FMO DATABASE

FMODB ID: 6488Z

Calculation Name: 3M1I-A-Xray547

Preferred Name:

Target Type:

Ligand Name: guanosine-5'-triphosphate | magnesium ion

Ligand 3-letter code: GTP | MG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3M1I

Chain ID: A

ChEMBL ID:

UniProt ID: P32835

Base Structure: X-ray

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	208
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2342659.780341
FMO2-HF: Nuclear repulsion	2259966.692135
FMO2-HF: Total energy	-82693.088206
FMO2-MP2: Total energy	-82935.943347

3D Structure Molmil

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:10:VAL)

Summations of interaction energy for fragment #1(A:10:VAL)

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.
-38.283	-30.61	3.08	-4.475	-6.278	-0.046

Interaction energy analysis for fragmet #1(A:10:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.859 / q_NPA : 0.927

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	12	THR	0	0.031	0.006	3.852	0.760	1.933	-0.009	-0.447	-0.716	0.000
50	A	59	GLY	0	0.023	0.023	4.438	-3.985	-3.881	-0.001	-0.009	-0.094	0.000
51	A	60	GLU	-1	-0.892	-0.917	2.325	-52.414	-49.272	1.696	-2.011	-2.828	-0.020
52	A	61	ILE	0	-0.037	-0.023	2.465	-13.752	-10.846	1.393	-1.973	-2.326	-0.026
53	A	62	LYS	1	0.877	0.949	3.701	41.112	41.460	0.001	-0.035	-0.314	0.000
4	A	13	PHE	0	-0.013	-0.008	6.079	2.257	2.257	0.000	0.000	0.000	0.000
5	A	14	LYS	1	0.815	0.922	9.666	18.129	18.129	0.000	0.000	0.000	0.000
6	A	15	LEU	0	0.008	-0.010	12.695	0.909	0.909	0.000	0.000	0.000	0.000
7	A	16	VAL	0	0.000	0.004	14.886	0.375	0.375	0.000	0.000	0.000	0.000
8	A	17	LEU	0	-0.016	0.002	18.503	0.259	0.259	0.000	0.000	0.000	0.000
9	A	18	VAL	0	0.020	0.028	20.484	0.434	0.434	0.000	0.000	0.000	0.000
10	A	19	GLY	0	0.070	0.027	24.190	-0.018	-0.018	0.000	0.000	0.000	0.000
11	A	20	ASP	-1	-0.790	-0.869	27.621	-9.544	-9.544	0.000	0.000	0.000	0.000
12	A	21	GLY	0	0.008	0.013	29.394	-0.314	-0.314	0.000	0.000	0.000	0.000
13	A	22	GLY	0	0.023	0.014	30.660	0.190	0.190	0.000	0.000	0.000	0.000
14	A	23	THR	0	-0.078	-0.050	28.081	-0.078	-0.078	0.000	0.000	0.000	0.000
15	A	24	GLY	0	0.041	0.020	27.039	-0.080	-0.080	0.000	0.000	0.000	0.000
16	A	25	LYS	1	0.791	0.911	22.923	11.618	11.618	0.000	0.000	0.000	0.000
17	A	26	THR	0	0.103	0.017	21.890	-0.272	-0.272	0.000	0.000	0.000	0.000
18	A	27	THR	0	-0.051	-0.011	22.015	-0.383	-0.383	0.000	0.000	0.000	0.000
19	A	28	PHE	0	-0.019	-0.013	18.620	-0.225	-0.225	0.000	0.000	0.000	0.000
20	A	29	VAL	0	0.012	0.001	16.444	-0.592	-0.592	0.000	0.000	0.000	0.000
