FMO DATABASE

FMODB ID: 8519Y

Calculation Name: 4M85-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4M85

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

Base Structure: X-ray

Registration Date: 2023-09-20

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	OptAll
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. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2173814.642942
FMO2-HF: Nuclear repulsion	2098080.130861
FMO2-HF: Total energy	-75734.51208
FMO2-MP2: Total energy	-75954.425005

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:SER)

Summations of interaction energy for fragment #1(A:-2:SER)

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.
-37.997	-48.789	37.079	-14.977	-11.31	-0.077

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.029 / q_NPA : -0.047

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	0	ALA	0	-0.008	0.001	3.854	0.111	2.078	-0.011	-1.018	-0.938	0.005
4	A	1	MET	0	-0.041	-0.018	6.586	0.045	0.045	0.000	0.000	0.000	0.000
5	A	2	ILE	0	-0.010	0.007	8.980	0.134	0.134	0.000	0.000	0.000	0.000
6	A	3	ARG	1	0.670	0.783	9.437	-0.616	-0.616	0.000	0.000	0.000	0.000
7	A	4	GLN	0	0.047	0.013	13.529	0.001	0.001	0.000	0.000	0.000	0.000
8	A	5	ALA	0	-0.020	0.007	14.485	0.066	0.066	0.000	0.000	0.000	0.000
9	A	6	ARG	1	0.850	0.900	8.581	-0.936	-0.936	0.000	0.000	0.000	0.000
10	A	7	PRO	0	0.053	0.021	16.102	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	8	GLU	-1	-0.878	-0.942	14.204	0.429	0.429	0.000	0.000	0.000	0.000
12	A	9	ASP	-1	-0.749	-0.838	12.620	0.539	0.539	0.000	0.000	0.000	0.000
13	A	10	ARG	1	0.910	0.949	15.032	-0.296	-0.296	0.000	0.000	0.000	0.000
14	A	11	PHE	0	0.010	0.019	16.349	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	12	ASP	-1	-0.930	-0.954	13.288	0.191	0.191	0.000	0.000	0.000	0.000
16	A	13	ILE	0	-0.013	-0.018	16.368	-0.055	-0.055	0.000	0.000	0.000	0.000
17	A	14	ALA	0	0.078	0.038	18.313	-0.034	-0.034	0.000	0.000	0.000	0.000
18	A	15	LYS	1	0.863	0.928	16.829	-0.162	-0.162	0.000	0.000	0.000	0.000
19	A	16	LEU	0	-0.069	-0.044	15.792	-0.032	-0.032	0.000	0.000	0.000	0.000
20	A	17	VAL	0	0.015	0.005	20.278	-0.018	-0.018	0.000	0.000	0.000	0.000
21	A	18	TYR	0	0.039	0.028	23.503	-0.012	-0.012	0.000	0.000	0.000	0.000
22	A	19	MET	0	-0.090	-0.049	21.041	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	20	VAL	0	0.031	0.026	23.963	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	21	TRP	0	0.059	0.010	26.540	0.004	0.004	0.000	0.000	0.000	0.000
25	A	22	ASP	-1	-0.811	-0.894	28.402	-0.029	-0.029	0.000	0.000	0.000	0.000
26	A	23	ASP	-1	-0.927	-0.965	27.041	-0.088	-0.088	0.000	0.000	0.000	0.000
27	A	24	MET	0	-0.092	-0.053	30.331	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	25	GLU	-1	-0.963	-0.987	32.588	-0.040	-0.040	0.000	0.000	0.000	0.000
29	A	26	LEU	0	0.012	0.026	31.796	0.004	0.004	0.000	0.000	0.000	0.000
