYR	0	-0.034	-0.019	25.848	-0.415	-0.415	0.000	0.000	0.000	0.000
29	A	20	PHE	0	-0.024	-0.020	22.137	-0.464	-0.464	0.000	0.000	0.000	0.000
30	A	21	HIS	0	0.023	0.016	24.628	0.457	0.457	0.000	0.000	0.000	0.000
31	A	22	GLY	0	0.036	0.002	22.187	-0.404	-0.404	0.000	0.000	0.000	0.000
32	A	23	TRP	0	-0.004	-0.008	22.632	-0.521	-0.521	0.000	0.000	0.000	0.000
33	A	24	GLU	-1	-0.827	-0.887	25.242	-10.215	-10.215	0.000	0.000	0.000	0.000
34	A	25	PRO	0	-0.049	-0.007	24.897	-0.191	-0.191	0.000	0.000	0.000	0.000
35	A	26	VAL	0	0.085	0.026	26.488	0.371	0.371	0.000	0.000	0.000	0.000
36	A	27	SER	0	-0.008	-0.009	27.943	-0.297	-0.297	0.000	0.000	0.000	0.000
37	A	28	ILE	0	-0.014	-0.014	26.624	0.173	0.173	0.000	0.000	0.000	0.000
38	A	29	ASN	0	-0.027	-0.026	30.569	-0.163	-0.163	0.000	0.000	0.000	0.000
39	A	30	GLY	0	0.093	0.058	33.561	0.094	0.094	0.000	0.000	0.000	0.000
40	A	31	GLY	0	-0.049	-0.012	29.550	-0.067	-0.067	0.000	0.000	0.000	0.000
41	A	32	ALA	0	-0.031	-0.013	26.824	0.035	0.035	0.000	0.000	0.000	0.000
42	A	33	GLU	-1	-0.893	-0.939	27.234	-10.693	-10.693	0.000	0.000	0.000	0.000
43	A	34	LYS	1	0.798	0.887	22.152	11.736	11.736	0.000	0.000	0.000	0.000
44	A	35	TYR	0	0.100	0.071	20.711	0.265	0.265	0.000	0.000	0.000	0.000
45	A	36	SER	0	-0.057	-0.055	21.481	-0.307	-0.307	0.000	0.000	0.000	0.000
46	A	37	VAL	0	0.012	0.010	20.121	0.171	0.171	0.000	0.000	0.000	0.000
47	A	38	SER	0	-0.016	-0.003	21.859	-0.293	-0.293	0.000	0.000	0.000	0.000
48	A	39	VAL	0	-0.023	-0.013	17.634	0.165	0.165	0.000	0.000	0.000	0.000
49	A	40	LEU	0	0.024	0.017	21.039	-0.044	-0.044	0.000	0.000	0.000	0.000
50	A	41	ILE	0	-0.017	-0.026	17.564	-0.372	-0.372	0.000	0.000	0.000	0.000
51	A	42	PRO	0	0.069	0.040	20.461	0.346	0.346	0.000	0.000	0.000	0.000
52	A	43	LYS	1	0.819	0.883	21.428	9.948	9.948	0.000	0.000	0.000	0.000
53	A	44	THR	0	-0.009	-0.012	22.792	-0.113	-0.113	0.000	0.000	0.000	0.000
54	A	45	ASP	-1	-0.811	-0.851	16.456	-15.902	-15.902	0.000	0.000	0.000	0.000
55	A	46	LYS	1	0.925	0.930	17.748	11.445	11.445	0.000	0.000	0.000	0.000
56	A	47	GLU	-1	-0.919	-0.936	11.571	-18.800	-18.800	0.000	0.000	0.000	0.000
57	A	48	THR	0	0.012	-0.023	13.217	-1.343	-1.343	0.000	0.000	0.000	0.000
58	A	49	ILE	0	-0.038	-0.014	14.175	-0.481	-0.481	0.000	0.000	0.000	0.000
59	A	50	ASN	0	-0.030	-0.022	14.585	0.264	0.264	0.000	0.000	0.000	0.000