21	A	30	LYS	1	0.914	0.949	17.642	11.660	11.660	0.000	0.000	0.000	0.000
22	A	31	ARG	1	0.809	0.921	19.112	11.766	11.766	0.000	0.000	0.000	0.000
23	A	32	HIS	1	0.804	0.886	14.886	16.913	16.913	0.000	0.000	0.000	0.000
24	A	33	LEU	0	-0.007	0.010	13.818	-0.948	-0.948	0.000	0.000	0.000	0.000
25	A	34	THR	0	-0.002	-0.034	15.795	-0.337	-0.337	0.000	0.000	0.000	0.000
26	A	35	GLY	0	0.032	0.039	18.647	0.370	0.370	0.000	0.000	0.000	0.000
27	A	36	GLU	-1	-0.804	-0.864	20.571	-12.082	-12.082	0.000	0.000	0.000	0.000
28	A	37	PHE	0	0.004	-0.024	23.518	-0.176	-0.176	0.000	0.000	0.000	0.000
29	A	38	GLU	-1	-0.807	-0.879	25.861	-9.927	-9.927	0.000	0.000	0.000	0.000
30	A	39	LYS	1	0.830	0.890	27.699	9.149	9.149	0.000	0.000	0.000	0.000
31	A	40	LYS	1	0.831	0.906	30.491	10.050	10.050	0.000	0.000	0.000	0.000
32	A	41	TYR	0	-0.009	-0.018	29.621	-0.434	-0.434	0.000	0.000	0.000	0.000
33	A	42	ILE	0	0.038	0.018	29.110	0.319	0.319	0.000	0.000	0.000	0.000
34	A	43	ALA	0	-0.078	-0.038	28.628	-0.312	-0.312	0.000	0.000	0.000	0.000
35	A	44	THR	0	0.079	0.039	23.512	0.312	0.312	0.000	0.000	0.000	0.000
36	A	45	ILE	0	-0.039	-0.026	26.493	0.382	0.382	0.000	0.000	0.000	0.000
37	A	46	GLY	0	0.002	-0.001	25.941	-0.314	-0.314	0.000	0.000	0.000	0.000
38	A	47	VAL	0	-0.061	-0.037	19.919	-0.058	-0.058	0.000	0.000	0.000	0.000
39	A	48	GLU	-1	-0.869	-0.906	19.863	-13.321	-13.321	0.000	0.000	0.000	0.000
40	A	49	VAL	0	-0.042	-0.032	14.161	-0.321	-0.321	0.000	0.000	0.000	0.000
41	A	50	HIS	0	-0.004	-0.011	14.511	-0.816	-0.816	0.000	0.000	0.000	0.000
42	A	51	PRO	0	-0.026	0.001	9.290	-0.791	-0.791	0.000	0.000	0.000	0.000
43	A	52	LEU	0	0.001	-0.004	9.656	1.076	1.076	0.000	0.000	0.000	0.000
44	A	53	SER	0	-0.011	-0.029	5.058	-1.263	-1.263	0.000	0.000	0.000	0.000
45	A	54	PHE	0	-0.024	-0.014	6.732	3.886	3.886	0.000	0.000	0.000	0.000
46	A	55	TYR	0	0.077	0.034	6.383	-4.149	-4.149	0.000	0.000	0.000	0.000
47	A	56	THR	0	-0.032	-0.038	7.032	3.687	3.687	0.000	0.000	0.000	0.000
48	A	57	ASN	0	0.035	0.009	8.362	-2.235	-2.235	0.000	0.000	0.000	0.000
49	A	58	PHE	0	-0.030	-0.010	7.582	1.128	1.128	0.000	0.000	0.000	0.000
54	A	63	PHE	0	-0.017	-0.015	5.456	1.118	1.118	0.000	0.000	0.000	0.000
55	A	64	ASP	-1	-0.805	-0.903	9.047	-29.580	-29.580	0.000	0.000	0.000	0.000
56	A	65	VAL	0	-0.040	-0.033	11.009	1.182	1.182	0.000	0.000	0.000	0.000
57	A	66	TRP	0	0.055	0.017	14.337	1.322	1.322	0.000	0.000	0.000	0.000
58	A	67	ASP	-1	-0.781	-0.888	17.449	-13.021	-13.021	0.000	0.000	0.000	0.000
59	A	68	THR	0	0.002	-0.021	20.247	0.510	0.510	0.000	0.000	0.000	0.000
