FMO DATABASE

FMODB ID: 89VNY

Calculation Name: 2CAR-A-Xray372

Preferred Name: Inosine triphosphate pyrophosphatase

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2CAR

Chain ID: A

ChEMBL ID: CHEMBL4105788

UniProt ID: Q9BY32

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	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	196
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2103976.254906
FMO2-HF: Nuclear repulsion	2027636.359532
FMO2-HF: Total energy	-76339.895374
FMO2-MP2: Total energy	-76560.34773

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:-1:GLY)

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

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.
5.728	1.782	1.11	3.809	-0.973	-0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.038 / q_NPA : 0.035

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	1	MET	0	0.057	0.051	2.782	4.253	0.118	1.111	3.863	-0.840	-0.005
4	A	2	ALA	0	0.077	0.050	4.517	-0.238	-0.251	-0.001	-0.009	0.023	0.000
5	A	3	ALA	0	0.018	0.003	4.617	0.105	0.149	-0.001	-0.015	-0.027	0.000
6	A	4	SER	0	-0.077	-0.036	3.745	0.296	0.454	0.001	-0.030	-0.129	0.000
7	A	5	LEU	0	0.025	0.000	5.553	0.428	0.428	0.000	0.000	0.000	0.000
8	A	6	VAL	0	0.038	0.041	8.707	0.141	0.141	0.000	0.000	0.000	0.000
9	A	7	GLY	0	-0.027	-0.014	10.793	-0.011	-0.011	0.000	0.000	0.000	0.000
10	A	8	LYS	1	0.838	0.921	8.736	0.473	0.473	0.000	0.000	0.000	0.000
11	A	9	LYS	1	0.928	0.966	13.761	-0.049	-0.049	0.000	0.000	0.000	0.000
12	A	10	ILE	0	-0.007	-0.001	12.625	0.043	0.043	0.000	0.000	0.000	0.000
13	A	11	VAL	0	-0.007	0.001	16.100	-0.030	-0.030	0.000	0.000	0.000	0.000
14	A	12	PHE	0	-0.013	-0.013	18.932	0.013	0.013	0.000	0.000	0.000	0.000
15	A	13	VAL	0	0.027	0.008	21.089	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	14	THR	0	-0.022	-0.018	23.661	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	15	GLY	0	0.026	0.017	26.997	0.004	0.004	0.000	0.000	0.000	0.000
18	A	16	ASN	0	-0.040	-0.030	29.579	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	17	ALA	0	0.100	0.044	29.310	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	18	LYS	1	0.855	0.915	29.507	0.045	0.045	0.000	0.000	0.000	0.000
21	A	19	LYS	1	0.865	0.923	28.098	0.012	0.012	0.000	0.000	0.000	0.000
22	A	20	LEU	0	0.030	0.019	22.930	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	21	GLU	-1	-0.770	-0.866	25.604	-0.074	-0.074	0.000	0.000	0.000	0.000
24	A	22	GLU	-1	-0.839	-0.907	27.321	-0.044	-0.044	0.000	0.000	0.000	0.000
25	A	23	VAL	0	0.011	0.013	21.708	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	24	VAL	0	0.030	0.009	22.238	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	25	GLN	0	-0.079	-0.048	23.571	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	26	ILE	0	-0.049	-0.014	23.655	-0.011	-0.011	0.000	0.000	0.000	0.000
29	A	27	LEU	0	-0.022	-0.008	18.444	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	28	GLY	0	0.033	0.037	20.734	-0.033	-0.033	0.000	0.000	0.000	0.000
31	A	29	ASP	-1	-0.907	-0.973	21.244	-0.286	-0.286	0.000	0.000	0.000	0.000
32	A	30	LYS	1	0.812	0.900	18.655	0.335	0.335	0.000	0.000	0.000	0.000
