FMO DATABASE

FMODB ID: G58Z1

Calculation Name: 3UMF-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3UMF

Chain ID: A

ChEMBL ID:

UniProt ID: G4V9S0

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	194
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2103972.239506
FMO2-HF: Nuclear repulsion	2026502.573157
FMO2-HF: Total energy	-77469.666349
FMO2-MP2: Total energy	-77693.354598

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:GLN)

Summations of interaction energy for fragment #1(A:4:GLN)

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.
-15.677	-7.838	4.07	-4.231	-7.677	0.031

Interaction energy analysis for fragmet #1(A:4:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.110 / q_NPA : 0.051

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	6	LEU	0	-0.052	-0.032	1.959	-12.228	-6.489	3.957	-3.878	-5.817	0.029
4	A	7	ALA	0	0.031	0.022	3.361	-2.774	-2.378	0.025	0.149	-0.571	0.000
5	A	8	LYS	1	0.876	0.930	4.914	-1.646	-1.532	-0.001	-0.007	-0.105	0.000
6	A	9	ALA	0	-0.037	-0.013	6.623	0.005	0.005	0.000	0.000	0.000	0.000
7	A	10	LYS	1	0.938	0.981	8.278	-0.639	-0.639	0.000	0.000	0.000	0.000
8	A	11	VAL	0	0.027	0.011	9.906	0.077	0.077	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.030	0.017	12.644	-0.123	-0.123	0.000	0.000	0.000	0.000
10	A	13	PHE	0	0.017	0.017	13.372	0.035	0.035	0.000	0.000	0.000	0.000
11	A	14	VAL	0	0.013	0.013	18.005	-0.034	-0.034	0.000	0.000	0.000	0.000
12	A	15	LEU	0	0.002	-0.003	21.519	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	16	GLY	0	0.052	0.004	24.290	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	17	GLY	0	0.009	0.024	27.891	0.005	0.005	0.000	0.000	0.000	0.000
15	A	18	PRO	0	0.003	-0.011	30.547	0.008	0.008	0.000	0.000	0.000	0.000
16	A	19	GLY	0	0.050	0.022	33.832	-0.005	-0.005	0.000	0.000	0.000	0.000
17	A	20	SER	0	-0.028	-0.011	30.450	0.004	0.004	0.000	0.000	0.000	0.000
18	A	21	GLY	0	0.031	0.017	32.157	0.001	0.001	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.871	0.916	25.200	-0.190	-0.190	0.000	0.000	0.000	0.000
20	A	23	GLY	0	0.011	0.012	27.043	0.017	0.017	0.000	0.000	0.000	0.000
21	A	24	THR	0	0.064	0.026	27.668	0.010	0.010	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.011	-0.013	27.496	0.015	0.015	0.000	0.000	0.000	0.000
23	A	26	CYS	0	-0.009	0.000	23.394	0.016	0.016	0.000	0.000	0.000	0.000
24	A	27	GLU	-1	-0.913	-0.946	24.145	0.238	0.238	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.923	0.964	26.276	-0.152	-0.152	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.018	-0.006	22.521	0.003	0.003	0.000	0.000	0.000	0.000
27	A	30	VAL	0	0.001	0.011	20.595	0.015	0.015	0.000	0.000	0.000	0.000
28	A	31	GLN	0	-0.035	-0.007	22.830	0.006	0.006	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.886	0.954	25.930	-0.198	-0.198	0.000	0.000	0.000	0.000
30	A	33	PHE	0	-0.050	-0.043	20.893	-0.017	-0.017	0.000	0.000	0.000	0.000
31	A	34	HIS	0	-0.023	0.003	20.489	0.048	0.048	0.000	0.000	0.000	0.000
32	A	35	PHE	0	-0.030	-0.013	17.607	0.063	0.063	0.000	0.000	0.000	0.000