30	A	27	GLU	-1	-0.835	-0.918	35.013	-0.010	-0.010	0.000	0.000	0.000	0.000
31	A	28	LEU	0	-0.024	-0.003	32.515	0.001	0.001	0.000	0.000	0.000	0.000
32	A	29	VAL	0	-0.067	-0.035	30.196	0.006	0.006	0.000	0.000	0.000	0.000
33	A	30	LYS	1	0.785	0.893	32.908	0.036	0.036	0.000	0.000	0.000	0.000
34	A	31	HIS	0	-0.071	-0.033	35.470	0.000	0.000	0.000	0.000	0.000	0.000
35	A	32	LEU	0	-0.030	0.001	34.403	0.004	0.004	0.000	0.000	0.000	0.000
36	A	33	PRO	0	-0.019	-0.013	33.078	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	34	LYS	1	0.871	0.914	28.332	0.020	0.020	0.000	0.000	0.000	0.000
38	A	35	ASP	-1	-0.949	-0.966	27.323	0.073	0.073	0.000	0.000	0.000	0.000
39	A	36	MET	0	0.055	0.035	27.925	0.010	0.010	0.000	0.000	0.000	0.000
40	A	37	VAL	0	0.004	0.004	28.828	0.004	0.004	0.000	0.000	0.000	0.000
41	A	38	LEU	0	-0.033	-0.017	22.880	0.001	0.001	0.000	0.000	0.000	0.000
42	A	39	ASP	-1	-0.813	-0.885	25.312	0.108	0.108	0.000	0.000	0.000	0.000
43	A	40	ALA	0	0.014	0.001	26.979	0.009	0.009	0.000	0.000	0.000	0.000
44	A	41	ILE	0	0.006	0.011	23.888	0.004	0.004	0.000	0.000	0.000	0.000
45	A	42	GLU	-1	-0.901	-0.966	21.384	0.172	0.172	0.000	0.000	0.000	0.000
46	A	43	LYS	1	0.824	0.895	23.571	-0.085	-0.085	0.000	0.000	0.000	0.000
47	A	44	SER	0	0.002	0.001	26.367	0.003	0.003	0.000	0.000	0.000	0.000
48	A	45	CYS	0	-0.097	-0.040	21.437	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	46	VAL	0	-0.119	-0.067	21.431	0.018	0.018	0.000	0.000	0.000	0.000
50	A	47	ASP	-1	-0.851	-0.926	24.382	0.142	0.142	0.000	0.000	0.000	0.000
51	A	48	ALA	0	0.003	0.002	27.986	-0.008	-0.008	0.000	0.000	0.000	0.000
52	A	49	THR	0	-0.072	-0.020	28.204	0.001	0.001	0.000	0.000	0.000	0.000
53	A	50	TYR	0	0.006	-0.028	27.762	-0.009	-0.009	0.000	0.000	0.000	0.000
54	A	51	ARG	1	0.784	0.865	28.070	0.002	0.002	0.000	0.000	0.000	0.000
55	A	52	THR	0	0.031	0.000	23.681	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	53	PHE	0	-0.015	0.015	23.205	0.017	0.017	0.000	0.000	0.000	0.000
57	A	54	TYR	0	0.049	0.006	19.298	-0.008	-0.008	0.000	0.000	0.000	0.000
58	A	55	GLN	0	-0.001	-0.001	20.473	-0.018	-0.018	0.000	0.000	0.000	0.000
59	A	56	HIS	1	0.781	0.908	22.433	-0.065	-0.065	0.000	0.000	0.000	0.000
60	A	57	ILE	0	-0.008	0.005	17.944	-0.023	-0.023	0.000	0.000	0.000	0.000
61	A	58	LEU	0	-0.009	0.016	16.793	0.024	0.024	0.000	0.000	0.000	0.000
62	A	59	VAL	0	-0.007	-0.018	12.173	-0.026	-0.026	0.000	0.000	0.000	0.000
63	A	60	TYR	0	0.003	-0.013	10.078	0.002	0.002	0.000	0.000	0.000	0.000
64	A	61	GLU	-1	-0.739	-0.830	5.947	1.229	1.229	0.000	0.000	0.000	0.000
65	A	62	VAL	0	-0.024	-0.045	5.679	-0.532	-0.532	0.000	0.000	0.000	0.000
66	A	63	GLU	-1	-0.842	-0.886	1.645	-37.399	-50.172	34.051	-13.561	-7.717	-0.094
67	A	64	ASN	0	-0.051	-0.023	2.289	-1.590	-1.659	3.040	-0.390	-2.581	0.012
68	A	65	LYS	1	0.989	1.004	4.839	-1.141	-1.058	-0.001	-0.008	-0.074	0.000
69	A	66	VAL	0	0.058	0.035	8.150	-0.091	-0.091	0.000	0.000	0.000	0.000
