FMO DATABASE

FMODB ID: MNL5Z

Calculation Name: 3FVW-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3FVW

Chain ID: A

ChEMBL ID:

UniProt ID: Q8DWD8

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	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	182
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1889394.972922
FMO2-HF: Nuclear repulsion	1820168.51707
FMO2-HF: Total energy	-69226.455852
FMO2-MP2: Total energy	-69433.523898

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:3:LYS)

Summations of interaction energy for fragment #1(A:3: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.
-386.314	-379.404	30.339	-18.089	-19.161	-0.183

Interaction energy analysis for fragmet #1(A:3:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.860 / q_NPA : 0.908

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	5	ILE	0	0.000	0.005	3.382	-2.091	0.633	-0.003	-1.263	-1.457	0.005
4	A	6	LEU	0	0.029	0.027	5.627	2.071	2.071	0.000	0.000	0.000	0.000
5	A	7	PHE	0	0.002	-0.016	9.314	0.185	0.185	0.000	0.000	0.000	0.000
6	A	8	ILE	0	0.050	0.017	11.924	1.128	1.128	0.000	0.000	0.000	0.000
7	A	9	VAL	0	0.016	0.005	15.395	0.142	0.142	0.000	0.000	0.000	0.000
8	A	10	GLY	0	0.020	0.021	18.427	0.506	0.506	0.000	0.000	0.000	0.000
9	A	11	SER	0	-0.085	-0.077	21.593	0.677	0.677	0.000	0.000	0.000	0.000
10	A	12	PHE	0	0.088	0.052	22.581	-0.250	-0.250	0.000	0.000	0.000	0.000
11	A	13	SER	0	-0.055	-0.009	24.932	0.043	0.043	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.874	-0.966	24.040	-12.131	-12.131	0.000	0.000	0.000	0.000
13	A	15	GLY	0	0.066	0.040	24.462	-0.328	-0.328	0.000	0.000	0.000	0.000
14	A	16	SER	0	-0.027	0.011	23.196	-0.021	-0.021	0.000	0.000	0.000	0.000
15	A	17	PHE	0	0.070	0.019	23.534	-0.407	-0.407	0.000	0.000	0.000	0.000
16	A	18	ASN	0	0.064	0.028	20.648	-0.761	-0.761	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.921	0.974	19.079	12.391	12.391	0.000	0.000	0.000	0.000
18	A	20	GLN	0	-0.063	-0.050	18.882	-0.675	-0.675	0.000	0.000	0.000	0.000
19	A	21	LEU	0	-0.022	-0.008	17.633	-0.291	-0.291	0.000	0.000	0.000	0.000
20	A	22	ALA	0	0.041	0.020	15.207	-0.760	-0.760	0.000	0.000	0.000	0.000
21	A	23	LYS	1	0.979	0.996	14.472	13.411	13.411	0.000	0.000	0.000	0.000
22	A	24	LYS	1	0.901	0.957	15.302	13.449	13.449	0.000	0.000	0.000	0.000
23	A	25	ALA	0	0.036	0.020	12.308	-0.639	-0.639	0.000	0.000	0.000	0.000
24	A	26	GLU	-1	-0.847	-0.930	10.663	-21.258	-21.258	0.000	0.000	0.000	0.000
25	A	27	THR	0	-0.032	-0.013	10.692	-0.855	-0.855	0.000	0.000	0.000	0.000
26	A	28	ILE	0	-0.053	-0.013	11.223	-0.261	-0.261	0.000	0.000	0.000	0.000
27	A	29	ILE	0	-0.033	0.012	5.765	-1.310	-1.310	0.000	0.000	0.000	0.000
28	A	30	GLY	0	-0.022	-0.005	7.896	-2.072	-2.072	0.000	0.000	0.000	0.000
29	A	31	ASP	-1	-0.923	-0.960	7.363	-28.846	-28.846	0.000	0.000	0.000	0.000
30	A	32	ARG	1	0.775	0.860	4.279	31.805	31.992	-0.001	-0.017	-0.169	0.000