33	A	31	PHE	0	0.044	0.022	15.284	-0.070	-0.070	0.000	0.000	0.000	0.000
34	A	32	PRO	0	-0.001	0.008	12.405	0.026	0.026	0.000	0.000	0.000	0.000
35	A	33	CYS	0	-0.020	0.002	11.987	-0.069	-0.069	0.000	0.000	0.000	0.000
36	A	34	THR	0	0.011	0.008	14.900	0.028	0.028	0.000	0.000	0.000	0.000
37	A	35	LEU	0	0.012	0.014	17.189	0.037	0.037	0.000	0.000	0.000	0.000
38	A	36	VAL	0	-0.015	-0.021	19.487	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	37	ALA	0	-0.034	-0.006	21.900	0.017	0.017	0.000	0.000	0.000	0.000
40	A	38	GLN	0	0.007	-0.001	23.676	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	39	LYS	1	0.899	0.944	25.495	-0.069	-0.069	0.000	0.000	0.000	0.000
42	A	40	ILE	0	0.013	0.002	23.011	0.003	0.003	0.000	0.000	0.000	0.000
43	A	41	ASP	-1	-0.919	-0.956	26.464	0.083	0.083	0.000	0.000	0.000	0.000
44	A	42	LEU	0	0.004	0.013	23.575	0.013	0.013	0.000	0.000	0.000	0.000
45	A	43	PRO	0	0.009	0.006	27.194	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	44	GLU	-1	-0.887	-0.934	28.401	0.078	0.078	0.000	0.000	0.000	0.000
47	A	45	TYR	0	0.022	0.000	26.158	0.002	0.002	0.000	0.000	0.000	0.000
48	A	46	GLN	0	-0.029	-0.027	29.955	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	47	GLY	0	0.067	0.048	29.077	0.011	0.011	0.000	0.000	0.000	0.000
50	A	48	GLU	-1	-0.936	-0.988	27.634	0.102	0.102	0.000	0.000	0.000	0.000
51	A	49	PRO	0	0.013	-0.007	26.527	0.010	0.010	0.000	0.000	0.000	0.000
52	A	50	ASP	-1	-0.769	-0.859	22.061	0.134	0.134	0.000	0.000	0.000	0.000
53	A	51	GLU	-1	-0.841	-0.887	22.283	0.185	0.185	0.000	0.000	0.000	0.000
54	A	52	ILE	0	-0.029	-0.020	23.969	0.014	0.014	0.000	0.000	0.000	0.000
55	A	53	SER	0	-0.033	-0.022	21.377	0.001	0.001	0.000	0.000	0.000	0.000
56	A	54	ILE	0	-0.004	-0.015	18.220	0.017	0.017	0.000	0.000	0.000	0.000
57	A	55	GLN	0	-0.009	0.004	20.101	0.018	0.018	0.000	0.000	0.000	0.000
58	A	56	LYS	1	0.862	0.909	22.661	-0.090	-0.090	0.000	0.000	0.000	0.000
59	A	57	CYS	0	-0.040	-0.020	17.024	0.004	0.004	0.000	0.000	0.000	0.000
60	A	58	GLN	0	0.010	-0.006	18.235	0.003	0.003	0.000	0.000	0.000	0.000
61	A	59	GLU	-1	-0.826	-0.883	19.374	0.238	0.238	0.000	0.000	0.000	0.000
62	A	60	ALA	0	-0.001	-0.020	19.796	-0.008	-0.008	0.000	0.000	0.000	0.000
63	A	61	VAL	0	-0.040	-0.017	15.452	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	62	ARG	1	0.900	0.960	18.266	-0.291	-0.291	0.000	0.000	0.000	0.000
65	A	63	GLN	0	-0.099	-0.045	21.094	-0.020	-0.020	0.000	0.000	0.000	0.000
66	A	64	VAL	0	-0.047	-0.034	18.056	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	65	GLN	0	-0.082	-0.034	17.292	0.006	0.006	0.000	0.000	0.000	0.000
68	A	66	GLY	0	0.029	0.014	14.332	0.017	0.017	0.000	0.000	0.000	0.000
69	A	67	PRO	0	-0.047	-0.024	11.427	0.001	0.001	0.000	0.000	0.000	0.000
70	A	68	VAL	0	-0.022	-0.008	13.768	-0.064	-0.064	0.000	0.000	0.000	0.000
71	A	69	LEU	0	0.009	0.004	15.670	0.020	0.020	0.000	0.000	0.000	0.000
72	A	70	VAL	0	0.008	-0.002	17.922	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	71	GLU	-1	-0.759	-0.850	20.755	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	72	ASP	-1	-0.800	-0.874	23.517	0.105	0.105	0.000	0.000	0.000	0.000