70	A	67	ALA	0	-0.007	0.001	9.944	-0.108	-0.108	0.000	0.000	0.000	0.000
71	A	68	GLY	0	-0.011	-0.032	11.687	-0.053	-0.053	0.000	0.000	0.000	0.000
72	A	69	CYS	0	-0.006	0.010	14.299	0.049	0.049	0.000	0.000	0.000	0.000
73	A	70	ILE	0	-0.047	-0.010	17.073	-0.039	-0.039	0.000	0.000	0.000	0.000
74	A	71	ILE	0	0.031	0.022	20.270	0.025	0.025	0.000	0.000	0.000	0.000
75	A	72	SER	0	-0.023	-0.019	23.071	-0.017	-0.017	0.000	0.000	0.000	0.000
76	A	73	TYR	0	-0.053	-0.057	25.867	0.013	0.013	0.000	0.000	0.000	0.000
77	A	74	SER	0	-0.009	-0.020	28.809	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	75	GLY	0	0.055	0.018	32.274	0.003	0.003	0.000	0.000	0.000	0.000
79	A	76	GLU	-1	-0.804	-0.860	35.053	0.014	0.014	0.000	0.000	0.000	0.000
80	A	77	ASN	0	-0.065	-0.049	34.476	0.007	0.007	0.000	0.000	0.000	0.000
81	A	78	GLU	-1	-0.742	-0.841	33.724	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	79	LEU	0	0.050	0.007	34.657	0.004	0.004	0.000	0.000	0.000	0.000
83	A	80	LYS	1	0.852	0.935	34.642	-0.035	-0.035	0.000	0.000	0.000	0.000
84	A	81	TYR	0	-0.044	-0.028	30.937	0.010	0.010	0.000	0.000	0.000	0.000
85	A	82	GLU	-1	-0.698	-0.804	32.517	0.023	0.023	0.000	0.000	0.000	0.000
86	A	83	LYS	1	0.858	0.895	34.214	-0.026	-0.026	0.000	0.000	0.000	0.000
87	A	84	ALA	0	-0.018	-0.009	32.350	0.002	0.002	0.000	0.000	0.000	0.000
88	A	85	TRP	0	0.060	0.019	28.940	0.008	0.008	0.000	0.000	0.000	0.000
89	A	86	GLU	-1	-0.851	-0.912	33.468	0.035	0.035	0.000	0.000	0.000	0.000
90	A	87	LEU	0	-0.074	-0.036	33.937	0.000	0.000	0.000	0.000	0.000	0.000
91	A	88	LEU	0	0.000	0.034	29.569	0.006	0.006	0.000	0.000	0.000	0.000
92	A	89	ASP	-1	-0.880	-0.933	32.042	0.083	0.083	0.000	0.000	0.000	0.000
93	A	90	LEU	0	-0.046	-0.010	30.846	0.005	0.005	0.000	0.000	0.000	0.000
94	A	91	PRO	0	0.029	0.010	33.659	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	92	GLU	-1	-0.850	-0.957	36.652	0.037	0.037	0.000	0.000	0.000	0.000
96	A	93	GLU	-1	-0.955	-0.978	37.540	0.027	0.027	0.000	0.000	0.000	0.000
97	A	94	ILE	0	0.031	0.005	32.521	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	95	LYS	1	0.844	0.930	36.427	-0.056	-0.056	0.000	0.000	0.000	0.000
99	A	96	GLN	0	-0.062	-0.028	38.413	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	97	TYR	0	-0.018	-0.012	37.765	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	98	GLY	0	-0.028	0.005	39.412	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	99	THR	0	-0.100	-0.077	35.433	0.003	0.003	0.000	0.000	0.000	0.000
103	A	100	PRO	0	0.013	0.000	31.647	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	101	LEU	0	-0.002	-0.002	30.232	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	102	PRO	0	-0.011	0.002	34.630	0.000	0.000	0.000	0.000	0.000	0.000
106	A	103	VAL	0	-0.041	-0.008	37.464	0.000	0.000	0.000	0.000	0.000	0.000
107	A	104	LYS	1	0.767	0.873	36.947	0.009	0.009	0.000	0.000	0.000	0.000
108	A	105	GLU	-1	-0.799	-0.891	32.762	-0.025	-0.025	0.000	0.000	0.000	0.000
