FMO DATABASE

FMODB ID: 4JLYN

Calculation Name: 2P2O-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2P2O

Chain ID: A

ChEMBL ID:

UniProt ID: Q75TD0

Base Structure: X-ray

Registration Date: 2023-09-22

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	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	184
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1933770.540439
FMO2-HF: Nuclear repulsion	1862440.596113
FMO2-HF: Total energy	-71329.944326
FMO2-MP2: Total energy	-71539.688113

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:2:LYS)

Summations of interaction energy for fragment #1(A:2: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.
-137.352	-125.692	10.571	-9.223	-13.008	-0.088

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.889 / q_NPA : 0.939

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	4	GLU	-1	-0.732	-0.873	2.887	-46.416	-43.916	0.275	-1.325	-1.449	-0.007
4	A	5	LYS	1	0.919	0.949	5.555	24.438	24.438	0.000	0.000	0.000	0.000
5	A	6	GLU	-1	-0.863	-0.939	1.965	-61.809	-58.663	5.778	-3.933	-4.991	-0.042
6	A	7	LYS	1	0.770	0.876	2.307	25.944	29.484	2.393	-2.226	-3.707	-0.014
7	A	8	MET	0	-0.005	0.019	3.101	2.837	2.417	0.049	0.611	-0.240	-0.001
8	A	9	LEU	0	-0.020	-0.012	5.886	2.299	2.299	0.000	0.000	0.000	0.000
9	A	10	ALA	0	-0.067	-0.027	2.132	-2.351	-1.788	1.957	-1.179	-1.341	-0.011
10	A	11	GLY	0	0.015	0.022	4.007	3.284	3.480	-0.001	-0.100	-0.096	-0.001
11	A	12	HIS	0	-0.150	-0.070	3.234	-10.144	-8.009	0.120	-1.071	-1.184	-0.012
12	A	13	LEU	0	0.025	0.003	6.056	2.356	2.356	0.000	0.000	0.000	0.000
13	A	14	TYR	0	0.002	0.004	6.483	-4.371	-4.371	0.000	0.000	0.000	0.000
14	A	15	ASN	0	0.066	0.021	8.221	3.946	3.946	0.000	0.000	0.000	0.000
15	A	16	PRO	0	0.050	0.033	10.745	-0.650	-0.650	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.021	-0.013	12.905	0.990	0.990	0.000	0.000	0.000	0.000
17	A	18	ASP	-1	-0.851	-0.935	9.372	-25.742	-25.742	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.032	-0.006	11.775	0.690	0.690	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.986	-0.973	9.032	-25.669	-25.669	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.008	0.000	8.822	0.922	0.922	0.000	0.000	0.000	0.000
21	A	22	VAL	0	-0.014	0.003	12.592	1.216	1.216	0.000	0.000	0.000	0.000
22	A	23	LYS	1	0.982	0.999	15.773	16.334	16.334	0.000	0.000	0.000	0.000
23	A	24	GLU	-1	-0.862	-0.900	12.551	-22.715	-22.715	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.891	0.942	14.184	19.907	19.907	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.943	-0.969	18.107	-13.284	-13.284	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.909	0.952	16.538	17.340	17.340	0.000	0.000	0.000	0.000
27	A	28	ALA	0	0.054	0.035	19.519	0.663	0.663	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.813	0.888	19.649	15.851	15.851	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.906	0.961	24.106	12.009	12.009	0.000	0.000	0.000	0.000