60	A	51	ALA	0	0.012	0.015	9.983	-0.371	-0.371	0.000	0.000	0.000	0.000
61	A	52	ILE	0	0.012	0.004	11.550	-0.813	-0.813	0.000	0.000	0.000	0.000
62	A	53	ASN	0	-0.017	-0.008	13.767	0.110	0.110	0.000	0.000	0.000	0.000
63	A	54	ALA	0	-0.001	0.005	11.505	0.218	0.218	0.000	0.000	0.000	0.000
64	A	55	ALA	0	0.019	0.015	10.341	-0.380	-0.380	0.000	0.000	0.000	0.000
65	A	56	VAL	0	-0.039	-0.027	11.754	0.068	0.068	0.000	0.000	0.000	0.000
66	A	57	ASP	-1	-0.800	-0.889	15.262	-14.438	-14.438	0.000	0.000	0.000	0.000
67	A	58	ALA	0	-0.024	0.000	10.621	0.305	0.305	0.000	0.000	0.000	0.000
68	A	59	ALA	0	0.017	0.011	12.701	-0.061	-0.061	0.000	0.000	0.000	0.000
69	A	60	ILE	0	-0.042	-0.026	13.914	0.754	0.754	0.000	0.000	0.000	0.000
70	A	61	GLU	-1	-0.829	-0.897	14.573	-16.816	-16.816	0.000	0.000	0.000	0.000
71	A	62	GLU	-1	-0.889	-0.944	9.758	-25.830	-25.830	0.000	0.000	0.000	0.000
72	A	63	GLY	0	-0.017	-0.009	14.511	0.380	0.380	0.000	0.000	0.000	0.000
73	A	64	ILE	0	-0.066	-0.036	17.730	0.602	0.602	0.000	0.000	0.000	0.000
74	A	65	ALA	0	-0.008	-0.001	15.629	0.523	0.523	0.000	0.000	0.000	0.000
75	A	66	LYS	1	0.886	0.961	16.578	16.531	16.531	0.000	0.000	0.000	0.000
76	A	67	PHE	0	-0.023	-0.030	18.263	0.341	0.341	0.000	0.000	0.000	0.000
77	A	68	GLY	0	0.019	0.037	21.392	0.633	0.633	0.000	0.000	0.000	0.000
78	A	69	GLY	0	0.026	0.009	23.322	0.100	0.100	0.000	0.000	0.000	0.000
79	A	70	LYS	1	0.931	0.960	24.589	9.388	9.388	0.000	0.000	0.000	0.000
80	A	71	LYS	1	0.934	0.950	18.659	14.392	14.392	0.000	0.000	0.000	0.000
81	A	72	PRO	0	-0.011	0.003	22.239	0.493	0.493	0.000	0.000	0.000	0.000
82	A	73	ASN	0	0.036	0.017	24.599	-0.421	-0.421	0.000	0.000	0.000	0.000
83	A	74	LYS	1	0.906	0.910	19.548	13.908	13.908	0.000	0.000	0.000	0.000
84	A	75	ALA	0	0.030	0.020	25.085	-0.069	-0.069	0.000	0.000	0.000	0.000
85	A	76	ALA	0	-0.059	-0.020	27.896	0.233	0.233	0.000	0.000	0.000	0.000
86	A	77	ILE	0	-0.073	-0.039	22.078	0.016	0.016	0.000	0.000	0.000	0.000
87	A	78	LYS	1	0.911	0.964	24.334	11.233	11.233	0.000	0.000	0.000	0.000
88	A	79	LEU	0	0.040	-0.001	20.812	-0.614	-0.614	0.000	0.000	0.000	0.000
89	A	80	PRO	0	0.005	-0.005	17.696	0.512	0.512	0.000	0.000	0.000	0.000
90	A	81	LEU	0	-0.011	0.009	18.405	0.041	0.041	0.000	0.000	0.000	0.000
91	A	82	ARG	1	0.784	0.884	20.847	11.657	11.657	0.000	0.000	0.000	0.000
92	A	83	ASP	-1	-0.779	-0.894	24.246	-10.584	-10.584	0.000	0.000	0.000	0.000