109	A	106	ALA	0	-0.038	-0.005	33.938	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	107	LYS	1	0.820	0.899	36.073	0.041	0.041	0.000	0.000	0.000	0.000
111	A	108	ASP	-1	-0.838	-0.936	37.255	-0.006	-0.006	0.000	0.000	0.000	0.000
112	A	109	ASP	-1	-0.848	-0.913	38.617	-0.023	-0.023	0.000	0.000	0.000	0.000
113	A	110	GLU	-1	-0.745	-0.833	34.122	-0.041	-0.041	0.000	0.000	0.000	0.000
114	A	111	TYR	0	-0.014	-0.002	26.270	0.010	0.010	0.000	0.000	0.000	0.000
115	A	112	TYR	0	-0.018	-0.014	30.433	-0.013	-0.013	0.000	0.000	0.000	0.000
116	A	113	ILE	0	-0.041	-0.036	24.758	0.005	0.005	0.000	0.000	0.000	0.000
117	A	114	GLU	-1	-0.784	-0.835	26.509	-0.009	-0.009	0.000	0.000	0.000	0.000
118	A	115	THR	0	0.009	-0.014	22.367	-0.013	-0.013	0.000	0.000	0.000	0.000
119	A	116	ILE	0	-0.019	-0.023	20.793	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	117	ALA	0	0.029	0.028	19.916	-0.012	-0.012	0.000	0.000	0.000	0.000
121	A	118	THR	0	-0.053	-0.052	15.113	-0.031	-0.031	0.000	0.000	0.000	0.000
122	A	119	PHE	0	0.081	0.063	13.946	-0.023	-0.023	0.000	0.000	0.000	0.000
123	A	120	ALA	0	0.025	0.003	16.402	-0.064	-0.064	0.000	0.000	0.000	0.000
124	A	121	ALA	0	0.014	0.010	13.918	-0.031	-0.031	0.000	0.000	0.000	0.000
125	A	122	TYR	0	0.005	-0.007	7.989	-0.088	-0.088	0.000	0.000	0.000	0.000
126	A	123	ARG	1	0.934	0.971	13.959	0.197	0.197	0.000	0.000	0.000	0.000
127	A	124	GLY	0	0.013	0.012	16.945	-0.054	-0.054	0.000	0.000	0.000	0.000
128	A	125	ARG	1	0.889	0.937	9.793	1.233	1.233	0.000	0.000	0.000	0.000
129	A	126	GLY	0	0.015	-0.002	15.493	-0.041	-0.041	0.000	0.000	0.000	0.000
130	A	127	ILE	0	-0.004	0.002	12.135	0.015	0.015	0.000	0.000	0.000	0.000
131	A	128	ALA	0	0.086	0.045	16.078	0.034	0.034	0.000	0.000	0.000	0.000
132	A	129	THR	0	0.011	0.007	19.445	0.019	0.019	0.000	0.000	0.000	0.000
133	A	130	LYS	1	0.887	0.970	14.769	0.665	0.665	0.000	0.000	0.000	0.000
134	A	131	LEU	0	0.026	0.016	14.967	0.016	0.016	0.000	0.000	0.000	0.000
135	A	132	LEU	0	0.029	0.020	18.254	0.028	0.028	0.000	0.000	0.000	0.000
136	A	133	THR	0	-0.052	-0.043	20.837	0.018	0.018	0.000	0.000	0.000	0.000
137	A	134	SER	0	-0.017	-0.018	18.004	0.010	0.010	0.000	0.000	0.000	0.000
138	A	135	LEU	0	0.000	0.008	19.997	0.021	0.021	0.000	0.000	0.000	0.000
139	A	136	LEU	0	-0.003	0.009	22.020	0.015	0.015	0.000	0.000	0.000	0.000
140	A	137	GLU	-1	-1.004	-0.996	22.179	-0.087	-0.087	0.000	0.000	0.000	0.000
141	A	138	SER	0	-0.029	-0.027	21.758	0.018	0.018	0.000	0.000	0.000	0.000
142	A	139	ASN	0	0.018	-0.001	23.716	0.013	0.013	0.000	0.000	0.000	0.000
143	A	140	THR	0	0.030	0.022	27.489	0.001	0.001	0.000	0.000	0.000	0.000
144	A	141	HIS	0	-0.079	-0.029	29.889	0.003	0.003	0.000	0.000	0.000	0.000
145	A	142	VAL	0	-0.008	0.001	30.396	0.007	0.007	0.000	0.000	0.000	0.000
146	A	143	LYS	1	0.767	0.890	32.579	0.027	0.027	0.000	0.000	0.000	0.000
147	A	144	TRP	0	0.052	0.010	25.173	0.005	0.005	0.000	0.000	0.000	0.000