30	A	31	LEU	0	0.031	0.013	22.954	0.580	0.580	0.000	0.000	0.000	0.000
31	A	32	VAL	0	0.012	0.018	24.385	0.442	0.442	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.920	0.962	27.118	10.872	10.872	0.000	0.000	0.000	0.000
33	A	34	LEU	0	-0.024	-0.021	29.195	0.383	0.383	0.000	0.000	0.000	0.000
34	A	35	TYR	0	-0.039	-0.036	29.265	0.305	0.305	0.000	0.000	0.000	0.000
35	A	36	ASN	0	-0.024	-0.017	29.622	0.345	0.345	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.975	-0.976	32.871	-8.992	-8.992	0.000	0.000	0.000	0.000
37	A	38	THR	0	-0.093	-0.025	34.033	0.282	0.282	0.000	0.000	0.000	0.000
38	A	39	LEU	0	0.038	0.007	36.661	0.042	0.042	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.940	-0.974	39.074	-7.761	-7.761	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.009	-0.010	40.657	-0.064	-0.064	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.917	-0.945	38.132	-8.269	-8.269	0.000	0.000	0.000	0.000
42	A	43	TYR	0	0.022	-0.005	37.006	-0.237	-0.237	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.868	-0.933	35.639	-8.700	-8.700	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.917	0.965	34.273	8.637	8.637	0.000	0.000	0.000	0.000
45	A	46	ARG	1	0.892	0.933	32.629	8.627	8.627	0.000	0.000	0.000	0.000
46	A	47	THR	0	0.012	0.003	30.990	-0.425	-0.425	0.000	0.000	0.000	0.000
47	A	48	GLY	0	-0.016	-0.009	29.796	-0.382	-0.382	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.001	0.000	28.455	-0.340	-0.340	0.000	0.000	0.000	0.000
49	A	50	LEU	0	0.001	-0.001	26.360	-0.533	-0.533	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.833	0.918	25.022	10.193	10.193	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.992	-0.973	23.889	-12.616	-12.616	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.067	-0.039	21.808	-0.634	-0.634	0.000	0.000	0.000	0.000
53	A	54	PHE	0	-0.021	-0.032	20.630	-0.669	-0.669	0.000	0.000	0.000	0.000
54	A	55	GLY	0	0.014	0.021	17.874	-0.024	-0.024	0.000	0.000	0.000	0.000
55	A	56	SER	0	-0.092	-0.071	18.763	0.293	0.293	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.015	-0.032	21.490	-0.028	-0.028	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.048	0.049	24.902	-0.040	-0.040	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.940	-0.970	28.009	-10.060	-10.060	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.898	0.951	31.346	8.743	8.743	0.000	0.000	0.000	0.000
60	A	61	LEU	0	0.013	0.008	26.881	-0.223	-0.223	0.000	0.000	0.000	0.000
61	A	62	PHE	0	-0.039	-0.016	31.001	0.197	0.197	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.014	0.012	26.963	-0.162	-0.162	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.874	-0.922	31.503	-8.506	-8.506	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.053	0.004	32.551	-0.275	-0.275	0.000	0.000	0.000	0.000
65	A	66	ASN	0	-0.020	-0.019	31.417	0.255	0.255	0.000	0.000	0.000	0.000
66	A	67	PHE	0	0.061	0.024	23.475	-0.055	-0.055	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.916	0.944	25.256	11.109	11.109	0.000	0.000	0.000	0.000