60	A	69	ALA	0	0.015	0.012	23.533	0.297	0.297	0.000	0.000	0.000	0.000
61	A	70	GLY	0	-0.012	-0.006	27.077	0.102	0.102	0.000	0.000	0.000	0.000
62	A	71	LEU	0	-0.056	-0.036	29.151	0.377	0.377	0.000	0.000	0.000	0.000
63	A	72	GLU	-1	-0.814	-0.885	32.078	-8.774	-8.774	0.000	0.000	0.000	0.000
64	A	73	LYS	1	0.925	0.957	33.713	8.295	8.295	0.000	0.000	0.000	0.000
65	A	74	PHE	0	0.032	0.004	30.444	0.131	0.131	0.000	0.000	0.000	0.000
66	A	75	GLY	0	0.032	0.023	29.269	-0.331	-0.331	0.000	0.000	0.000	0.000
67	A	76	GLY	0	0.026	0.011	28.140	-0.371	-0.371	0.000	0.000	0.000	0.000
68	A	77	LEU	0	0.012	-0.010	25.072	0.286	0.286	0.000	0.000	0.000	0.000
69	A	78	ARG	1	0.833	0.908	27.578	9.536	9.536	0.000	0.000	0.000	0.000
70	A	79	ASP	-1	-0.849	-0.932	25.634	-11.341	-11.341	0.000	0.000	0.000	0.000
71	A	80	GLY	0	0.050	0.025	25.089	-0.442	-0.442	0.000	0.000	0.000	0.000
72	A	81	TYR	0	-0.033	-0.017	21.610	-0.435	-0.435	0.000	0.000	0.000	0.000
73	A	82	TYR	0	-0.008	0.000	20.430	-0.922	-0.922	0.000	0.000	0.000	0.000
74	A	83	ILE	0	0.082	0.047	20.484	-0.624	-0.624	0.000	0.000	0.000	0.000
75	A	84	ASN	0	-0.009	-0.006	16.711	-0.140	-0.140	0.000	0.000	0.000	0.000
76	A	85	ALA	0	-0.005	-0.004	16.019	-1.370	-1.370	0.000	0.000	0.000	0.000
77	A	86	GLN	0	0.045	0.030	10.642	0.343	0.343	0.000	0.000	0.000	0.000
78	A	87	CYS	0	-0.045	-0.001	13.918	-0.095	-0.095	0.000	0.000	0.000	0.000
79	A	88	ALA	0	0.037	0.019	16.262	0.146	0.146	0.000	0.000	0.000	0.000
80	A	89	ILE	0	-0.003	-0.002	17.190	0.158	0.158	0.000	0.000	0.000	0.000
81	A	90	ILE	0	0.006	0.005	20.639	0.297	0.297	0.000	0.000	0.000	0.000
82	A	91	MET	0	-0.009	0.005	22.793	0.238	0.238	0.000	0.000	0.000	0.000
83	A	92	PHE	0	-0.007	-0.026	26.039	0.428	0.428	0.000	0.000	0.000	0.000
84	A	93	ASP	-1	-0.728	-0.828	29.387	-9.450	-9.450	0.000	0.000	0.000	0.000
85	A	94	VAL	0	-0.026	-0.009	31.558	0.341	0.341	0.000	0.000	0.000	0.000
86	A	95	THR	0	-0.022	-0.037	34.111	0.388	0.388	0.000	0.000	0.000	0.000
87	A	96	SER	0	0.028	0.014	35.379	0.348	0.348	0.000	0.000	0.000	0.000
88	A	97	ARG	1	0.932	0.950	36.022	7.252	7.252	0.000	0.000	0.000	0.000
89	A	98	ILE	0	-0.004	0.006	36.924	-0.050	-0.050	0.000	0.000	0.000	0.000
90	A	99	THR	0	0.055	0.026	32.206	-0.195	-0.195	0.000	0.000	0.000	0.000
91	A	100	TYR	0	0.013	0.009	32.288	-0.261	-0.261	0.000	0.000	0.000	0.000
92	A	101	LYS	1	0.936	0.961	34.093	7.560	7.560	0.000	0.000	0.000	0.000
93	A	102	ASN	0	0.020	-0.001	33.144	0.205	0.205	0.000	0.000	0.000	0.000
94	A	103	VAL	0	-0.006	0.019	29.244	-0.238	-0.238	0.000	0.000	0.000	0.000
95	A	104	PRO	0	-0.038	-0.029	30.503	-0.270	-0.270	0.000	0.000	0.000	0.000
