FMO DATABASE

FMODB ID: 89G4Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2106190.057421
FMO2-HF: Nuclear repulsion	2028719.402381
FMO2-HF: Total energy	-77470.65504
FMO2-MP2: Total energy	-77694.448309

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.
-18.512	-10.685	4.402	-4.31	-7.918	0.035

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 : 0.111 / q_NPA : 0.049

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	-0.048	-0.029	2.090	-13.421	-7.874	4.091	-3.817	-5.821	0.034
4	A	7	ALA	0	0.022	0.018	3.350	-3.342	-2.792	0.030	0.028	-0.609	0.000
5	A	8	LYS	1	0.880	0.930	4.866	-2.218	-2.104	-0.001	-0.008	-0.104	0.000
6	A	9	ALA	0	-0.042	-0.012	6.639	-0.054	-0.054	0.000	0.000	0.000	0.000
7	A	10	LYS	1	0.928	0.987	8.305	-0.708	-0.708	0.000	0.000	0.000	0.000
8	A	11	VAL	0	0.011	-0.001	9.866	0.064	0.064	0.000	0.000	0.000	0.000
9	A	12	ILE	0	0.026	0.012	12.656	-0.122	-0.122	0.000	0.000	0.000	0.000
10	A	13	PHE	0	0.021	0.017	13.408	0.028	0.028	0.000	0.000	0.000	0.000
11	A	14	VAL	0	0.018	0.016	18.014	-0.027	-0.027	0.000	0.000	0.000	0.000
12	A	15	LEU	0	0.011	0.003	21.541	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	16	GLY	0	0.050	0.002	24.265	0.002	0.002	0.000	0.000	0.000	0.000
14	A	17	GLY	0	0.016	0.030	27.866	0.002	0.002	0.000	0.000	0.000	0.000
15	A	18	PRO	0	0.002	-0.004	30.524	0.009	0.009	0.000	0.000	0.000	0.000
16	A	19	GLY	0	0.048	0.023	33.810	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	20	SER	0	-0.023	-0.016	30.485	0.005	0.005	0.000	0.000	0.000	0.000
18	A	21	GLY	0	0.024	0.012	32.129	0.003	0.003	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.875	0.919	24.875	-0.155	-0.155	0.000	0.000	0.000	0.000
20	A	23	GLY	0	0.006	0.009	26.934	0.016	0.016	0.000	0.000	0.000	0.000
21	A	24	THR	0	0.055	0.024	27.504	0.010	0.010	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.019	-0.018	27.583	0.019	0.019	0.000	0.000	0.000	0.000
23	A	26	CYS	0	-0.043	-0.025	23.283	0.015	0.015	0.000	0.000	0.000	0.000
24	A	27	GLU	-1	-0.891	-0.938	23.970	0.218	0.218	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.895	0.954	26.106	-0.141	-0.141	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.025	-0.013	22.702	0.006	0.006	0.000	0.000	0.000	0.000
27	A	30	VAL	0	-0.004	0.010	20.416	0.020	0.020	0.000	0.000	0.000	0.000
28	A	31	GLN	0	-0.031	-0.006	22.657	0.011	0.011	0.000	0.000	0.000	0.000
29	A	32	LYS	1	0.870	0.950	25.789	-0.205	-0.205	0.000	0.000	0.000	0.000
30	A	33	PHE	0	-0.033	-0.037	20.999	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	34	HIS	0	-0.013	0.010	20.544	0.059	0.059	0.000	0.000	0.000	0.000
32	A	35	PHE	0	-0.024	-0.012	17.512	0.070	0.070	0.000	0.000	0.000	0.000
33	A	36	ASN	0	0.017	0.019	12.911	-0.134	-0.134	0.000	0.000	0.000	0.000
34	A	37	HIS	0	-0.054	-0.037	16.129	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	38	LEU	0	-0.008	-0.002	12.036	0.015	0.015	0.000	0.000	0.000	0.000
36	A	39	SER	0	0.014	-0.023	16.653	-0.051	-0.051	0.000	0.000	0.000	0.000