33	A	36	ASN	0	0.017	0.016	13.390	-0.124	-0.124	0.000	0.000	0.000	0.000
34	A	37	HIS	0	-0.033	-0.023	16.289	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	38	LEU	0	-0.009	-0.002	12.070	0.022	0.022	0.000	0.000	0.000	0.000
36	A	39	SER	0	0.052	0.023	16.787	-0.053	-0.053	0.000	0.000	0.000	0.000
37	A	40	SER	0	0.033	0.008	18.148	0.020	0.020	0.000	0.000	0.000	0.000
38	A	41	GLY	0	0.029	0.014	19.134	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	42	ASP	-1	-0.853	-0.931	20.119	0.295	0.295	0.000	0.000	0.000	0.000
40	A	43	LEU	0	-0.048	-0.028	14.237	0.010	0.010	0.000	0.000	0.000	0.000
41	A	44	LEU	0	0.015	0.006	17.995	-0.022	-0.022	0.000	0.000	0.000	0.000
42	A	45	ARG	1	0.961	0.990	20.128	-0.221	-0.221	0.000	0.000	0.000	0.000
43	A	46	ALA	0	-0.032	-0.023	18.441	-0.018	-0.018	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.820	-0.893	16.384	0.154	0.154	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.022	0.017	19.250	-0.030	-0.030	0.000	0.000	0.000	0.000
46	A	49	GLN	0	-0.090	-0.051	22.693	-0.030	-0.030	0.000	0.000	0.000	0.000
47	A	50	SER	0	-0.018	-0.028	19.250	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	51	GLY	0	-0.008	0.004	21.199	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	52	SER	0	-0.021	-0.022	18.831	-0.032	-0.032	0.000	0.000	0.000	0.000
50	A	53	PRO	0	0.019	-0.015	20.634	0.002	0.002	0.000	0.000	0.000	0.000
51	A	54	LYS	1	1.007	1.003	14.547	0.072	0.072	0.000	0.000	0.000	0.000
52	A	55	GLY	0	0.067	0.043	20.525	0.004	0.004	0.000	0.000	0.000	0.000
53	A	56	LYS	1	0.881	0.935	21.711	-0.035	-0.035	0.000	0.000	0.000	0.000
54	A	57	GLU	-1	-0.850	-0.928	23.287	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	58	LEU	0	0.008	-0.002	19.184	0.002	0.002	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.954	0.978	23.649	-0.067	-0.067	0.000	0.000	0.000	0.000
57	A	60	ALA	0	0.014	0.011	26.673	0.000	0.000	0.000	0.000	0.000	0.000
58	A	61	MET	0	-0.032	-0.006	23.109	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	62	MET	0	-0.038	-0.030	23.238	0.004	0.004	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-1.003	-0.986	28.296	0.045	0.045	0.000	0.000	0.000	0.000
61	A	64	ARG	1	0.798	0.881	29.031	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	65	GLY	0	-0.025	0.003	31.287	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	66	GLU	-1	-0.882	-0.919	28.049	-0.012	-0.012	0.000	0.000	0.000	0.000
64	A	67	LEU	0	-0.015	-0.014	24.971	0.011	0.011	0.000	0.000	0.000	0.000
65	A	68	VAL	0	-0.017	-0.007	20.176	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	69	PRO	0	0.024	0.013	19.339	0.005	0.005	0.000	0.000	0.000	0.000
67	A	70	LEU	0	0.047	0.021	15.827	0.018	0.018	0.000	0.000	0.000	0.000
68	A	71	GLU	-1	-0.874	-0.953	14.581	-0.109	-0.109	0.000	0.000	0.000	0.000
69	A	72	VAL	0	-0.028	-0.006	14.064	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	73	VAL	0	0.023	0.006	14.755	0.055	0.055	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.006	-0.007	10.698	0.116	0.116	0.000	0.000	0.000	0.000
72	A	75	ALA	0	-0.015	-0.007	9.956	0.138	0.138	0.000	0.000	0.000	0.000