68	A	69	CYS	0	-0.036	0.006	20.525	-0.133	-0.133	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.831	-0.917	16.884	-16.754	-16.754	0.000	0.000	0.000	0.000
70	A	71	TYR	0	-0.006	-0.028	13.179	-0.035	-0.035	0.000	0.000	0.000	0.000
71	A	72	GLY	0	0.003	0.003	17.147	0.440	0.440	0.000	0.000	0.000	0.000
72	A	73	TYR	0	0.008	-0.036	12.040	-0.274	-0.274	0.000	0.000	0.000	0.000
73	A	74	ASN	0	-0.074	-0.033	11.457	-0.994	-0.994	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.026	0.002	15.113	-0.085	-0.085	0.000	0.000	0.000	0.000
75	A	76	HIS	0	0.001	0.029	15.005	1.155	1.155	0.000	0.000	0.000	0.000
76	A	77	VAL	0	-0.019	-0.011	19.963	0.090	0.090	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.051	0.034	23.538	0.038	0.038	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.886	-0.963	26.080	-10.501	-10.501	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.097	-0.053	29.697	0.175	0.175	0.000	0.000	0.000	0.000
80	A	81	PHE	0	0.050	0.035	26.142	0.101	0.101	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.027	0.010	29.651	0.237	0.237	0.000	0.000	0.000	0.000
82	A	83	MET	0	-0.031	-0.006	26.000	-0.346	-0.346	0.000	0.000	0.000	0.000
83	A	84	ASN	0	0.031	0.012	30.660	0.215	0.215	0.000	0.000	0.000	0.000
84	A	85	PHE	0	0.016	0.007	32.081	-0.257	-0.257	0.000	0.000	0.000	0.000
85	A	86	ASP	-1	-0.891	-0.936	31.731	-9.434	-9.434	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.016	0.003	28.384	-0.117	-0.117	0.000	0.000	0.000	0.000
87	A	88	VAL	0	-0.057	-0.049	23.406	-0.049	-0.049	0.000	0.000	0.000	0.000
88	A	89	ILE	0	0.023	0.008	19.561	-0.023	-0.023	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.008	0.017	18.390	-0.114	-0.114	0.000	0.000	0.000	0.000
90	A	91	ASP	-1	-0.667	-0.828	16.002	-18.636	-18.636	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.033	0.016	11.324	-0.786	-0.786	0.000	0.000	0.000	0.000
92	A	93	CYS	0	-0.039	-0.019	8.881	-2.376	-2.376	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.844	-0.919	11.287	-21.636	-21.636	0.000	0.000	0.000	0.000
94	A	95	VAL	0	-0.003	-0.004	13.576	0.401	0.401	0.000	0.000	0.000	0.000
95	A	96	ARG	1	0.823	0.915	14.515	19.868	19.868	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.003	-0.011	18.835	0.278	0.278	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.002	0.009	22.622	-0.007	-0.007	0.000	0.000	0.000	0.000
98	A	99	ASP	-1	-0.833	-0.934	25.140	-11.151	-11.151	0.000	0.000	0.000	0.000
99	A	100	HIS	0	-0.066	-0.047	28.588	0.173	0.173	0.000	0.000	0.000	0.000
100	A	101	CYS	0	-0.025	0.015	26.623	0.180	0.180	0.000	0.000	0.000	0.000
101	A	102	PHE	0	0.021	0.017	29.845	0.191	0.191	0.000	0.000	0.000	0.000
102	A	103	ILE	0	0.004	-0.011	26.203	-0.064	-0.064	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.003	-0.006	30.741	0.231	0.231	0.000	0.000	0.000	0.000
104	A	105	PRO	0	0.018	0.006	31.858	-0.249	-0.249	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.029	-0.007	31.579	0.054	0.054	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.077	-0.018	26.728	-0.085	-0.085	0.000	0.000	0.000	0.000