37	A	40	SER	0	0.044	0.011	17.834	0.017	0.017	0.000	0.000	0.000	0.000
38	A	41	GLY	0	0.034	0.017	18.865	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	42	ASP	-1	-0.841	-0.899	19.962	0.231	0.231	0.000	0.000	0.000	0.000
40	A	43	LEU	0	-0.034	-0.019	14.025	0.008	0.008	0.000	0.000	0.000	0.000
41	A	44	LEU	0	0.007	0.000	17.619	-0.029	-0.029	0.000	0.000	0.000	0.000
42	A	45	ARG	1	0.940	0.976	19.782	-0.168	-0.168	0.000	0.000	0.000	0.000
43	A	46	ALA	0	-0.024	-0.016	18.110	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.765	-0.846	16.220	-0.022	-0.022	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.002	0.000	18.964	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	49	GLN	0	-0.060	-0.029	22.392	-0.014	-0.014	0.000	0.000	0.000	0.000
47	A	50	SER	0	-0.013	0.001	18.955	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.015	0.015	20.968	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	52	SER	0	-0.029	-0.028	18.832	-0.030	-0.030	0.000	0.000	0.000	0.000
50	A	53	PRO	0	0.029	-0.009	20.479	0.005	0.005	0.000	0.000	0.000	0.000
51	A	54	LYS	1	0.926	0.954	13.985	0.144	0.144	0.000	0.000	0.000	0.000
52	A	55	GLY	0	0.054	0.032	20.356	0.006	0.006	0.000	0.000	0.000	0.000
53	A	56	LYS	1	0.850	0.916	21.487	0.021	0.021	0.000	0.000	0.000	0.000
54	A	57	GLU	-1	-0.818	-0.893	23.210	-0.066	-0.066	0.000	0.000	0.000	0.000
55	A	58	LEU	0	-0.008	-0.008	18.798	0.003	0.003	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.845	0.914	23.400	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	60	ALA	0	0.018	0.014	26.407	0.004	0.004	0.000	0.000	0.000	0.000
58	A	61	MET	0	-0.039	-0.005	23.814	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	62	MET	0	-0.028	-0.024	22.669	0.009	0.009	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-0.886	-0.924	28.002	0.011	0.011	0.000	0.000	0.000	0.000
61	A	64	ARG	1	0.754	0.846	28.313	0.055	0.055	0.000	0.000	0.000	0.000
62	A	65	GLY	0	-0.023	0.005	30.988	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	66	GLU	-1	-0.874	-0.925	27.864	-0.065	-0.065	0.000	0.000	0.000	0.000
64	A	67	LEU	0	-0.031	-0.018	24.842	0.009	0.009	0.000	0.000	0.000	0.000
65	A	68	VAL	0	0.004	-0.002	19.873	-0.014	-0.014	0.000	0.000	0.000	0.000
66	A	69	PRO	0	0.020	0.009	19.039	0.003	0.003	0.000	0.000	0.000	0.000
67	A	70	LEU	0	0.028	0.018	15.828	0.013	0.013	0.000	0.000	0.000	0.000
68	A	71	GLU	-1	-0.825	-0.929	14.472	-0.254	-0.254	0.000	0.000	0.000	0.000
69	A	72	VAL	0	-0.009	0.002	13.744	-0.044	-0.044	0.000	0.000	0.000	0.000
70	A	73	VAL	0	0.016	0.002	14.459	0.036	0.036	0.000	0.000	0.000	0.000
71	A	74	LEU	0	-0.005	0.000	10.499	0.097	0.097	0.000	0.000	0.000	0.000
72	A	75	ALA	0	-0.006	-0.003	9.675	0.071	0.071	0.000	0.000	0.000	0.000
73	A	76	LEU	0	0.003	0.007	9.704	0.095	0.095	0.000	0.000	0.000	0.000
74	A	77	LEU	0	-0.005	-0.004	11.313	0.186	0.186	0.000	0.000	0.000	0.000
75	A	78	LYS	1	0.896	0.943	4.340	2.918	3.097	-0.001	-0.019	-0.160	0.000
76	A	79	GLU	-1	-0.973	-0.980	6.558	1.089	1.089	0.000	0.000	0.000	0.000