73	A	76	LEU	0	0.014	0.015	10.021	0.158	0.158	0.000	0.000	0.000	0.000
74	A	77	LEU	0	-0.007	-0.006	11.437	0.191	0.191	0.000	0.000	0.000	0.000
75	A	78	LYS	1	0.954	0.982	3.753	2.066	2.559	0.018	-0.172	-0.340	0.001
76	A	79	GLU	-1	-0.970	-0.982	6.952	1.572	1.572	0.000	0.000	0.000	0.000
77	A	80	ALA	0	0.012	-0.001	8.424	0.290	0.290	0.000	0.000	0.000	0.000
78	A	81	MET	0	-0.031	-0.021	7.309	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.026	-0.016	3.111	-0.343	0.596	0.072	-0.313	-0.698	0.001
80	A	83	LYS	1	0.918	0.972	6.123	-1.218	-1.218	0.000	0.000	0.000	0.000
81	A	84	LEU	0	-0.016	-0.015	9.648	-0.311	-0.311	0.000	0.000	0.000	0.000
82	A	85	VAL	0	-0.021	0.000	6.451	-0.408	-0.408	0.000	0.000	0.000	0.000
83	A	86	ASP	-1	-0.829	-0.915	9.383	1.695	1.695	0.000	0.000	0.000	0.000
84	A	87	LYS	1	0.925	0.986	11.664	-0.971	-0.971	0.000	0.000	0.000	0.000
85	A	88	ASN	0	0.068	0.015	13.361	-0.143	-0.143	0.000	0.000	0.000	0.000
86	A	89	CYS	0	0.009	0.014	10.798	0.130	0.130	0.000	0.000	0.000	0.000
87	A	90	HIS	0	-0.017	0.002	11.180	0.015	0.015	0.000	0.000	0.000	0.000
88	A	91	PHE	0	0.016	0.001	9.666	0.112	0.112	0.000	0.000	0.000	0.000
89	A	92	LEU	0	0.004	0.019	14.116	-0.082	-0.082	0.000	0.000	0.000	0.000
90	A	93	ILE	0	-0.003	-0.009	13.225	0.044	0.044	0.000	0.000	0.000	0.000
91	A	94	ASP	-1	-0.831	-0.909	17.239	0.198	0.198	0.000	0.000	0.000	0.000
92	A	95	GLY	0	-0.037	-0.015	20.856	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	96	TYR	0	-0.054	-0.006	14.564	-0.020	-0.020	0.000	0.000	0.000	0.000
94	A	97	PRO	0	0.011	0.008	17.305	0.027	0.027	0.000	0.000	0.000	0.000
95	A	98	ARG	1	0.952	0.945	19.064	-0.120	-0.120	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.895	-0.943	21.112	0.014	0.014	0.000	0.000	0.000	0.000
97	A	100	LEU	0	0.027	-0.002	19.834	0.010	0.010	0.000	0.000	0.000	0.000
98	A	101	ASP	-1	-0.838	-0.917	18.631	-0.029	-0.029	0.000	0.000	0.000	0.000
99	A	102	GLN	0	0.021	-0.011	16.555	0.004	0.004	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.020	0.013	14.936	0.025	0.025	0.000	0.000	0.000	0.000
101	A	104	ILE	0	0.056	0.027	14.008	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	105	LYS	1	0.914	0.949	12.818	0.071	0.071	0.000	0.000	0.000	0.000
103	A	106	PHE	0	0.034	0.021	10.467	-0.074	-0.074	0.000	0.000	0.000	0.000
104	A	107	GLU	-1	-0.811	-0.901	9.004	0.008	0.008	0.000	0.000	0.000	0.000
105	A	108	LYS	1	0.880	0.967	8.839	0.355	0.355	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.961	-0.987	7.272	-1.062	-1.062	0.000	0.000	0.000	0.000
107	A	110	VAL	0	-0.100	-0.053	5.030	-0.360	-0.360	0.000	0.000	0.000	0.000
108	A	111	CYS	0	-0.004	-0.009	4.570	-0.328	-0.170	-0.001	-0.010	-0.146	0.000
109	A	112	PRO	0	0.025	0.012	7.139	0.100	0.100	0.000	0.000	0.000	0.000
110	A	113	CYS	0	-0.089	-0.011	10.526	0.112	0.112	0.000	0.000	0.000	0.000
111	A	114	LEU	0	-0.058	-0.039	13.036	-0.065	-0.065	0.000	0.000	0.000	0.000
112	A	115	CYS	0	-0.038	-0.026	14.785	-0.040	-0.040	0.000	0.000	0.000	0.000
113	A	116	VAL	0	0.020	0.013	17.698	0.042	0.042	0.000	0.000	0.000	0.000