93	A	84	GLY	0	-0.006	-0.016	26.585	0.283	0.283	0.000	0.000	0.000	0.000
94	A	85	ASP	-1	-0.775	-0.866	28.329	-9.442	-9.442	0.000	0.000	0.000	0.000
95	A	86	VAL	0	-0.015	-0.015	30.380	0.304	0.304	0.000	0.000	0.000	0.000
96	A	87	GLU	-1	-0.836	-0.887	27.574	-10.520	-10.520	0.000	0.000	0.000	0.000
97	A	88	ARG	1	0.836	0.920	29.570	9.801	9.801	0.000	0.000	0.000	0.000
98	A	89	ASP	-1	-0.876	-0.920	32.697	-8.116	-8.116	0.000	0.000	0.000	0.000
99	A	90	ASP	-1	-0.870	-0.943	32.248	-8.984	-8.984	0.000	0.000	0.000	0.000
100	A	91	GLU	-1	-0.875	-0.964	32.839	-8.489	-8.489	0.000	0.000	0.000	0.000
101	A	92	ALA	0	-0.065	-0.023	29.623	-0.170	-0.170	0.000	0.000	0.000	0.000
102	A	93	TYR	0	-0.054	-0.047	27.058	-0.546	-0.546	0.000	0.000	0.000	0.000
103	A	94	LYS	1	0.922	0.981	28.631	8.564	8.564	0.000	0.000	0.000	0.000
104	A	95	GLY	0	-0.003	0.009	28.522	-0.166	-0.166	0.000	0.000	0.000	0.000
105	A	96	HIS	0	-0.090	-0.061	23.702	-0.731	-0.731	0.000	0.000	0.000	0.000
106	A	97	TYR	0	0.019	0.013	21.454	0.231	0.231	0.000	0.000	0.000	0.000
107	A	98	PHE	0	-0.001	-0.011	22.099	-0.161	-0.161	0.000	0.000	0.000	0.000
108	A	99	VAL	0	-0.006	0.009	17.358	-0.087	-0.087	0.000	0.000	0.000	0.000
109	A	100	ASN	0	-0.011	0.005	20.749	0.229	0.229	0.000	0.000	0.000	0.000
110	A	101	ALA	0	0.009	0.013	17.351	-0.240	-0.240	0.000	0.000	0.000	0.000
111	A	102	ASN	0	-0.019	-0.027	18.616	0.684	0.684	0.000	0.000	0.000	0.000
112	A	103	SER	0	0.030	0.015	16.433	-0.790	-0.790	0.000	0.000	0.000	0.000
113	A	104	LYS	1	0.972	0.982	18.887	13.185	13.185	0.000	0.000	0.000	0.000
114	A	105	THR	0	0.011	0.023	17.007	0.539	0.539	0.000	0.000	0.000	0.000
115	A	106	PRO	0	0.011	0.005	18.893	-0.351	-0.351	0.000	0.000	0.000	0.000
116	A	107	PRO	0	-0.028	0.011	16.447	-0.887	-0.887	0.000	0.000	0.000	0.000
117	A	108	GLN	0	0.018	0.002	13.518	-0.477	-0.477	0.000	0.000	0.000	0.000
118	A	109	ILE	0	-0.008	0.000	16.639	-0.741	-0.741	0.000	0.000	0.000	0.000
119	A	110	VAL	0	-0.005	0.003	15.677	0.430	0.430	0.000	0.000	0.000	0.000
120	A	111	ASP	-1	-0.692	-0.830	19.035	-14.249	-14.249	0.000	0.000	0.000	0.000
121	A	112	LYS	1	0.915	0.944	18.581	12.504	12.504	0.000	0.000	0.000	0.000
122	A	113	ALA	0	-0.043	-0.009	18.444	-0.536	-0.536	0.000	0.000	0.000	0.000
123	A	114	VAL	0	-0.057	-0.029	13.732	-0.642	-0.642	0.000	0.000	0.000	0.000