77	A	80	ALA	0	0.002	-0.007	8.078	0.330	0.330	0.000	0.000	0.000	0.000
78	A	81	MET	0	-0.022	-0.017	7.274	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.026	-0.018	2.735	-0.757	0.508	0.284	-0.483	-1.065	0.001
80	A	83	LYS	1	0.925	0.970	6.063	-1.009	-1.009	0.000	0.000	0.000	0.000
81	A	84	LEU	0	-0.011	-0.013	9.535	-0.282	-0.282	0.000	0.000	0.000	0.000
82	A	85	VAL	0	-0.021	0.003	6.050	-0.346	-0.346	0.000	0.000	0.000	0.000
83	A	86	ASP	-1	-0.842	-0.915	9.243	2.102	2.102	0.000	0.000	0.000	0.000
84	A	87	LYS	1	0.932	0.986	11.556	-0.963	-0.963	0.000	0.000	0.000	0.000
85	A	88	ASN	0	0.060	0.021	13.227	-0.122	-0.122	0.000	0.000	0.000	0.000
86	A	89	CYS	0	0.005	0.019	10.990	0.143	0.143	0.000	0.000	0.000	0.000
87	A	90	HIS	0	-0.022	-0.016	11.232	0.022	0.022	0.000	0.000	0.000	0.000
88	A	91	PHE	0	0.010	-0.001	9.410	0.085	0.085	0.000	0.000	0.000	0.000
89	A	92	LEU	0	0.013	0.024	14.064	-0.080	-0.080	0.000	0.000	0.000	0.000
90	A	93	ILE	0	-0.011	-0.017	12.936	0.033	0.033	0.000	0.000	0.000	0.000
91	A	94	ASP	-1	-0.784	-0.873	17.076	0.171	0.171	0.000	0.000	0.000	0.000
92	A	95	GLY	0	-0.051	-0.020	20.700	-0.016	-0.016	0.000	0.000	0.000	0.000
93	A	96	TYR	0	-0.058	-0.017	14.445	-0.024	-0.024	0.000	0.000	0.000	0.000
94	A	97	PRO	0	0.001	0.004	17.136	0.030	0.030	0.000	0.000	0.000	0.000
95	A	98	ARG	1	0.967	0.958	19.037	-0.056	-0.056	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.824	-0.927	21.101	-0.021	-0.021	0.000	0.000	0.000	0.000
97	A	100	LEU	0	0.014	-0.007	19.904	0.004	0.004	0.000	0.000	0.000	0.000
98	A	101	ASP	-1	-0.803	-0.919	18.593	-0.143	-0.143	0.000	0.000	0.000	0.000
99	A	102	GLN	0	0.012	0.008	16.527	-0.005	-0.005	0.000	0.000	0.000	0.000
100	A	103	GLY	0	0.018	0.020	14.908	0.010	0.010	0.000	0.000	0.000	0.000
101	A	104	ILE	0	0.044	0.019	13.975	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	105	LYS	1	0.843	0.915	12.811	0.174	0.174	0.000	0.000	0.000	0.000
103	A	106	PHE	0	0.019	0.009	10.185	-0.118	-0.118	0.000	0.000	0.000	0.000
104	A	107	GLU	-1	-0.758	-0.851	8.974	-0.061	-0.061	0.000	0.000	0.000	0.000
105	A	108	LYS	1	0.818	0.918	8.802	0.668	0.668	0.000	0.000	0.000	0.000
106	A	109	GLU	-1	-0.874	-0.926	7.268	-1.663	-1.663	0.000	0.000	0.000	0.000
107	A	110	VAL	0	-0.069	-0.034	4.991	-0.698	-0.698	0.000	0.000	0.000	0.000
108	A	111	CYS	0	0.007	0.003	4.535	-0.309	-0.137	-0.001	-0.011	-0.159	0.000
109	A	112	PRO	0	0.025	0.004	7.104	0.089	0.089	0.000	0.000	0.000	0.000
110	A	113	CYS	0	-0.114	-0.034	10.475	0.131	0.131	0.000	0.000	0.000	0.000
111	A	114	LEU	0	-0.024	-0.018	12.996	-0.058	-0.058	0.000	0.000	0.000	0.000
112	A	115	CYS	0	-0.047	-0.026	14.745	-0.038	-0.038	0.000	0.000	0.000	0.000
113	A	116	VAL	0	0.025	0.011	17.681	0.038	0.038	0.000	0.000	0.000	0.000
114	A	117	ILE	0	0.002	0.015	20.274	-0.018	-0.018	0.000	0.000	0.000	0.000
115	A	118	ASN	0	-0.034	-0.021	23.184	0.007	0.007	0.000	0.000	0.000	0.000
116	A	119	PHE	0	-0.022	-0.022	25.167	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	120	ASP	-1	-0.905	-0.946	28.888	0.053	0.053	0.000	0.000	0.000	0.000