114	A	117	ILE	0	0.011	0.016	20.294	-0.022	-0.022	0.000	0.000	0.000	0.000
115	A	118	ASN	0	-0.011	-0.008	23.188	0.012	0.012	0.000	0.000	0.000	0.000
116	A	119	PHE	0	-0.021	-0.021	25.184	-0.007	-0.007	0.000	0.000	0.000	0.000
117	A	120	ASP	-1	-0.927	-0.961	28.880	0.069	0.069	0.000	0.000	0.000	0.000
118	A	121	VAL	0	-0.028	-0.014	31.735	0.001	0.001	0.000	0.000	0.000	0.000
119	A	122	SER	0	0.091	0.047	35.230	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	123	GLU	-1	-0.719	-0.839	38.085	0.045	0.045	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.870	-0.954	39.742	0.047	0.047	0.000	0.000	0.000	0.000
122	A	125	VAL	0	-0.029	-0.014	38.253	0.001	0.001	0.000	0.000	0.000	0.000
123	A	126	MET	0	-0.023	0.004	37.263	0.003	0.003	0.000	0.000	0.000	0.000
124	A	127	ARG	1	0.944	0.952	39.285	-0.041	-0.041	0.000	0.000	0.000	0.000
125	A	128	LYS	1	0.942	0.986	42.801	-0.058	-0.058	0.000	0.000	0.000	0.000
126	A	129	ARG	1	0.769	0.880	35.863	-0.092	-0.092	0.000	0.000	0.000	0.000
127	A	130	LEU	0	-0.062	-0.043	37.013	0.003	0.003	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.004	0.024	41.553	0.000	0.000	0.000	0.000	0.000	0.000
129	A	132	LYS	1	0.913	0.962	44.728	-0.043	-0.043	0.000	0.000	0.000	0.000
130	A	133	ARG	1	0.867	0.926	45.642	-0.060	-0.060	0.000	0.000	0.000	0.000
131	A	134	ALA	0	-0.038	-0.032	50.368	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	135	GLU	-1	-0.886	-0.927	52.541	0.031	0.031	0.000	0.000	0.000	0.000
133	A	136	THR	0	0.032	0.034	49.028	0.001	0.001	0.000	0.000	0.000	0.000
134	A	137	SER	0	0.035	0.006	50.772	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	138	ASN	0	0.019	-0.005	51.652	0.002	0.002	0.000	0.000	0.000	0.000
136	A	139	ARG	1	0.931	0.979	49.093	-0.048	-0.048	0.000	0.000	0.000	0.000
137	A	140	VAL	0	-0.076	-0.060	47.520	0.002	0.002	0.000	0.000	0.000	0.000
138	A	141	ASP	-1	-0.857	-0.919	47.517	0.037	0.037	0.000	0.000	0.000	0.000
139	A	142	ASP	-1	-0.855	-0.920	46.343	0.039	0.039	0.000	0.000	0.000	0.000
140	A	143	ASN	0	0.000	-0.005	43.802	0.000	0.000	0.000	0.000	0.000	0.000
141	A	144	GLU	-1	-0.880	-0.960	42.601	0.053	0.053	0.000	0.000	0.000	0.000
142	A	145	GLU	-1	-0.821	-0.915	42.678	0.038	0.038	0.000	0.000	0.000	0.000
143	A	146	THR	0	-0.018	-0.008	39.025	0.000	0.000	0.000	0.000	0.000	0.000
144	A	147	ILE	0	-0.041	-0.029	37.715	0.003	0.003	0.000	0.000	0.000	0.000
145	A	148	VAL	0	0.005	0.010	37.970	0.003	0.003	0.000	0.000	0.000	0.000
146	A	149	LYS	1	0.920	0.964	38.656	-0.032	-0.032	0.000	0.000	0.000	0.000
147	A	150	ARG	1	0.951	0.984	33.199	-0.076	-0.076	0.000	0.000	0.000	0.000
148	A	151	PHE	0	-0.036	-0.022	33.822	0.004	0.004	0.000	0.000	0.000	0.000
149	A	152	ARG	1	0.856	0.891	34.221	-0.035	-0.035	0.000	0.000	0.000	0.000
150	A	153	THR	0	0.006	0.014	31.895	-0.004	-0.004	0.000	0.000	0.000	0.000
151	A	154	PHE	0	-0.037	-0.024	26.524	0.000	0.000	0.000	0.000	0.000	0.000
152	A	155	ASN	0	-0.013	-0.018	29.762	-0.005	-0.005	0.000	0.000	0.000	0.000
153	A	156	GLU	-1	-0.850	-0.930	31.075	0.018	0.018	0.000	0.000	0.000	0.000
