FMO DATABASE

FMODB ID: NNG2Q

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

Total energy (hartree)

FMO2-HF: Electronic energy	-2108867.046098
FMO2-HF: Nuclear repulsion	2032526.37991
FMO2-HF: Total energy	-76340.666189
FMO2-MP2: Total energy	-76561.041862

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.
4.672	1.461	2.465	2.415	-1.667	-0.012

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 : 0.034 / q_NPA : 0.030

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	0.058	0.058	2.592	3.465	-0.174	2.455	2.561	-1.376	-0.012
4	A	2	ALA	0	0.076	0.056	4.561	-0.227	-0.223	-0.001	-0.006	0.003	0.000
5	A	3	ALA	0	0.028	0.005	3.836	0.182	0.311	0.002	-0.057	-0.073	0.000
6	A	4	SER	0	-0.079	-0.045	3.344	0.245	0.518	0.010	-0.081	-0.202	0.000
7	A	5	LEU	0	0.031	0.005	4.961	0.309	0.331	-0.001	-0.002	-0.019	0.000
8	A	6	VAL	0	0.024	0.028	8.070	0.104	0.104	0.000	0.000	0.000	0.000
9	A	7	GLY	0	-0.002	-0.003	10.082	0.034	0.034	0.000	0.000	0.000	0.000
10	A	8	LYS	1	0.812	0.918	8.707	0.295	0.295	0.000	0.000	0.000	0.000
11	A	9	LYS	1	0.910	0.960	13.328	-0.118	-0.118	0.000	0.000	0.000	0.000
12	A	10	ILE	0	0.014	0.008	12.258	0.041	0.041	0.000	0.000	0.000	0.000
13	A	11	VAL	0	-0.029	-0.014	15.768	-0.035	-0.035	0.000	0.000	0.000	0.000
14	A	12	PHE	0	-0.001	0.001	18.597	0.010	0.010	0.000	0.000	0.000	0.000
15	A	13	VAL	0	0.025	-0.003	20.769	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	14	THR	0	-0.024	-0.002	23.305	-0.010	-0.010	0.000	0.000	0.000	0.000
17	A	15	GLY	0	0.028	0.008	26.534	0.005	0.005	0.000	0.000	0.000	0.000
18	A	16	ASN	0	-0.040	-0.030	29.384	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	17	ALA	0	0.087	0.040	28.552	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	18	LYS	1	0.846	0.911	28.730	0.032	0.032	0.000	0.000	0.000	0.000
21	A	19	LYS	1	0.888	0.926	28.076	0.003	0.003	0.000	0.000	0.000	0.000
22	A	20	LEU	0	0.044	0.027	22.292	0.001	0.001	0.000	0.000	0.000	0.000
23	A	21	GLU	-1	-0.777	-0.866	24.951	-0.060	-0.060	0.000	0.000	0.000	0.000
24	A	22	GLU	-1	-0.819	-0.886	26.963	-0.034	-0.034	0.000	0.000	0.000	0.000
25	A	23	VAL	0	0.013	0.016	21.228	-0.009	-0.009	0.000	0.000	0.000	0.000
26	A	24	VAL	0	0.020	0.001	21.719	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	25	GLN	0	-0.093	-0.068	23.146	-0.020	-0.020	0.000	0.000	0.000	0.000
28	A	26	ILE	0	-0.058	-0.018	23.468	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	27	LEU	0	-0.018	0.001	18.041	-0.010	-0.010	0.000	0.000	0.000	0.000
30	A	28	GLY	0	0.042	0.037	20.443	-0.032	-0.032	0.000	0.000	0.000	0.000
31	A	29	ASP	-1	-0.868	-0.950	20.568	-0.268	-0.268	0.000	0.000	0.000	0.000
32	A	30	LYS	1	0.823	0.911	18.492	0.297	0.297	0.000	0.000	0.000	0.000
33	A	31	PHE	0	0.019	0.016	14.796	-0.068	-0.068	0.000	0.000	0.000	0.000
34	A	32	PRO	0	0.010	0.012	11.952	0.029	0.029	0.000	0.000	0.000	0.000
35	A	33	CYS	0	-0.044	-0.022	11.531	-0.033	-0.033	0.000	0.000	0.000	0.000
36	A	34	THR	0	0.011	0.006	14.431	0.025	0.025	0.000	0.000	0.000	0.000
37	A	35	LEU	0	0.012	0.006	16.669	0.046	0.046	0.000	0.000	0.000	0.000