118	A	121	VAL	0	-0.022	-0.016	31.732	0.002	0.002	0.000	0.000	0.000	0.000
119	A	122	SER	0	0.034	-0.006	35.225	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	123	GLU	-1	-0.717	-0.820	38.056	0.029	0.029	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.803	-0.901	39.714	0.037	0.037	0.000	0.000	0.000	0.000
122	A	125	VAL	0	-0.041	-0.017	38.245	0.002	0.002	0.000	0.000	0.000	0.000
123	A	126	MET	0	-0.027	0.003	37.159	0.003	0.003	0.000	0.000	0.000	0.000
124	A	127	ARG	1	0.927	0.940	39.261	-0.027	-0.027	0.000	0.000	0.000	0.000
125	A	128	LYS	1	0.935	0.982	42.777	-0.050	-0.050	0.000	0.000	0.000	0.000
126	A	129	ARG	1	0.763	0.874	35.758	-0.079	-0.079	0.000	0.000	0.000	0.000
127	A	130	LEU	0	-0.063	-0.041	36.959	0.003	0.003	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.010	0.018	41.505	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	132	LYS	1	0.904	0.956	44.707	-0.031	-0.031	0.000	0.000	0.000	0.000
130	A	133	ARG	1	0.866	0.922	45.576	-0.049	-0.049	0.000	0.000	0.000	0.000
131	A	134	ALA	0	-0.039	-0.031	50.346	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	135	GLU	-1	-0.891	-0.934	52.521	0.021	0.021	0.000	0.000	0.000	0.000
133	A	136	THR	0	0.022	0.024	49.414	0.000	0.000	0.000	0.000	0.000	0.000
134	A	137	SER	0	-0.003	-0.015	51.116	0.000	0.000	0.000	0.000	0.000	0.000
135	A	138	ASN	0	-0.004	-0.018	51.688	0.001	0.001	0.000	0.000	0.000	0.000
136	A	139	ARG	1	0.911	0.971	49.044	-0.036	-0.036	0.000	0.000	0.000	0.000
137	A	140	VAL	0	-0.057	-0.044	47.489	0.002	0.002	0.000	0.000	0.000	0.000
138	A	141	ASP	-1	-0.743	-0.862	47.498	0.023	0.023	0.000	0.000	0.000	0.000
139	A	142	ASP	-1	-0.909	-0.943	46.445	0.020	0.020	0.000	0.000	0.000	0.000
140	A	143	ASN	0	0.004	-0.003	43.791	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	144	GLU	-1	-0.844	-0.939	42.582	0.039	0.039	0.000	0.000	0.000	0.000
142	A	145	GLU	-1	-0.762	-0.878	42.657	0.022	0.022	0.000	0.000	0.000	0.000
143	A	146	THR	0	-0.020	-0.006	39.089	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	147	ILE	0	-0.042	-0.029	37.662	0.001	0.001	0.000	0.000	0.000	0.000
145	A	148	VAL	0	-0.002	0.011	37.947	0.002	0.002	0.000	0.000	0.000	0.000
146	A	149	LYS	1	0.887	0.930	38.632	-0.015	-0.015	0.000	0.000	0.000	0.000
147	A	150	ARG	1	0.941	0.992	33.412	-0.049	-0.049	0.000	0.000	0.000	0.000
148	A	151	PHE	0	-0.023	-0.017	33.799	0.002	0.002	0.000	0.000	0.000	0.000
149	A	152	ARG	1	0.881	0.899	34.195	-0.020	-0.020	0.000	0.000	0.000	0.000
150	A	153	THR	0	-0.012	-0.014	32.006	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	154	PHE	0	-0.032	-0.014	26.548	-0.003	-0.003	0.000	0.000	0.000	0.000
152	A	155	ASN	0	-0.005	-0.006	29.734	-0.005	-0.005	0.000	0.000	0.000	0.000
153	A	156	GLU	-1	-0.830	-0.903	31.044	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	157	LEU	0	-0.033	-0.011	26.694	-0.004	-0.004	0.000	0.000	0.000	0.000