148	A	145	SER	0	-0.080	-0.065	30.992	-0.004	-0.004	0.000	0.000	0.000	0.000
149	A	146	LEU	0	0.015	0.012	27.935	0.000	0.000	0.000	0.000	0.000	0.000
150	A	147	ASN	0	0.030	0.012	31.022	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	148	CYS	0	-0.044	-0.014	31.233	-0.008	-0.008	0.000	0.000	0.000	0.000
152	A	149	ASP	-1	-0.755	-0.866	31.868	-0.085	-0.085	0.000	0.000	0.000	0.000
153	A	150	ILE	0	-0.039	-0.024	33.712	-0.007	-0.007	0.000	0.000	0.000	0.000
154	A	151	ASN	0	-0.054	-0.032	34.584	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	152	ASN	0	0.003	0.010	27.483	-0.017	-0.017	0.000	0.000	0.000	0.000
156	A	153	GLU	-1	-0.782	-0.889	31.504	-0.139	-0.139	0.000	0.000	0.000	0.000
157	A	154	ALA	0	0.014	0.002	28.182	-0.005	-0.005	0.000	0.000	0.000	0.000
158	A	155	ALA	0	-0.002	0.005	27.597	-0.011	-0.011	0.000	0.000	0.000	0.000
159	A	156	LEU	0	0.050	0.022	28.556	0.000	0.000	0.000	0.000	0.000	0.000
160	A	157	LYS	1	0.776	0.871	30.714	0.144	0.144	0.000	0.000	0.000	0.000
161	A	158	LEU	0	-0.050	-0.016	23.664	-0.007	-0.007	0.000	0.000	0.000	0.000
162	A	159	TYR	0	0.067	0.008	25.675	-0.006	-0.006	0.000	0.000	0.000	0.000
163	A	160	LYS	1	0.889	0.952	29.418	0.096	0.096	0.000	0.000	0.000	0.000
164	A	161	LYS	1	0.908	0.963	26.115	0.229	0.229	0.000	0.000	0.000	0.000
165	A	162	VAL	0	-0.056	-0.031	25.215	-0.007	-0.007	0.000	0.000	0.000	0.000
166	A	163	GLY	0	0.024	0.019	28.614	0.006	0.006	0.000	0.000	0.000	0.000
167	A	164	PHE	0	-0.006	0.001	27.910	0.009	0.009	0.000	0.000	0.000	0.000
168	A	165	ILE	0	-0.019	-0.018	33.056	-0.003	-0.003	0.000	0.000	0.000	0.000
169	A	166	SER	0	0.004	-0.018	36.353	-0.002	-0.002	0.000	0.000	0.000	0.000
170	A	167	ASP	-1	-0.824	-0.899	38.265	-0.040	-0.040	0.000	0.000	0.000	0.000
171	A	168	GLY	0	0.036	0.020	40.085	0.005	0.005	0.000	0.000	0.000	0.000
172	A	169	GLN	0	-0.028	-0.010	39.841	-0.008	-0.008	0.000	0.000	0.000	0.000
173	A	170	ILE	0	0.013	0.011	37.483	0.004	0.004	0.000	0.000	0.000	0.000
174	A	171	GLU	-1	-0.818	-0.900	39.108	-0.034	-0.034	0.000	0.000	0.000	0.000
175	A	172	LEU	0	-0.016	-0.005	34.699	0.004	0.004	0.000	0.000	0.000	0.000
176	A	173	TYR	0	0.033	-0.015	34.607	-0.002	-0.002	0.000	0.000	0.000	0.000
177	A	174	LYS	1	0.820	0.905	38.594	0.027	0.027	0.000	0.000	0.000	0.000
178	A	175	HIS	0	0.006	0.029	34.751	-0.005	-0.005	0.000	0.000	0.000	0.000
179	A	176	MET	0	-0.007	-0.009	38.171	0.004	0.004	0.000	0.000	0.000	0.000
180	A	177	TYR	0	0.039	0.015	32.160	-0.008	-0.008	0.000	0.000	0.000	0.000
181	A	178	HIS	0	-0.048	-0.039	35.616	0.002	0.002	0.000	0.000	0.000	0.000
182	A	179	HIS	1	0.812	0.895	35.188	0.041	0.041	0.000	0.000	0.000	0.000
183	A	180	LEU	0	-0.074	-0.041	32.014	-0.003	-0.003	0.000	0.000	0.000	0.000
184	A	181	ILE	0	0.021	0.006	33.860	0.004	0.004	0.000	0.000	0.000	0.000
185	A	182	VAL	0	0.023	0.021	29.842	-0.003	-0.003	0.000	0.000	0.000	0.000

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