31	A	33	ALA	0	-0.002	-0.021	2.302	-14.678	-12.307	2.282	-1.847	-2.807	-0.010
32	A	34	GLN	0	-0.024	0.005	3.137	7.742	7.728	0.015	0.702	-0.704	-0.001
33	A	35	VAL	0	-0.003	0.006	5.337	-0.487	-0.442	-0.001	-0.008	-0.035	0.000
34	A	36	SER	0	0.002	0.012	7.975	1.621	1.621	0.000	0.000	0.000	0.000
35	A	37	TYR	0	-0.064	-0.039	10.773	0.011	0.011	0.000	0.000	0.000	0.000
36	A	38	LEU	0	0.046	0.036	13.804	0.485	0.485	0.000	0.000	0.000	0.000
37	A	39	SER	0	-0.042	-0.038	15.695	0.624	0.624	0.000	0.000	0.000	0.000
38	A	40	TYR	0	-0.001	-0.021	19.327	0.141	0.141	0.000	0.000	0.000	0.000
39	A	41	ASP	-1	-0.948	-0.982	21.760	-11.621	-11.621	0.000	0.000	0.000	0.000
40	A	42	ARG	1	0.887	0.942	24.872	10.535	10.535	0.000	0.000	0.000	0.000
41	A	43	VAL	0	0.049	0.025	23.365	-0.237	-0.237	0.000	0.000	0.000	0.000
42	A	44	PRO	0	-0.012	0.022	26.651	0.260	0.260	0.000	0.000	0.000	0.000
43	A	45	PHE	0	0.009	-0.007	28.793	-0.271	-0.271	0.000	0.000	0.000	0.000
44	A	46	PHE	0	0.006	-0.015	28.169	0.175	0.175	0.000	0.000	0.000	0.000
45	A	47	ASN	0	-0.008	-0.034	30.274	0.253	0.253	0.000	0.000	0.000	0.000
46	A	48	GLN	0	0.084	0.033	32.585	0.051	0.051	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.955	-0.950	33.697	-7.897	-7.897	0.000	0.000	0.000	0.000
48	A	50	LEU	0	-0.052	-0.029	32.438	0.105	0.105	0.000	0.000	0.000	0.000
49	A	51	GLU	-1	-0.874	-0.955	29.376	-10.066	-10.066	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.044	-0.004	30.078	-0.185	-0.185	0.000	0.000	0.000	0.000
51	A	53	SER	0	-0.069	-0.028	31.935	0.178	0.178	0.000	0.000	0.000	0.000
52	A	54	VAL	0	-0.004	-0.008	26.718	-0.301	-0.301	0.000	0.000	0.000	0.000
53	A	55	HIS	0	0.002	0.003	27.031	0.237	0.237	0.000	0.000	0.000	0.000
54	A	56	PRO	0	0.002	0.000	25.067	-0.438	-0.438	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.868	-0.941	23.200	-10.832	-10.832	0.000	0.000	0.000	0.000
56	A	58	VAL	0	-0.016	-0.015	22.118	-0.505	-0.505	0.000	0.000	0.000	0.000
57	A	59	ALA	0	-0.065	-0.038	21.076	-0.485	-0.485	0.000	0.000	0.000	0.000
58	A	60	HIS	0	0.054	0.025	17.323	-0.430	-0.430	0.000	0.000	0.000	0.000
59	A	61	ALA	0	0.001	0.001	17.254	-0.745	-0.745	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.946	0.976	16.206	12.118	12.118	0.000	0.000	0.000	0.000
61	A	63	GLU	-1	-0.921	-0.955	15.183	-15.003	-15.003	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.916	-0.953	12.638	-19.533	-19.533	0.000	0.000	0.000	0.000
63	A	65	VAL	0	-0.056	-0.027	11.172	-1.769	-1.769	0.000	0.000	0.000	0.000
64	A	66	GLN	0	-0.059	-0.038	11.300	-0.872	-0.872	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.948	-0.989	9.544	-20.358	-20.358	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.089	-0.025	6.787	-2.783	-2.783	0.000	0.000	0.000	0.000
67	A	69	ASP	-1	-0.834	-0.917	2.464	-50.185	-47.011	1.858	-2.662	-2.370	-0.029
68	A	70	ALA	0	-0.028	-0.018	5.731	0.917	0.917	0.000	0.000	0.000	0.000
69	A	71	ILE	0	0.007	-0.002	7.245	1.228	1.228	0.000	0.000	0.000	0.000