38	A	36	VAL	0	-0.024	-0.019	18.918	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	37	ALA	0	-0.008	0.007	21.549	0.019	0.019	0.000	0.000	0.000	0.000
40	A	38	GLN	0	0.033	0.006	22.899	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	39	LYS	1	0.840	0.911	25.020	-0.081	-0.081	0.000	0.000	0.000	0.000
42	A	40	ILE	0	0.003	0.000	22.679	0.001	0.001	0.000	0.000	0.000	0.000
43	A	41	ASP	-1	-0.890	-0.924	26.176	0.089	0.089	0.000	0.000	0.000	0.000
44	A	42	LEU	0	0.020	0.006	23.565	0.015	0.015	0.000	0.000	0.000	0.000
45	A	43	PRO	0	0.002	0.009	27.557	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	44	GLU	-1	-0.851	-0.909	28.277	0.088	0.088	0.000	0.000	0.000	0.000
47	A	45	TYR	0	0.014	0.000	26.191	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	46	GLN	0	-0.031	-0.027	30.155	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	47	GLY	0	0.053	0.035	29.292	0.011	0.011	0.000	0.000	0.000	0.000
50	A	48	GLU	-1	-0.920	-0.971	27.482	0.090	0.090	0.000	0.000	0.000	0.000
51	A	49	PRO	0	-0.003	-0.027	26.594	0.010	0.010	0.000	0.000	0.000	0.000
52	A	50	ASP	-1	-0.786	-0.854	21.947	0.120	0.120	0.000	0.000	0.000	0.000
53	A	51	GLU	-1	-0.816	-0.897	22.326	0.178	0.178	0.000	0.000	0.000	0.000
54	A	52	ILE	0	-0.019	0.003	23.907	0.017	0.017	0.000	0.000	0.000	0.000
55	A	53	SER	0	0.000	-0.016	21.720	0.004	0.004	0.000	0.000	0.000	0.000
56	A	54	ILE	0	-0.021	-0.018	18.365	0.020	0.020	0.000	0.000	0.000	0.000
57	A	55	GLN	0	-0.006	0.003	20.229	0.018	0.018	0.000	0.000	0.000	0.000
58	A	56	LYS	1	0.851	0.897	22.848	-0.095	-0.095	0.000	0.000	0.000	0.000
59	A	57	CYS	0	-0.031	-0.014	17.054	0.004	0.004	0.000	0.000	0.000	0.000
60	A	58	GLN	0	0.002	0.004	18.521	0.013	0.013	0.000	0.000	0.000	0.000
61	A	59	GLU	-1	-0.850	-0.895	19.535	0.254	0.254	0.000	0.000	0.000	0.000
62	A	60	ALA	0	0.015	-0.001	19.601	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	61	VAL	0	-0.018	-0.008	15.375	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	62	ARG	1	0.851	0.914	18.045	-0.295	-0.295	0.000	0.000	0.000	0.000
65	A	63	GLN	0	-0.067	-0.033	21.051	-0.018	-0.018	0.000	0.000	0.000	0.000
66	A	64	VAL	0	-0.074	-0.043	17.677	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	65	GLN	0	-0.085	-0.036	17.405	0.002	0.002	0.000	0.000	0.000	0.000
68	A	66	GLY	0	0.039	0.020	14.231	0.025	0.025	0.000	0.000	0.000	0.000
69	A	67	PRO	0	-0.036	-0.016	11.217	-0.005	-0.005	0.000	0.000	0.000	0.000
70	A	68	VAL	0	-0.011	0.001	13.443	-0.079	-0.079	0.000	0.000	0.000	0.000
71	A	69	LEU	0	0.004	0.006	15.373	0.028	0.028	0.000	0.000	0.000	0.000
72	A	70	VAL	0	0.001	-0.006	17.582	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	71	GLU	-1	-0.756	-0.855	20.609	0.005	0.005	0.000	0.000	0.000	0.000
74	A	72	ASP	-1	-0.787	-0.873	23.425	0.117	0.117	0.000	0.000	0.000	0.000
75	A	73	THR	0	-0.057	-0.053	25.955	-0.017	-0.017	0.000	0.000	0.000	0.000
76	A	74	CYS	0	-0.080	-0.001	28.742	0.008	0.008	0.000	0.000	0.000	0.000