107	A	108	HIS	0	0.010	0.037	24.916	-0.498	-0.498	0.000	0.000	0.000	0.000
108	A	109	ILE	0	0.013	0.000	20.000	0.128	0.128	0.000	0.000	0.000	0.000
109	A	110	TYR	0	-0.039	-0.058	19.508	-0.179	-0.179	0.000	0.000	0.000	0.000
110	A	111	THR	0	-0.005	-0.015	14.004	-0.602	-0.602	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.013	0.010	14.496	-1.338	-1.338	0.000	0.000	0.000	0.000
112	A	113	THR	0	-0.051	-0.033	14.512	1.628	1.628	0.000	0.000	0.000	0.000
113	A	114	HIS	0	0.068	0.039	14.928	-1.319	-1.319	0.000	0.000	0.000	0.000
114	A	115	PRO	0	0.022	0.019	14.774	0.343	0.343	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.002	-0.021	17.151	0.866	0.866	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.825	-0.908	20.125	-13.257	-13.257	0.000	0.000	0.000	0.000
117	A	118	PRO	0	-0.021	-0.016	20.750	-0.471	-0.471	0.000	0.000	0.000	0.000
118	A	119	HIS	0	0.005	0.010	20.538	0.161	0.161	0.000	0.000	0.000	0.000
119	A	120	GLU	-1	-0.910	-0.968	16.891	-17.836	-17.836	0.000	0.000	0.000	0.000
120	A	121	ARG	1	0.852	0.944	17.140	13.313	13.313	0.000	0.000	0.000	0.000
121	A	122	ASN	0	-0.033	-0.030	18.599	-0.396	-0.396	0.000	0.000	0.000	0.000
122	A	123	SER	0	-0.063	-0.022	15.721	-0.213	-0.213	0.000	0.000	0.000	0.000
123	A	124	GLY	0	-0.006	0.002	16.363	-0.231	-0.231	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.075	-0.036	10.758	-1.050	-1.050	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.905	-0.947	11.788	-18.253	-18.253	0.000	0.000	0.000	0.000
126	A	127	TYR	0	-0.021	-0.041	9.863	-2.623	-2.623	0.000	0.000	0.000	0.000
127	A	128	GLY	0	0.033	0.014	10.148	2.369	2.369	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.910	0.949	10.532	18.037	18.037	0.000	0.000	0.000	0.000
129	A	130	PRO	0	0.056	0.031	10.933	1.385	1.385	0.000	0.000	0.000	0.000
130	A	131	VAL	0	-0.011	0.011	13.695	0.845	0.845	0.000	0.000	0.000	0.000
131	A	132	VAL	0	-0.020	-0.003	16.735	-0.237	-0.237	0.000	0.000	0.000	0.000
132	A	133	ILE	0	-0.011	-0.020	19.227	0.608	0.608	0.000	0.000	0.000	0.000
133	A	134	GLY	0	0.031	0.022	22.955	-0.156	-0.156	0.000	0.000	0.000	0.000
134	A	135	HIS	0	0.071	0.042	25.252	0.166	0.166	0.000	0.000	0.000	0.000
135	A	136	ASN	0	-0.061	-0.041	28.261	0.284	0.284	0.000	0.000	0.000	0.000
136	A	137	VAL	0	-0.014	0.014	27.074	0.232	0.232	0.000	0.000	0.000	0.000
137	A	138	TRP	0	-0.019	-0.006	30.227	0.229	0.229	0.000	0.000	0.000	0.000
138	A	139	ILE	0	0.025	0.002	26.184	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	140	GLY	0	0.010	0.001	30.567	0.160	0.160	0.000	0.000	0.000	0.000
140	A	141	GLY	0	0.035	-0.007	32.181	-0.245	-0.245	0.000	0.000	0.000	0.000
141	A	142	ARG	1	0.931	0.955	31.976	9.470	9.470	0.000	0.000	0.000	0.000
142	A	143	ALA	0	-0.033	0.010	29.200	-0.019	-0.019	0.000	0.000	0.000	0.000
143	A	144	VAL	0	0.016	0.005	25.133	-0.140	-0.140	0.000	0.000	0.000	0.000
144	A	145	ILE	0	-0.009	0.002	21.779	0.222	0.222	0.000	0.000	0.000	0.000