70	A	72	TRP	0	0.002	-0.008	9.380	-0.811	-0.811	0.000	0.000	0.000	0.000
71	A	73	ILE	0	-0.014	0.006	11.696	0.884	0.884	0.000	0.000	0.000	0.000
72	A	74	PHE	0	0.036	0.015	12.690	0.646	0.646	0.000	0.000	0.000	0.000
73	A	75	SER	0	0.018	0.000	17.623	0.474	0.474	0.000	0.000	0.000	0.000
74	A	76	PRO	0	-0.067	-0.004	21.064	-0.028	-0.028	0.000	0.000	0.000	0.000
75	A	77	VAL	0	0.056	0.045	24.712	-0.126	-0.126	0.000	0.000	0.000	0.000
76	A	78	TYR	0	-0.043	-0.021	26.858	0.317	0.317	0.000	0.000	0.000	0.000
77	A	79	ASN	0	-0.034	-0.021	30.250	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	80	TYR	0	0.000	-0.017	30.167	0.259	0.259	0.000	0.000	0.000	0.000
79	A	81	ALA	0	0.045	0.045	28.485	-0.195	-0.195	0.000	0.000	0.000	0.000
80	A	82	ILE	0	-0.006	-0.005	23.150	-0.187	-0.187	0.000	0.000	0.000	0.000
81	A	83	PRO	0	-0.030	-0.024	23.775	0.412	0.412	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.053	0.027	25.687	-0.230	-0.230	0.000	0.000	0.000	0.000
83	A	85	PRO	0	0.004	-0.022	25.006	-0.089	-0.089	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.016	0.021	20.447	-0.241	-0.241	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.860	0.916	22.539	10.580	10.580	0.000	0.000	0.000	0.000
86	A	88	ASN	0	0.046	0.023	24.961	0.243	0.243	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.012	0.003	18.429	0.039	0.039	0.000	0.000	0.000	0.000
88	A	90	LEU	0	0.023	-0.001	18.615	-0.231	-0.231	0.000	0.000	0.000	0.000
89	A	91	ASP	-1	-0.820	-0.875	21.879	-11.018	-11.018	0.000	0.000	0.000	0.000
90	A	92	TRP	0	-0.022	-0.003	23.614	0.111	0.111	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.002	-0.010	17.298	-0.071	-0.071	0.000	0.000	0.000	0.000
92	A	94	SER	0	-0.042	-0.023	20.270	-0.240	-0.240	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.844	0.931	22.240	11.380	11.380	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.005	-0.014	22.877	-0.683	-0.683	0.000	0.000	0.000	0.000
95	A	97	LEU	0	-0.022	-0.026	18.214	0.139	0.139	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.866	-0.928	22.869	-10.324	-10.324	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.021	-0.017	26.123	0.157	0.157	0.000	0.000	0.000	0.000
98	A	100	SER	0	-0.107	-0.044	29.392	0.492	0.492	0.000	0.000	0.000	0.000
99	A	101	ASP	-1	-0.882	-0.950	27.872	-10.328	-10.328	0.000	0.000	0.000	0.000
100	A	102	PRO	0	-0.007	0.015	28.074	-0.396	-0.396	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.093	-0.043	28.660	-0.049	-0.049	0.000	0.000	0.000	0.000
102	A	104	GLY	0	0.029	0.034	25.634	-0.183	-0.183	0.000	0.000	0.000	0.000
103	A	105	PRO	0	-0.035	-0.023	20.135	-0.032	-0.032	0.000	0.000	0.000	0.000
104	A	106	SER	0	0.051	0.035	20.487	-0.111	-0.111	0.000	0.000	0.000	0.000
105	A	107	VAL	0	-0.003	-0.021	15.565	-0.432	-0.432	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.040	-0.035	15.074	-1.187	-1.187	0.000	0.000	0.000	0.000
107	A	109	GLN	0	-0.053	-0.022	16.373	0.268	0.268	0.000	0.000	0.000	0.000