96	A	105	ASN	0	-0.027	-0.004	32.463	0.005	0.005	0.000	0.000	0.000	0.000
97	A	106	TRP	0	0.036	0.000	27.449	-0.206	-0.206	0.000	0.000	0.000	0.000
98	A	107	HIS	0	0.021	0.005	26.369	0.008	0.008	0.000	0.000	0.000	0.000
99	A	108	ARG	1	0.753	0.843	28.173	9.168	9.168	0.000	0.000	0.000	0.000
100	A	109	ASP	-1	-0.785	-0.873	29.353	-9.920	-9.920	0.000	0.000	0.000	0.000
101	A	110	LEU	0	0.018	0.018	21.812	-0.223	-0.223	0.000	0.000	0.000	0.000
102	A	111	VAL	0	-0.012	-0.019	25.083	-0.269	-0.269	0.000	0.000	0.000	0.000
103	A	112	ARG	1	0.894	0.955	26.532	9.709	9.709	0.000	0.000	0.000	0.000
104	A	113	VAL	0	-0.014	0.014	23.209	0.085	0.085	0.000	0.000	0.000	0.000
105	A	114	CYS	0	-0.053	-0.021	20.436	-0.443	-0.443	0.000	0.000	0.000	0.000
106	A	115	GLU	-1	-0.922	-0.960	22.915	-12.135	-12.135	0.000	0.000	0.000	0.000
107	A	116	ASN	0	-0.055	-0.031	21.841	0.361	0.361	0.000	0.000	0.000	0.000
108	A	117	ILE	0	0.004	0.018	18.084	-0.809	-0.809	0.000	0.000	0.000	0.000
109	A	118	PRO	0	-0.022	0.003	15.632	0.884	0.884	0.000	0.000	0.000	0.000
110	A	119	ILE	0	0.024	-0.007	18.274	-0.365	-0.365	0.000	0.000	0.000	0.000
111	A	120	VAL	0	-0.028	-0.011	18.767	0.407	0.407	0.000	0.000	0.000	0.000
112	A	121	LEU	0	-0.051	-0.013	21.533	0.139	0.139	0.000	0.000	0.000	0.000
113	A	122	CYS	0	0.008	-0.006	22.049	-0.077	-0.077	0.000	0.000	0.000	0.000
114	A	123	GLY	0	0.038	0.027	25.385	0.231	0.231	0.000	0.000	0.000	0.000
115	A	124	ASN	0	0.019	-0.013	26.773	-0.015	-0.015	0.000	0.000	0.000	0.000
116	A	125	LYS	1	0.865	0.906	28.534	9.992	9.992	0.000	0.000	0.000	0.000
117	A	126	VAL	0	-0.060	-0.034	29.728	0.370	0.370	0.000	0.000	0.000	0.000
118	A	127	ASP	-1	-0.793	-0.857	31.097	-9.565	-9.565	0.000	0.000	0.000	0.000
119	A	128	VAL	0	-0.004	0.005	33.301	0.311	0.311	0.000	0.000	0.000	0.000
120	A	129	LYS	1	1.020	1.002	36.134	7.091	7.091	0.000	0.000	0.000	0.000
121	A	130	GLU	-1	-0.863	-0.919	39.428	-7.160	-7.160	0.000	0.000	0.000	0.000
122	A	131	ARG	1	0.818	0.872	32.541	9.173	9.173	0.000	0.000	0.000	0.000
123	A	132	LYS	1	0.812	0.899	38.331	7.625	7.625	0.000	0.000	0.000	0.000
124	A	133	VAL	0	-0.036	-0.010	34.821	0.208	0.208	0.000	0.000	0.000	0.000
125	A	134	LYS	1	0.962	0.981	36.060	7.477	7.477	0.000	0.000	0.000	0.000
126	A	135	ALA	0	0.115	0.040	35.116	0.018	0.018	0.000	0.000	0.000	0.000
127	A	136	LYS	1	0.971	0.986	35.850	6.998	6.998	0.000	0.000	0.000	0.000
128	A	137	THR	0	-0.036	-0.009	37.340	0.165	0.165	0.000	0.000	0.000	0.000
129	A	138	ILE	0	-0.043	-0.007	31.214	-0.013	-0.013	0.000	0.000	0.000	0.000
130	A	139	THR	0	-0.051	-0.038	33.699	-0.079	-0.079	0.000	0.000	0.000	0.000