77	A	75	LEU	0	-0.008	0.004	31.378	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	76	CYS	0	-0.040	-0.002	31.241	0.006	0.006	0.000	0.000	0.000	0.000
79	A	77	PHE	0	0.070	0.011	34.797	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	78	ASN	0	-0.017	-0.027	35.917	0.007	0.007	0.000	0.000	0.000	0.000
81	A	79	ALA	0	0.011	0.010	38.265	0.003	0.003	0.000	0.000	0.000	0.000
82	A	80	LEU	0	-0.049	-0.010	39.787	0.001	0.001	0.000	0.000	0.000	0.000
83	A	81	GLY	0	0.014	0.006	37.592	0.005	0.005	0.000	0.000	0.000	0.000
84	A	82	GLY	0	-0.016	-0.005	34.288	0.004	0.004	0.000	0.000	0.000	0.000
85	A	83	LEU	0	0.005	0.004	34.678	0.003	0.003	0.000	0.000	0.000	0.000
86	A	84	PRO	0	0.022	-0.001	37.090	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	85	GLY	0	0.076	0.039	33.427	0.006	0.006	0.000	0.000	0.000	0.000
88	A	86	PRO	0	0.022	-0.014	29.967	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	87	TYR	0	-0.029	-0.017	31.948	0.001	0.001	0.000	0.000	0.000	0.000
90	A	88	ILE	0	-0.006	-0.001	33.973	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	89	LYS	1	0.885	0.949	33.268	-0.073	-0.073	0.000	0.000	0.000	0.000
92	A	90	TRP	0	0.064	0.011	35.486	-0.005	-0.005	0.000	0.000	0.000	0.000
93	A	91	PHE	0	0.011	0.010	39.384	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	92	LEU	0	0.006	0.014	38.788	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	93	GLU	-1	-0.838	-0.891	40.955	0.037	0.037	0.000	0.000	0.000	0.000
96	A	94	LYS	1	0.815	0.890	42.654	-0.043	-0.043	0.000	0.000	0.000	0.000
97	A	95	LEU	0	-0.018	-0.003	44.158	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	96	LYS	1	0.879	0.934	44.974	-0.028	-0.028	0.000	0.000	0.000	0.000
99	A	97	PRO	0	0.032	0.000	43.439	0.001	0.001	0.000	0.000	0.000	0.000
100	A	98	GLU	-1	-0.870	-0.938	45.078	0.008	0.008	0.000	0.000	0.000	0.000
101	A	99	GLY	0	0.037	0.014	48.021	0.000	0.000	0.000	0.000	0.000	0.000
102	A	100	LEU	0	-0.055	-0.034	41.011	0.002	0.002	0.000	0.000	0.000	0.000
103	A	101	HIS	0	0.042	0.024	44.608	0.001	0.001	0.000	0.000	0.000	0.000
104	A	102	GLN	0	-0.024	-0.013	46.567	0.001	0.001	0.000	0.000	0.000	0.000
105	A	103	LEU	0	-0.039	-0.012	43.070	0.001	0.001	0.000	0.000	0.000	0.000
106	A	104	LEU	0	0.007	0.006	42.388	0.001	0.001	0.000	0.000	0.000	0.000
107	A	105	ALA	0	-0.017	-0.007	46.720	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	106	GLY	0	-0.055	-0.024	50.170	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	107	PHE	0	0.046	0.025	45.588	0.002	0.002	0.000	0.000	0.000	0.000
110	A	108	GLU	-1	-0.879	-0.927	48.556	0.012	0.012	0.000	0.000	0.000	0.000
111	A	109	ASP	-1	-0.831	-0.887	42.172	0.005	0.005	0.000	0.000	0.000	0.000
112	A	110	LYS	1	0.812	0.883	44.239	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	111	SER	0	-0.042	-0.034	39.677	0.000	0.000	0.000	0.000	0.000	0.000
114	A	112	ALA	0	0.022	0.000	37.319	0.005	0.005	0.000	0.000	0.000	0.000
115	A	113	TYR	0	0.016	0.007	29.821	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	114	ALA	0	0.031	0.040	32.393	0.007	0.007	0.000	0.000	0.000	0.000