155	A	158	THR	0	-0.026	-0.029	25.218	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	159	LYS	1	0.866	0.933	26.281	-0.003	-0.003	0.000	0.000	0.000	0.000
157	A	160	PRO	0	0.002	0.004	25.533	0.000	0.000	0.000	0.000	0.000	0.000
158	A	161	VAL	0	-0.024	-0.008	20.447	-0.007	-0.007	0.000	0.000	0.000	0.000
159	A	162	ILE	0	0.021	0.006	22.487	0.006	0.006	0.000	0.000	0.000	0.000
160	A	163	GLU	-1	-0.828	-0.902	24.843	0.003	0.003	0.000	0.000	0.000	0.000
161	A	164	HIS	0	-0.008	0.000	17.683	-0.019	-0.019	0.000	0.000	0.000	0.000
162	A	165	TYR	0	-0.039	-0.056	15.551	0.005	0.005	0.000	0.000	0.000	0.000
163	A	166	LYS	1	0.872	0.919	21.547	-0.012	-0.012	0.000	0.000	0.000	0.000
164	A	167	GLN	0	-0.034	-0.020	24.503	-0.006	-0.006	0.000	0.000	0.000	0.000
165	A	168	GLN	0	-0.040	-0.005	17.831	0.002	0.002	0.000	0.000	0.000	0.000
166	A	169	ASN	0	-0.060	-0.024	21.414	0.002	0.002	0.000	0.000	0.000	0.000
167	A	170	LYS	1	0.874	0.940	14.542	-0.020	-0.020	0.000	0.000	0.000	0.000
168	A	171	VAL	0	-0.032	-0.008	20.756	0.025	0.025	0.000	0.000	0.000	0.000
169	A	172	ILE	0	-0.021	-0.015	22.219	-0.008	-0.008	0.000	0.000	0.000	0.000
170	A	173	THR	0	0.000	-0.008	25.155	0.006	0.006	0.000	0.000	0.000	0.000
171	A	174	ILE	0	-0.054	-0.023	27.390	-0.002	-0.002	0.000	0.000	0.000	0.000
172	A	175	ASP	-1	-0.784	-0.852	30.069	0.063	0.063	0.000	0.000	0.000	0.000
173	A	176	ALA	0	-0.002	-0.017	31.840	0.005	0.005	0.000	0.000	0.000	0.000
174	A	177	SER	0	-0.061	-0.056	33.903	0.000	0.000	0.000	0.000	0.000	0.000
175	A	178	GLY	0	0.001	0.011	36.796	-0.003	-0.003	0.000	0.000	0.000	0.000
176	A	179	THR	0	0.019	-0.008	37.619	0.003	0.003	0.000	0.000	0.000	0.000
177	A	180	VAL	0	0.063	0.016	33.334	0.003	0.003	0.000	0.000	0.000	0.000
178	A	181	ASP	-1	-0.841	-0.933	33.663	0.129	0.129	0.000	0.000	0.000	0.000
179	A	182	ALA	0	0.017	0.022	34.470	0.004	0.004	0.000	0.000	0.000	0.000
180	A	183	ILE	0	-0.041	-0.009	30.657	0.003	0.003	0.000	0.000	0.000	0.000
181	A	184	PHE	0	-0.004	-0.007	27.140	0.006	0.006	0.000	0.000	0.000	0.000
182	A	185	ASP	-1	-0.875	-0.939	29.599	0.137	0.137	0.000	0.000	0.000	0.000
183	A	186	LYS	1	0.844	0.917	30.680	-0.088	-0.088	0.000	0.000	0.000	0.000
184	A	187	VAL	0	0.032	-0.001	25.233	0.001	0.001	0.000	0.000	0.000	0.000
185	A	188	ASN	0	0.009	-0.006	25.992	0.027	0.027	0.000	0.000	0.000	0.000
186	A	189	HIS	0	-0.081	-0.035	26.568	0.000	0.000	0.000	0.000	0.000	0.000
187	A	190	GLU	-1	-0.775	-0.864	26.155	0.088	0.088	0.000	0.000	0.000	0.000
188	A	191	LEU	0	0.050	0.020	20.496	-0.001	-0.001	0.000	0.000	0.000	0.000
189	A	192	GLN	0	0.014	0.025	22.052	0.013	0.013	0.000	0.000	0.000	0.000
190	A	193	LYS	1	0.826	0.903	23.551	-0.090	-0.090	0.000	0.000	0.000	0.000
191	A	194	PHE	0	0.006	0.010	18.722	-0.011	-0.011	0.000	0.000	0.000	0.000
192	A	195	GLY	0	0.011	0.005	18.558	0.023	0.023	0.000	0.000	0.000	0.000
193	A	196	VAL	0	-0.086	-0.044	17.727	0.037	0.037	0.000	0.000	0.000	0.000
194	A	197	LYS	1	0.942	0.968	20.386	-0.162	-0.162	0.000	0.000	0.000	0.000

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