124	A	115	ARG	1	0.885	0.928	17.058	12.927	12.927	0.000	0.000	0.000	0.000
125	A	116	PRO	0	-0.003	-0.013	19.627	0.071	0.071	0.000	0.000	0.000	0.000
126	A	117	ILE	0	-0.010	0.003	21.209	0.504	0.504	0.000	0.000	0.000	0.000
127	A	118	LEU	0	-0.029	-0.020	23.853	-0.024	-0.024	0.000	0.000	0.000	0.000
128	A	119	ASP	-1	-0.789	-0.880	27.096	-9.607	-9.607	0.000	0.000	0.000	0.000
129	A	120	ARG	1	0.842	0.885	27.562	10.479	10.479	0.000	0.000	0.000	0.000
130	A	121	ASN	0	-0.050	-0.044	28.646	-0.039	-0.039	0.000	0.000	0.000	0.000
131	A	122	GLU	-1	-0.877	-0.920	26.354	-11.004	-11.004	0.000	0.000	0.000	0.000
132	A	123	VAL	0	-0.081	-0.049	22.879	-0.427	-0.427	0.000	0.000	0.000	0.000
133	A	124	TYR	0	0.028	-0.010	26.065	0.129	0.129	0.000	0.000	0.000	0.000
134	A	125	SER	0	0.023	0.003	27.222	-0.487	-0.487	0.000	0.000	0.000	0.000
135	A	126	GLY	0	0.062	0.039	27.444	0.400	0.400	0.000	0.000	0.000	0.000
136	A	127	CYS	0	-0.074	0.007	25.173	-0.129	-0.129	0.000	0.000	0.000	0.000
137	A	128	TYR	0	0.031	-0.005	22.596	-0.091	-0.091	0.000	0.000	0.000	0.000
138	A	129	ALA	0	0.049	0.002	19.677	-0.026	-0.026	0.000	0.000	0.000	0.000
139	A	130	ARG	1	0.836	0.931	10.615	21.123	21.123	0.000	0.000	0.000	0.000
140	A	131	VAL	0	0.037	0.011	15.238	-0.031	-0.031	0.000	0.000	0.000	0.000
141	A	132	SER	0	-0.029	-0.011	9.887	-2.004	-2.004	0.000	0.000	0.000	0.000
142	A	133	LEU	0	-0.023	-0.005	11.325	1.293	1.293	0.000	0.000	0.000	0.000
143	A	134	ASN	0	0.011	0.005	8.660	-4.518	-4.518	0.000	0.000	0.000	0.000
144	A	135	PHE	0	0.009	0.004	11.243	2.147	2.147	0.000	0.000	0.000	0.000
145	A	136	TYR	0	0.023	0.004	12.319	-0.952	-0.952	0.000	0.000	0.000	0.000
146	A	137	ALA	0	0.028	0.020	14.853	1.025	1.025	0.000	0.000	0.000	0.000
147	A	138	PHE	0	-0.043	-0.021	18.064	-0.062	-0.062	0.000	0.000	0.000	0.000
148	A	139	ASN	0	-0.005	-0.024	21.013	0.576	0.576	0.000	0.000	0.000	0.000
149	A	140	SER	0	0.042	0.028	24.679	-0.025	-0.025	0.000	0.000	0.000	0.000
150	A	141	ASN	0	0.031	0.008	26.828	0.266	0.266	0.000	0.000	0.000	0.000
151	A	142	GLY	0	0.044	0.035	29.851	0.134	0.134	0.000	0.000	0.000	0.000
152	A	143	ASN	0	-0.047	-0.011	26.856	-0.021	-0.021	0.000	0.000	0.000	0.000
153	A	144	LYS	1	1.013	0.995	24.825	10.094	10.094	0.000	0.000	0.000	0.000
154	A	145	GLY	0	0.006	0.013	22.475	0.391	0.391	0.000	0.000	0.000	0.000
155	A	146	VAL	0	-0.044	-0.010	16.364	-0.415	-0.415	0.000	0.000	0.000	0.000