75	A	73	THR	0	-0.064	-0.054	26.113	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	74	CYS	0	-0.065	0.005	28.636	0.006	0.006	0.000	0.000	0.000	0.000
77	A	75	LEU	0	-0.010	-0.003	31.151	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	76	CYS	0	-0.062	-0.009	31.590	0.006	0.006	0.000	0.000	0.000	0.000
79	A	77	PHE	0	0.071	0.015	35.145	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	78	ASN	0	-0.014	-0.034	36.426	0.008	0.008	0.000	0.000	0.000	0.000
81	A	79	ALA	0	0.042	0.038	38.787	0.003	0.003	0.000	0.000	0.000	0.000
82	A	80	LEU	0	-0.079	-0.033	39.946	0.002	0.002	0.000	0.000	0.000	0.000
83	A	81	GLY	0	0.022	0.013	37.834	0.005	0.005	0.000	0.000	0.000	0.000
84	A	82	GLY	0	-0.008	0.000	34.440	0.005	0.005	0.000	0.000	0.000	0.000
85	A	83	LEU	0	-0.009	0.003	34.816	0.002	0.002	0.000	0.000	0.000	0.000
86	A	84	PRO	0	0.035	-0.014	37.060	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	85	GLY	0	0.076	0.049	33.326	0.006	0.006	0.000	0.000	0.000	0.000
88	A	86	PRO	0	0.026	-0.013	29.966	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	87	TYR	0	-0.030	-0.019	31.911	0.002	0.002	0.000	0.000	0.000	0.000
90	A	88	ILE	0	0.027	0.023	33.807	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	89	LYS	1	0.891	0.949	33.513	-0.066	-0.066	0.000	0.000	0.000	0.000
92	A	90	TRP	0	0.043	0.012	35.378	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	91	PHE	0	0.039	0.016	39.404	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	92	LEU	0	0.000	0.010	39.104	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	93	GLU	-1	-0.863	-0.907	41.119	0.033	0.033	0.000	0.000	0.000	0.000
96	A	94	LYS	1	0.833	0.892	42.896	-0.040	-0.040	0.000	0.000	0.000	0.000
97	A	95	LEU	0	-0.021	0.011	44.074	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	96	LYS	1	0.865	0.918	44.945	-0.024	-0.024	0.000	0.000	0.000	0.000
99	A	97	PRO	0	0.053	0.011	43.493	0.001	0.001	0.000	0.000	0.000	0.000
100	A	98	GLU	-1	-0.885	-0.947	45.145	0.008	0.008	0.000	0.000	0.000	0.000
101	A	99	GLY	0	0.035	0.014	47.811	0.000	0.000	0.000	0.000	0.000	0.000
102	A	100	LEU	0	-0.058	-0.039	40.865	0.002	0.002	0.000	0.000	0.000	0.000
103	A	101	HIS	0	0.036	0.015	44.549	0.001	0.001	0.000	0.000	0.000	0.000
104	A	102	GLN	0	-0.006	0.000	46.425	0.001	0.001	0.000	0.000	0.000	0.000
105	A	103	LEU	0	-0.041	-0.004	43.040	0.001	0.001	0.000	0.000	0.000	0.000
106	A	104	LEU	0	0.010	-0.005	42.748	0.002	0.002	0.000	0.000	0.000	0.000
107	A	105	ALA	0	-0.072	-0.036	46.969	-0.001	-0.001	0.000	0.000	0.000	0.000
108	A	106	GLY	0	-0.021	-0.007	50.095	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	107	PHE	0	0.012	0.014	46.082	0.001	0.001	0.000	0.000	0.000	0.000
110	A	108	GLU	-1	-0.868	-0.939	48.477	0.014	0.014	0.000	0.000	0.000	0.000
111	A	109	ASP	-1	-0.868	-0.900	42.010	0.012	0.012	0.000	0.000	0.000	0.000
112	A	110	LYS	1	0.834	0.913	44.304	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	111	SER	0	-0.025	-0.023	39.738	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	112	ALA	0	0.021	0.003	37.609	0.005	0.005	0.000	0.000	0.000	0.000