117	A	115	LEU	0	-0.006	-0.025	25.538	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	116	CYS	0	-0.081	-0.006	25.317	0.003	0.003	0.000	0.000	0.000	0.000
119	A	117	THR	0	0.044	0.003	21.288	-0.015	-0.015	0.000	0.000	0.000	0.000
120	A	118	PHE	0	0.045	0.026	18.967	0.006	0.006	0.000	0.000	0.000	0.000
121	A	119	ALA	0	-0.010	-0.006	17.359	0.007	0.007	0.000	0.000	0.000	0.000
122	A	120	LEU	0	0.019	0.011	11.370	-0.019	-0.019	0.000	0.000	0.000	0.000
123	A	121	SER	0	0.043	0.011	11.604	0.100	0.100	0.000	0.000	0.000	0.000
124	A	122	THR	0	-0.004	-0.027	6.880	-0.105	-0.105	0.000	0.000	0.000	0.000
125	A	123	GLY	0	-0.008	0.008	10.288	-0.056	-0.056	0.000	0.000	0.000	0.000
126	A	124	ASP	-1	-0.833	-0.909	11.164	0.894	0.894	0.000	0.000	0.000	0.000
127	A	125	PRO	0	-0.043	-0.012	8.260	0.051	0.051	0.000	0.000	0.000	0.000
128	A	126	SER	0	0.015	-0.020	10.264	-0.101	-0.101	0.000	0.000	0.000	0.000
129	A	127	GLN	0	-0.099	-0.036	7.441	0.608	0.608	0.000	0.000	0.000	0.000
130	A	128	PRO	0	0.010	0.011	9.851	-0.207	-0.207	0.000	0.000	0.000	0.000
131	A	129	VAL	0	-0.004	-0.004	11.712	0.039	0.039	0.000	0.000	0.000	0.000
132	A	130	ARG	1	0.802	0.912	11.578	-0.008	-0.008	0.000	0.000	0.000	0.000
133	A	131	LEU	0	-0.024	-0.006	13.634	-0.036	-0.036	0.000	0.000	0.000	0.000
134	A	132	PHE	0	-0.012	0.000	12.584	-0.014	-0.014	0.000	0.000	0.000	0.000
135	A	133	ARG	1	0.842	0.884	18.379	-0.083	-0.083	0.000	0.000	0.000	0.000
136	A	134	GLY	0	0.042	0.021	21.992	-0.020	-0.020	0.000	0.000	0.000	0.000
137	A	135	ARG	1	0.879	0.930	25.085	-0.018	-0.018	0.000	0.000	0.000	0.000
138	A	136	THR	0	-0.037	-0.040	28.519	-0.012	-0.012	0.000	0.000	0.000	0.000
139	A	137	SER	0	0.004	0.014	32.043	0.007	0.007	0.000	0.000	0.000	0.000
140	A	138	GLY	0	0.098	0.054	34.847	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	139	ARG	1	0.856	0.939	38.474	0.003	0.003	0.000	0.000	0.000	0.000
142	A	140	ILE	0	0.002	0.012	39.391	-0.001	-0.001	0.000	0.000	0.000	0.000
143	A	141	VAL	0	-0.063	-0.034	42.811	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	142	ALA	0	0.034	0.014	46.142	0.001	0.001	0.000	0.000	0.000	0.000
145	A	143	PRO	0	-0.059	-0.013	46.312	-0.002	-0.002	0.000	0.000	0.000	0.000
146	A	144	ARG	1	0.796	0.861	46.234	0.010	0.010	0.000	0.000	0.000	0.000
147	A	145	GLY	0	0.036	0.026	45.386	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	146	CYS	0	-0.067	-0.047	44.272	0.001	0.001	0.000	0.000	0.000	0.000
149	A	147	GLN	0	0.051	0.001	44.090	0.002	0.002	0.000	0.000	0.000	0.000
150	A	148	ASP	-1	-0.857	-0.914	43.626	0.003	0.003	0.000	0.000	0.000	0.000
151	A	149	PHE	0	-0.081	-0.026	39.462	0.002	0.002	0.000	0.000	0.000	0.000
152	A	150	GLY	0	0.022	-0.004	38.776	0.000	0.000	0.000	0.000	0.000	0.000
153	A	151	TRP	0	0.051	0.006	33.022	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	152	ASP	-1	-0.779	-0.879	36.772	-0.006	-0.006	0.000	0.000	0.000	0.000
155	A	153	PRO	0	-0.018	-0.005	39.436	-0.002	-0.002	0.000	0.000	0.000	0.000
156	A	154	CYS	0	-0.040	-0.011	41.429	0.000	0.000	0.000	0.000	0.000	0.000
157	A	155	PHE	0	0.005	0.009	35.992	0.002	0.002	0.000	0.000	0.000	0.000