108	A	110	ASP	-1	-0.890	-0.950	13.857	-18.789	-18.789	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.837	0.951	9.970	22.080	22.080	0.000	0.000	0.000	0.000
110	A	112	ILE	0	0.022	0.021	6.782	1.262	1.262	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.025	-0.010	10.084	-0.492	-0.492	0.000	0.000	0.000	0.000
112	A	114	THR	0	0.029	0.019	10.592	0.573	0.573	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.021	0.002	13.035	0.191	0.191	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.013	0.021	15.691	-0.426	-0.426	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.046	-0.021	17.557	0.412	0.412	0.000	0.000	0.000	0.000
116	A	118	VAL	0	-0.047	-0.034	21.097	0.015	0.015	0.000	0.000	0.000	0.000
117	A	119	ALA	0	-0.001	-0.010	23.740	0.407	0.407	0.000	0.000	0.000	0.000
118	A	120	ASN	0	-0.058	-0.039	27.225	-0.078	-0.078	0.000	0.000	0.000	0.000
119	A	121	GLY	0	0.082	0.045	29.073	0.299	0.299	0.000	0.000	0.000	0.000
120	A	122	ALA	0	0.035	0.022	29.384	-0.203	-0.203	0.000	0.000	0.000	0.000
121	A	123	SER	0	-0.046	0.002	27.341	-0.472	-0.472	0.000	0.000	0.000	0.000
122	A	124	PRO	0	-0.043	-0.035	25.534	0.354	0.354	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.930	-0.959	25.537	-12.358	-12.358	0.000	0.000	0.000	0.000
124	A	126	GLU	-1	-0.792	-0.908	27.165	-9.048	-9.048	0.000	0.000	0.000	0.000
125	A	127	VAL	0	-0.094	-0.034	23.731	-0.013	-0.013	0.000	0.000	0.000	0.000
126	A	128	PHE	0	0.001	-0.024	19.713	-0.142	-0.142	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.882	-0.932	22.999	-10.845	-10.845	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.851	-0.935	25.138	-11.118	-11.118	0.000	0.000	0.000	0.000
129	A	131	TYR	0	-0.002	-0.037	19.750	-0.205	-0.205	0.000	0.000	0.000	0.000
130	A	132	ARG	1	0.852	0.906	20.658	13.146	13.146	0.000	0.000	0.000	0.000
131	A	133	SER	0	-0.036	0.000	21.746	-0.109	-0.109	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.021	0.002	22.620	0.026	0.026	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.025	-0.018	16.632	-0.028	-0.028	0.000	0.000	0.000	0.000
134	A	136	PRO	0	0.027	0.016	18.976	-0.433	-0.433	0.000	0.000	0.000	0.000
135	A	137	PHE	0	-0.044	-0.004	20.023	0.198	0.198	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.091	-0.044	19.653	0.378	0.378	0.000	0.000	0.000	0.000
137	A	139	ARG	1	0.931	0.961	19.737	12.934	12.934	0.000	0.000	0.000	0.000
138	A	140	MET	0	0.034	0.064	14.026	-0.333	-0.333	0.000	0.000	0.000	0.000
139	A	141	HIS	0	-0.021	-0.017	12.021	1.348	1.348	0.000	0.000	0.000	0.000
140	A	142	LEU	0	-0.005	-0.013	12.886	-1.480	-1.480	0.000	0.000	0.000	0.000
141	A	143	VAL	0	-0.001	-0.003	9.686	0.379	0.379	0.000	0.000	0.000	0.000
142	A	144	ASP	-1	-0.883	-0.955	13.084	-15.431	-15.431	0.000	0.000	0.000	0.000
143	A	145	GLN	0	-0.045	-0.014	13.602	1.485	1.485	0.000	0.000	0.000	0.000
144	A	146	LEU	0	-0.045	-0.019	15.350	-0.690	-0.690	0.000	0.000	0.000	0.000