115	A	113	TYR	0	-0.008	-0.014	30.123	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	114	ALA	0	0.016	0.035	32.347	0.006	0.006	0.000	0.000	0.000	0.000
117	A	115	LEU	0	0.002	-0.026	25.485	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	116	CYS	0	-0.074	0.002	25.223	0.002	0.002	0.000	0.000	0.000	0.000
119	A	117	THR	0	0.039	-0.007	20.991	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	118	PHE	0	0.036	0.020	18.873	0.001	0.001	0.000	0.000	0.000	0.000
121	A	119	ALA	0	-0.010	-0.017	17.184	0.011	0.011	0.000	0.000	0.000	0.000
122	A	120	LEU	0	0.003	-0.005	11.468	-0.020	-0.020	0.000	0.000	0.000	0.000
123	A	121	SER	0	0.064	0.023	11.877	0.097	0.097	0.000	0.000	0.000	0.000
124	A	122	THR	0	0.045	0.015	7.069	-0.133	-0.133	0.000	0.000	0.000	0.000
125	A	123	GLY	0	-0.031	-0.017	10.573	-0.045	-0.045	0.000	0.000	0.000	0.000
126	A	124	ASP	-1	-0.786	-0.874	10.709	0.926	0.926	0.000	0.000	0.000	0.000
127	A	125	PRO	0	-0.002	0.000	7.533	0.004	0.004	0.000	0.000	0.000	0.000
128	A	126	SER	0	-0.096	-0.055	10.178	-0.048	-0.048	0.000	0.000	0.000	0.000
129	A	127	GLN	0	-0.112	-0.071	6.939	0.604	0.604	0.000	0.000	0.000	0.000
130	A	128	PRO	0	0.009	0.019	9.492	-0.211	-0.211	0.000	0.000	0.000	0.000
131	A	129	VAL	0	0.016	0.005	11.460	0.016	0.016	0.000	0.000	0.000	0.000
132	A	130	ARG	1	0.889	0.963	11.611	-0.038	-0.038	0.000	0.000	0.000	0.000
133	A	131	LEU	0	-0.016	-0.001	13.701	-0.040	-0.040	0.000	0.000	0.000	0.000
134	A	132	PHE	0	-0.026	-0.004	12.615	-0.012	-0.012	0.000	0.000	0.000	0.000
135	A	133	ARG	1	0.836	0.877	18.496	-0.099	-0.099	0.000	0.000	0.000	0.000
136	A	134	GLY	0	0.056	0.034	22.167	-0.018	-0.018	0.000	0.000	0.000	0.000
137	A	135	ARG	1	0.910	0.957	25.216	-0.026	-0.026	0.000	0.000	0.000	0.000
138	A	136	THR	0	-0.026	-0.032	28.663	-0.009	-0.009	0.000	0.000	0.000	0.000
139	A	137	SER	0	-0.003	0.010	32.039	0.007	0.007	0.000	0.000	0.000	0.000
140	A	138	GLY	0	0.108	0.058	35.053	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	139	ARG	1	0.928	0.970	38.474	0.003	0.003	0.000	0.000	0.000	0.000
142	A	140	ILE	0	-0.036	0.000	39.391	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	141	VAL	0	-0.073	-0.036	42.966	0.000	0.000	0.000	0.000	0.000	0.000
144	A	142	ALA	0	0.036	0.014	46.117	0.001	0.001	0.000	0.000	0.000	0.000
145	A	143	PRO	0	-0.065	-0.027	46.405	-0.002	-0.002	0.000	0.000	0.000	0.000
146	A	144	ARG	1	0.861	0.923	46.119	0.010	0.010	0.000	0.000	0.000	0.000
147	A	145	GLY	0	0.052	0.022	45.680	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	146	CYS	0	-0.068	-0.041	44.848	0.002	0.002	0.000	0.000	0.000	0.000
149	A	147	GLN	0	0.050	0.003	44.447	0.001	0.001	0.000	0.000	0.000	0.000
150	A	148	ASP	-1	-0.876	-0.929	43.722	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	149	PHE	0	-0.064	-0.015	39.644	0.001	0.001	0.000	0.000	0.000	0.000
152	A	150	GLY	0	0.021	-0.006	38.562	0.000	0.000	0.000	0.000	0.000	0.000
153	A	151	TRP	0	0.050	0.010	33.142	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	152	ASP	-1	-0.775	-0.872	36.861	-0.010	-0.010	0.000	0.000	0.000	0.000
155	A	153	PRO	0	-0.003	-0.013	39.582	-0.002	-0.002	0.000	0.000	0.000	0.000