145	A	146	ASN	0	0.008	-0.006	21.152	-0.520	-0.520	0.000	0.000	0.000	0.000
146	A	147	PRO	0	0.039	0.009	15.770	-0.069	-0.069	0.000	0.000	0.000	0.000
147	A	148	GLY	0	-0.066	-0.035	15.678	0.329	0.329	0.000	0.000	0.000	0.000
148	A	149	VAL	0	-0.054	0.012	16.562	0.439	0.439	0.000	0.000	0.000	0.000
149	A	150	THR	0	0.023	0.005	18.985	-0.547	-0.547	0.000	0.000	0.000	0.000
150	A	151	ILE	0	-0.047	-0.027	21.049	0.689	0.689	0.000	0.000	0.000	0.000
151	A	152	GLY	0	0.019	-0.002	24.567	-0.174	-0.174	0.000	0.000	0.000	0.000
152	A	153	ASP	-1	-0.814	-0.915	26.491	-11.377	-11.377	0.000	0.000	0.000	0.000
153	A	154	ASN	0	-0.078	-0.055	28.762	0.385	0.385	0.000	0.000	0.000	0.000
154	A	155	ALA	0	-0.026	0.010	29.065	0.330	0.330	0.000	0.000	0.000	0.000
155	A	156	VAL	0	-0.013	-0.007	31.147	0.056	0.056	0.000	0.000	0.000	0.000
156	A	157	ILE	0	-0.036	-0.006	28.164	0.019	0.019	0.000	0.000	0.000	0.000
157	A	158	ALA	0	0.041	0.014	31.647	0.148	0.148	0.000	0.000	0.000	0.000
158	A	159	SER	0	0.034	0.000	33.433	-0.241	-0.241	0.000	0.000	0.000	0.000
159	A	160	GLY	0	-0.058	-0.022	33.510	0.154	0.154	0.000	0.000	0.000	0.000
160	A	161	ALA	0	-0.081	-0.024	30.900	-0.053	-0.053	0.000	0.000	0.000	0.000
161	A	162	VAL	0	0.024	0.016	27.387	-0.262	-0.262	0.000	0.000	0.000	0.000
162	A	163	VAL	0	0.007	-0.013	24.829	0.171	0.171	0.000	0.000	0.000	0.000
163	A	164	THR	0	-0.023	-0.016	23.897	-0.472	-0.472	0.000	0.000	0.000	0.000
164	A	165	LYS	1	0.960	0.983	23.013	10.632	10.632	0.000	0.000	0.000	0.000
165	A	166	ASP	-1	-0.805	-0.890	21.143	-14.641	-14.641	0.000	0.000	0.000	0.000
166	A	167	VAL	0	-0.081	-0.040	23.902	0.655	0.655	0.000	0.000	0.000	0.000
167	A	168	PRO	0	-0.010	-0.004	26.550	-0.210	-0.210	0.000	0.000	0.000	0.000
168	A	169	ALA	0	0.093	0.044	28.578	0.113	0.113	0.000	0.000	0.000	0.000
169	A	170	ASN	0	-0.065	-0.066	29.775	0.021	0.021	0.000	0.000	0.000	0.000
170	A	171	ALA	0	0.009	0.025	31.367	0.377	0.377	0.000	0.000	0.000	0.000
171	A	172	VAL	0	0.009	0.007	32.695	-0.104	-0.104	0.000	0.000	0.000	0.000
172	A	173	VAL	0	0.003	0.002	29.562	0.118	0.118	0.000	0.000	0.000	0.000
173	A	174	GLY	0	0.042	0.007	33.064	0.043	0.043	0.000	0.000	0.000	0.000
174	A	175	GLY	0	-0.010	0.001	34.478	0.046	0.046	0.000	0.000	0.000	0.000
175	A	176	ASN	0	0.008	0.011	31.176	-0.508	-0.508	0.000	0.000	0.000	0.000
176	A	177	PRO	0	0.055	0.019	28.997	0.179	0.179	0.000	0.000	0.000	0.000
177	A	178	ALA	0	-0.053	-0.009	29.575	0.332	0.332	0.000	0.000	0.000	0.000
178	A	179	LYS	1	0.917	0.949	30.742	8.323	8.323	0.000	0.000	0.000	0.000
179	A	180	VAL	0	0.064	0.023	31.988	0.058	0.058	0.000	0.000	0.000	0.000
180	A	181	ILE	0	-0.081	-0.044	34.227	0.232	0.232	0.000	0.000	0.000	0.000
181	A	182	LYS	1	0.936	0.966	36.878	8.051	8.051	0.000	0.000	0.000	0.000
182	A	183	TRP	0	0.055	0.031	32.453	-0.284	-0.284	0.000	0.000	0.000	0.000
183	A	184	LEU	0	-0.023	0.000	35.203	0.322	0.322	0.000	0.000	0.000	0.000
184	A	185	LYS	1	0.991	1.026	35.709	8.606	8.606	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)