154	A	157	LEU	0	-0.027	-0.009	26.594	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	158	THR	0	-0.046	-0.027	25.464	-0.002	-0.002	0.000	0.000	0.000	0.000
156	A	159	LYS	1	0.905	0.963	26.312	-0.024	-0.024	0.000	0.000	0.000	0.000
157	A	160	PRO	0	0.024	0.017	25.521	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	161	VAL	0	-0.012	-0.003	20.527	-0.007	-0.007	0.000	0.000	0.000	0.000
159	A	162	ILE	0	0.003	-0.007	22.521	0.005	0.005	0.000	0.000	0.000	0.000
160	A	163	GLU	-1	-0.900	-0.953	24.877	0.012	0.012	0.000	0.000	0.000	0.000
161	A	164	HIS	0	-0.007	0.001	17.980	-0.020	-0.020	0.000	0.000	0.000	0.000
162	A	165	TYR	0	-0.055	-0.057	15.623	0.005	0.005	0.000	0.000	0.000	0.000
163	A	166	LYS	1	0.945	0.961	21.584	-0.042	-0.042	0.000	0.000	0.000	0.000
164	A	167	GLN	0	-0.021	0.001	24.346	-0.009	-0.009	0.000	0.000	0.000	0.000
165	A	168	GLN	0	-0.054	-0.011	17.977	-0.011	-0.011	0.000	0.000	0.000	0.000
166	A	169	ASN	0	-0.040	-0.013	21.337	0.004	0.004	0.000	0.000	0.000	0.000
167	A	170	LYS	1	0.927	0.971	14.515	-0.017	-0.017	0.000	0.000	0.000	0.000
168	A	171	VAL	0	-0.034	-0.005	20.802	0.026	0.026	0.000	0.000	0.000	0.000
169	A	172	ILE	0	-0.011	-0.009	22.468	-0.010	-0.010	0.000	0.000	0.000	0.000
170	A	173	THR	0	-0.020	-0.021	25.184	0.008	0.008	0.000	0.000	0.000	0.000
171	A	174	ILE	0	-0.042	-0.017	27.476	-0.004	-0.004	0.000	0.000	0.000	0.000
172	A	175	ASP	-1	-0.784	-0.869	30.077	0.073	0.073	0.000	0.000	0.000	0.000
173	A	176	ALA	0	-0.010	-0.014	31.886	0.004	0.004	0.000	0.000	0.000	0.000
174	A	177	SER	0	-0.057	-0.043	33.892	0.001	0.001	0.000	0.000	0.000	0.000
175	A	178	GLY	0	0.001	0.010	36.790	-0.003	-0.003	0.000	0.000	0.000	0.000
176	A	179	THR	0	0.023	-0.005	37.594	0.004	0.004	0.000	0.000	0.000	0.000
177	A	180	VAL	0	0.053	0.008	33.271	0.003	0.003	0.000	0.000	0.000	0.000
178	A	181	ASP	-1	-0.882	-0.951	33.626	0.130	0.130	0.000	0.000	0.000	0.000
179	A	182	ALA	0	0.020	0.023	34.441	0.003	0.003	0.000	0.000	0.000	0.000
180	A	183	ILE	0	-0.046	-0.010	30.548	0.002	0.002	0.000	0.000	0.000	0.000
181	A	184	PHE	0	0.000	-0.006	26.959	0.006	0.006	0.000	0.000	0.000	0.000
182	A	185	ASP	-1	-0.885	-0.939	29.577	0.132	0.132	0.000	0.000	0.000	0.000
183	A	186	LYS	1	0.867	0.941	30.651	-0.087	-0.087	0.000	0.000	0.000	0.000
184	A	187	VAL	0	0.031	0.002	25.218	-0.001	-0.001	0.000	0.000	0.000	0.000
185	A	188	ASN	0	0.024	-0.006	25.966	0.022	0.022	0.000	0.000	0.000	0.000
186	A	189	HIS	0	-0.079	-0.020	26.567	-0.004	-0.004	0.000	0.000	0.000	0.000
187	A	190	GLU	-1	-0.814	-0.918	26.141	0.084	0.084	0.000	0.000	0.000	0.000
188	A	191	LEU	0	0.039	0.016	20.521	-0.002	-0.002	0.000	0.000	0.000	0.000
189	A	192	GLN	0	0.047	0.035	22.068	0.013	0.013	0.000	0.000	0.000	0.000
190	A	193	LYS	1	0.825	0.916	23.582	-0.087	-0.087	0.000	0.000	0.000	0.000
191	A	194	PHE	0	0.006	0.011	18.787	-0.011	-0.011	0.000	0.000	0.000	0.000
192	A	195	GLY	0	-0.002	-0.002	18.593	0.017	0.017	0.000	0.000	0.000	0.000
193	A	196	VAL	0	-0.065	-0.027	17.801	0.030	0.030	0.000	0.000	0.000	0.000
194	A	197	LYS	1	0.911	0.948	20.387	-0.144	-0.144	0.000	0.000	0.000	0.000

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