158	A	156	GLN	0	0.035	0.023	40.690	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	157	PRO	0	-0.049	-0.007	36.533	0.002	0.002	0.000	0.000	0.000	0.000
160	A	158	ASP	-1	-0.847	-0.959	36.962	-0.016	-0.016	0.000	0.000	0.000	0.000
161	A	159	GLY	0	-0.060	-0.029	37.753	-0.004	-0.004	0.000	0.000	0.000	0.000
162	A	160	TYR	0	-0.090	-0.060	37.313	-0.002	-0.002	0.000	0.000	0.000	0.000
163	A	161	GLU	-1	-0.905	-0.951	42.144	-0.018	-0.018	0.000	0.000	0.000	0.000
164	A	162	GLN	0	0.002	-0.002	42.955	0.003	0.003	0.000	0.000	0.000	0.000
165	A	163	THR	0	0.025	-0.011	42.270	-0.002	-0.002	0.000	0.000	0.000	0.000
166	A	164	TYR	0	-0.033	-0.048	32.710	-0.005	-0.005	0.000	0.000	0.000	0.000
167	A	165	ALA	0	-0.039	-0.011	39.191	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	166	GLU	-1	-0.787	-0.862	41.851	-0.013	-0.013	0.000	0.000	0.000	0.000
169	A	167	MET	0	-0.066	-0.014	37.802	-0.002	-0.002	0.000	0.000	0.000	0.000
170	A	168	PRO	0	0.030	0.028	40.286	0.001	0.001	0.000	0.000	0.000	0.000
171	A	169	LYS	1	0.891	0.914	32.772	0.032	0.032	0.000	0.000	0.000	0.000
172	A	170	ALA	0	-0.012	-0.011	35.353	-0.002	-0.002	0.000	0.000	0.000	0.000
173	A	171	GLU	-1	-0.829	-0.885	35.324	-0.056	-0.056	0.000	0.000	0.000	0.000
174	A	172	LYS	1	0.805	0.893	34.767	0.013	0.013	0.000	0.000	0.000	0.000
175	A	173	ASN	0	-0.028	-0.033	31.241	0.006	0.006	0.000	0.000	0.000	0.000
176	A	174	ALA	0	0.028	0.034	30.835	-0.004	-0.004	0.000	0.000	0.000	0.000
177	A	175	VAL	0	0.015	-0.001	31.799	-0.003	-0.003	0.000	0.000	0.000	0.000
178	A	176	SER	0	0.004	0.040	30.036	0.010	0.010	0.000	0.000	0.000	0.000
179	A	177	HIS	0	0.048	0.029	28.428	-0.014	-0.014	0.000	0.000	0.000	0.000
180	A	178	ARG	1	0.784	0.839	25.783	0.007	0.007	0.000	0.000	0.000	0.000
181	A	179	PHE	0	0.043	0.005	24.855	-0.004	-0.004	0.000	0.000	0.000	0.000
182	A	180	ARG	1	0.879	0.954	24.256	0.038	0.038	0.000	0.000	0.000	0.000
183	A	181	ALA	0	0.014	0.011	22.051	-0.009	-0.009	0.000	0.000	0.000	0.000
184	A	182	LEU	0	-0.029	-0.016	20.281	-0.003	-0.003	0.000	0.000	0.000	0.000
185	A	183	LEU	0	0.018	0.017	19.789	-0.022	-0.022	0.000	0.000	0.000	0.000
186	A	184	GLU	-1	-0.853	-0.921	17.511	-0.112	-0.112	0.000	0.000	0.000	0.000
187	A	185	LEU	0	-0.065	-0.026	14.577	-0.018	-0.018	0.000	0.000	0.000	0.000
188	A	186	GLN	0	-0.054	-0.044	15.073	-0.040	-0.040	0.000	0.000	0.000	0.000
189	A	187	GLU	-1	-0.957	-0.981	14.812	-0.426	-0.426	0.000	0.000	0.000	0.000
190	A	188	TYR	0	0.008	-0.033	8.670	-0.071	-0.071	0.000	0.000	0.000	0.000
191	A	189	PHE	0	-0.055	-0.041	9.566	-0.111	-0.111	0.000	0.000	0.000	0.000
192	A	190	GLY	0	0.031	0.038	11.578	-0.160	-0.160	0.000	0.000	0.000	0.000
193	A	191	SER	0	-0.008	-0.016	14.045	-0.028	-0.028	0.000	0.000	0.000	0.000
194	A	192	LEU	0	-0.046	-0.027	14.162	0.035	0.035	0.000	0.000	0.000	0.000
195	A	193	ALA	0	0.015	0.005	11.393	0.010	0.010	0.000	0.000	0.000	0.000
196	A	194	ALA	0	-0.022	0.015	13.364	0.098	0.098	0.000	0.000	0.000	0.000

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