145	A	147	THR	0	0.032	0.015	16.304	0.996	0.996	0.000	0.000	0.000	0.000
146	A	148	GLY	0	0.001	-0.001	18.779	0.016	0.016	0.000	0.000	0.000	0.000
147	A	149	VAL	0	-0.056	-0.044	20.625	0.227	0.227	0.000	0.000	0.000	0.000
148	A	150	PRO	0	0.036	0.029	23.428	0.199	0.199	0.000	0.000	0.000	0.000
149	A	151	ILE	0	0.014	-0.011	26.597	-0.234	-0.234	0.000	0.000	0.000	0.000
150	A	152	ASN	0	0.030	0.027	28.903	0.045	0.045	0.000	0.000	0.000	0.000
151	A	153	SER	0	0.054	-0.004	30.901	0.026	0.026	0.000	0.000	0.000	0.000
152	A	154	GLU	-1	-0.860	-0.947	32.838	-9.032	-9.032	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.051	-0.010	29.824	0.118	0.118	0.000	0.000	0.000	0.000
154	A	156	TRP	0	0.005	0.022	31.689	-0.022	-0.022	0.000	0.000	0.000	0.000
155	A	157	SER	0	-0.005	0.002	34.419	0.149	0.149	0.000	0.000	0.000	0.000
156	A	158	THR	0	-0.059	-0.032	32.285	-0.081	-0.081	0.000	0.000	0.000	0.000
157	A	159	GLY	0	0.057	0.022	31.148	-0.092	-0.092	0.000	0.000	0.000	0.000
158	A	160	ILE	0	-0.044	-0.019	26.634	-0.366	-0.366	0.000	0.000	0.000	0.000
159	A	161	LEU	0	0.008	0.008	22.795	0.305	0.305	0.000	0.000	0.000	0.000
160	A	162	LYS	1	0.779	0.894	25.438	9.896	9.896	0.000	0.000	0.000	0.000
161	A	163	VAL	0	0.016	0.007	21.204	0.195	0.195	0.000	0.000	0.000	0.000
162	A	164	SER	0	0.033	0.022	24.224	-0.155	-0.155	0.000	0.000	0.000	0.000
163	A	165	ALA	0	0.064	0.007	22.817	-0.495	-0.495	0.000	0.000	0.000	0.000
164	A	166	GLU	-1	-0.904	-0.957	21.842	-12.238	-12.238	0.000	0.000	0.000	0.000
165	A	167	LYS	1	0.839	0.909	21.348	12.741	12.741	0.000	0.000	0.000	0.000
166	A	168	LEU	0	-0.047	-0.017	18.094	-0.631	-0.631	0.000	0.000	0.000	0.000
167	A	169	ALA	0	0.015	0.012	17.416	-1.046	-1.046	0.000	0.000	0.000	0.000
168	A	170	GLU	-1	-0.825	-0.901	16.401	-15.654	-15.654	0.000	0.000	0.000	0.000
169	A	171	LEU	0	-0.002	0.002	14.458	-0.918	-0.918	0.000	0.000	0.000	0.000
170	A	172	SER	0	-0.045	-0.027	12.809	-1.485	-1.485	0.000	0.000	0.000	0.000
171	A	173	ALA	0	0.067	0.038	11.500	-1.907	-1.907	0.000	0.000	0.000	0.000
172	A	174	GLN	0	0.001	0.013	11.376	-0.816	-0.816	0.000	0.000	0.000	0.000
173	A	175	ALA	0	0.001	-0.016	9.052	-1.568	-1.568	0.000	0.000	0.000	0.000
174	A	176	ASP	-1	-0.846	-0.907	7.272	-34.912	-34.912	0.000	0.000	0.000	0.000
175	A	177	ALA	0	-0.047	-0.017	7.095	-3.634	-3.634	0.000	0.000	0.000	0.000
176	A	178	LEU	0	-0.022	-0.013	5.734	-1.136	-1.136	0.000	0.000	0.000	0.000
177	A	179	LEU	0	0.010	-0.005	2.804	-4.752	-3.733	0.482	-0.231	-1.270	-0.001
178	A	180	SER	0	0.007	-0.006	2.855	-14.036	-12.349	0.261	-0.878	-1.070	-0.011
179	A	181	ALA	0	-0.073	-0.022	5.589	0.099	0.099	0.000	0.000	0.000	0.000
180	A	182	ILE	0	-0.014	-0.019	2.260	-0.476	0.921	1.675	-0.597	-2.475	-0.007
181	A	183	GLU	-1	-0.891	-0.889	1.756	-144.931	-150.679	23.771	-11.267	-6.757	-0.129
182	A	184	ASN	0	-0.083	-0.039	4.374	7.442	7.510	0.000	-0.021	-0.047	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:3:LYS)