156	A	154	CYS	0	-0.036	-0.011	41.434	0.000	0.000	0.000	0.000	0.000	0.000
157	A	155	PHE	0	0.004	0.008	35.813	0.002	0.002	0.000	0.000	0.000	0.000
158	A	156	GLN	0	0.034	0.027	40.423	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	157	PRO	0	-0.051	-0.009	36.647	0.002	0.002	0.000	0.000	0.000	0.000
160	A	158	ASP	-1	-0.857	-0.968	37.449	-0.015	-0.015	0.000	0.000	0.000	0.000
161	A	159	GLY	0	-0.054	-0.029	38.039	-0.004	-0.004	0.000	0.000	0.000	0.000
162	A	160	TYR	0	-0.099	-0.071	37.373	-0.002	-0.002	0.000	0.000	0.000	0.000
163	A	161	GLU	-1	-0.896	-0.946	42.411	-0.017	-0.017	0.000	0.000	0.000	0.000
164	A	162	GLN	0	-0.044	-0.021	43.162	0.002	0.002	0.000	0.000	0.000	0.000
165	A	163	THR	0	0.020	-0.009	42.196	-0.001	-0.001	0.000	0.000	0.000	0.000
166	A	164	TYR	0	0.005	-0.032	32.847	-0.005	-0.005	0.000	0.000	0.000	0.000
167	A	165	ALA	0	-0.066	-0.018	39.474	-0.003	-0.003	0.000	0.000	0.000	0.000
168	A	166	GLU	-1	-0.811	-0.894	41.848	-0.016	-0.016	0.000	0.000	0.000	0.000
169	A	167	MET	0	-0.074	-0.005	37.770	-0.001	-0.001	0.000	0.000	0.000	0.000
170	A	168	PRO	0	0.029	0.025	40.852	0.000	0.000	0.000	0.000	0.000	0.000
171	A	169	LYS	1	0.920	0.939	33.026	0.042	0.042	0.000	0.000	0.000	0.000
172	A	170	ALA	0	-0.013	-0.015	35.502	-0.002	-0.002	0.000	0.000	0.000	0.000
173	A	171	GLU	-1	-0.813	-0.879	35.604	-0.058	-0.058	0.000	0.000	0.000	0.000
174	A	172	LYS	1	0.801	0.892	34.049	0.018	0.018	0.000	0.000	0.000	0.000
175	A	173	ASN	0	-0.062	-0.058	31.550	0.006	0.006	0.000	0.000	0.000	0.000
176	A	174	ALA	0	0.012	0.022	31.032	-0.005	-0.005	0.000	0.000	0.000	0.000
177	A	175	VAL	0	0.003	0.007	32.003	-0.003	-0.003	0.000	0.000	0.000	0.000
178	A	176	SER	0	-0.006	0.035	30.318	0.009	0.009	0.000	0.000	0.000	0.000
179	A	177	HIS	0	0.065	0.027	28.490	-0.013	-0.013	0.000	0.000	0.000	0.000
180	A	178	ARG	1	0.810	0.847	26.078	0.021	0.021	0.000	0.000	0.000	0.000
181	A	179	PHE	0	0.030	-0.001	24.958	-0.005	-0.005	0.000	0.000	0.000	0.000
182	A	180	ARG	1	0.912	0.964	24.537	0.036	0.036	0.000	0.000	0.000	0.000
183	A	181	ALA	0	0.002	0.005	22.108	-0.009	-0.009	0.000	0.000	0.000	0.000
184	A	182	LEU	0	-0.008	-0.007	20.397	-0.005	-0.005	0.000	0.000	0.000	0.000
185	A	183	LEU	0	0.018	0.017	19.883	-0.024	-0.024	0.000	0.000	0.000	0.000
186	A	184	GLU	-1	-0.916	-0.951	18.195	-0.125	-0.125	0.000	0.000	0.000	0.000
187	A	185	LEU	0	-0.078	-0.033	14.487	-0.022	-0.022	0.000	0.000	0.000	0.000
188	A	186	GLN	0	-0.049	-0.053	15.026	-0.051	-0.051	0.000	0.000	0.000	0.000
189	A	187	GLU	-1	-0.960	-0.978	15.561	-0.387	-0.387	0.000	0.000	0.000	0.000
190	A	188	TYR	0	-0.047	-0.062	8.448	-0.044	-0.044	0.000	0.000	0.000	0.000
191	A	189	PHE	0	-0.066	-0.037	9.973	-0.103	-0.103	0.000	0.000	0.000	0.000
192	A	190	GLY	0	0.008	0.023	11.937	-0.169	-0.169	0.000	0.000	0.000	0.000
193	A	191	SER	0	-0.006	-0.022	14.435	0.011	0.011	0.000	0.000	0.000	0.000
194	A	192	LEU	0	-0.019	-0.016	14.220	0.039	0.039	0.000	0.000	0.000	0.000
195	A	193	ALA	0	-0.006	-0.001	12.289	-0.043	-0.043	0.000	0.000	0.000	0.000
196	A	194	ALA	0	0.021	0.047	14.280	0.083	0.083	0.000	0.000	0.000	0.000

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