156	A	147	ALA	0	-0.004	0.013	18.192	0.583	0.583	0.000	0.000	0.000	0.000
157	A	148	CYS	0	-0.008	-0.020	15.281	-0.937	-0.937	0.000	0.000	0.000	0.000
158	A	149	GLY	0	0.008	0.012	14.573	0.865	0.865	0.000	0.000	0.000	0.000
159	A	150	LEU	0	-0.029	-0.020	14.048	-1.099	-1.099	0.000	0.000	0.000	0.000
160	A	151	GLY	0	0.009	0.004	12.152	-0.462	-0.462	0.000	0.000	0.000	0.000
161	A	152	ASN	0	-0.014	-0.025	12.002	2.064	2.064	0.000	0.000	0.000	0.000
162	A	153	ILE	0	0.029	0.011	14.235	-0.177	-0.177	0.000	0.000	0.000	0.000
163	A	154	GLN	0	-0.050	-0.020	15.496	-0.519	-0.519	0.000	0.000	0.000	0.000
164	A	155	LYS	1	0.815	0.898	17.410	11.815	11.815	0.000	0.000	0.000	0.000
165	A	156	ILE	0	-0.112	-0.058	17.640	-0.176	-0.176	0.000	0.000	0.000	0.000
166	A	157	ARG	1	0.918	0.952	21.704	11.908	11.908	0.000	0.000	0.000	0.000
167	A	158	ASP	-1	-0.756	-0.846	25.296	-11.032	-11.032	0.000	0.000	0.000	0.000
168	A	159	GLY	0	-0.015	-0.016	28.382	-0.102	-0.102	0.000	0.000	0.000	0.000
169	A	160	GLU	-1	-0.914	-0.941	29.707	-8.609	-8.609	0.000	0.000	0.000	0.000
170	A	161	PRO	0	0.047	0.019	31.663	-0.304	-0.304	0.000	0.000	0.000	0.000
171	A	162	LEU	0	-0.066	-0.026	28.965	0.189	0.189	0.000	0.000	0.000	0.000
172	A	163	GLY	0	0.029	0.017	32.843	-0.050	-0.050	0.000	0.000	0.000	0.000
173	A	164	GLY	0	-0.023	-0.018	32.865	-0.286	-0.286	0.000	0.000	0.000	0.000
174	A	165	ARG	1	0.940	0.965	27.309	10.673	10.673	0.000	0.000	0.000	0.000
175	A	166	THR	0	-0.009	-0.012	34.671	0.002	0.002	0.000	0.000	0.000	0.000
176	A	167	ASN	0	-0.071	-0.046	35.291	0.184	0.184	0.000	0.000	0.000	0.000
177	A	168	ALA	0	0.092	0.060	37.696	-0.018	-0.018	0.000	0.000	0.000	0.000
178	A	169	ALA	0	-0.022	-0.019	40.745	0.092	0.092	0.000	0.000	0.000	0.000
179	A	170	ASP	-1	-0.898	-0.936	35.835	-8.573	-8.573	0.000	0.000	0.000	0.000
180	A	171	ASP	-1	-0.975	-0.970	38.646	-8.228	-8.228	0.000	0.000	0.000	0.000
181	A	172	PHE	0	-0.100	-0.056	40.994	0.164	0.164	0.000	0.000	0.000	0.000
182	A	173	THR	0	0.024	0.014	44.637	-0.073	-0.073	0.000	0.000	0.000	0.000
183	A	174	THR	0	-0.056	-0.043	47.258	-0.012	-0.012	0.000	0.000	0.000	0.000
184	A	175	ILE	0	-0.035	-0.015	50.359	0.022	0.022	0.000	0.000	0.000	0.000
185	A	176	GLU	-1	-0.913	-0.940	52.726	-5.905	-5.905	0.000	0.000	0.000	0.000

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