131	A	140	PHE	0	0.011	0.013	29.549	-0.009	-0.009	0.000	0.000	0.000	0.000
132	A	141	HIS	0	0.075	0.028	27.645	0.093	0.093	0.000	0.000	0.000	0.000
133	A	142	ARG	1	0.949	0.981	29.073	8.729	8.729	0.000	0.000	0.000	0.000
134	A	143	LYS	1	0.956	0.973	31.363	8.301	8.301	0.000	0.000	0.000	0.000
135	A	144	LYS	1	0.907	0.960	28.480	9.834	9.834	0.000	0.000	0.000	0.000
136	A	145	ASN	0	-0.006	0.011	25.600	-0.247	-0.247	0.000	0.000	0.000	0.000
137	A	146	LEU	0	-0.012	0.014	23.823	-0.407	-0.407	0.000	0.000	0.000	0.000
138	A	147	GLN	0	0.024	0.022	21.362	0.916	0.916	0.000	0.000	0.000	0.000
139	A	148	TYR	0	-0.064	-0.092	23.684	0.090	0.090	0.000	0.000	0.000	0.000
140	A	149	TYR	0	0.010	-0.001	20.214	-0.252	-0.252	0.000	0.000	0.000	0.000
141	A	150	ASP	-1	-0.746	-0.800	25.494	-9.659	-9.659	0.000	0.000	0.000	0.000
142	A	151	ILE	0	-0.003	-0.008	23.108	-0.232	-0.232	0.000	0.000	0.000	0.000
143	A	152	SER	0	-0.063	-0.062	26.045	0.390	0.390	0.000	0.000	0.000	0.000
144	A	153	ALA	0	0.008	0.010	24.488	-0.230	-0.230	0.000	0.000	0.000	0.000
145	A	154	LYS	1	0.887	0.960	25.492	8.964	8.964	0.000	0.000	0.000	0.000
146	A	155	SER	0	0.048	-0.003	28.085	-0.076	-0.076	0.000	0.000	0.000	0.000
147	A	156	ASN	0	0.032	0.017	22.731	-0.436	-0.436	0.000	0.000	0.000	0.000
148	A	157	TYR	0	0.011	0.017	23.718	-0.438	-0.438	0.000	0.000	0.000	0.000
149	A	158	ASN	0	-0.020	-0.032	23.019	-0.231	-0.231	0.000	0.000	0.000	0.000
150	A	159	PHE	0	0.034	0.022	18.789	-0.480	-0.480	0.000	0.000	0.000	0.000
151	A	160	GLU	-1	-0.764	-0.901	16.832	-14.878	-14.878	0.000	0.000	0.000	0.000
152	A	161	LYS	1	0.876	0.953	16.576	11.824	11.824	0.000	0.000	0.000	0.000
153	A	162	PRO	0	-0.029	-0.024	17.896	-0.371	-0.371	0.000	0.000	0.000	0.000
154	A	163	PHE	0	0.049	0.025	12.829	-0.223	-0.223	0.000	0.000	0.000	0.000
155	A	164	LEU	0	0.014	0.021	13.162	-1.141	-1.141	0.000	0.000	0.000	0.000
156	A	165	TRP	0	-0.026	-0.019	14.462	-0.407	-0.407	0.000	0.000	0.000	0.000
157	A	166	LEU	0	-0.004	-0.010	13.923	-0.120	-0.120	0.000	0.000	0.000	0.000
158	A	167	ALA	0	0.047	0.028	10.246	-0.777	-0.777	0.000	0.000	0.000	0.000
159	A	168	ARG	1	0.782	0.889	11.286	16.284	16.284	0.000	0.000	0.000	0.000
160	A	169	LYS	1	0.852	0.941	13.831	15.903	15.903	0.000	0.000	0.000	0.000
161	A	170	LEU	0	-0.016	-0.013	10.296	0.377	0.377	0.000	0.000	0.000	0.000
162	A	171	ALA	0	-0.012	-0.004	8.796	-1.437	-1.437	0.000	0.000	0.000	0.000
163	A	172	GLY	0	-0.012	0.006	10.261	0.382	0.382	0.000	0.000	0.000	0.000
164	A	173	ASN	0	0.025	0.016	12.803	1.899	1.899	0.000	0.000	0.000	0.000
165	A	174	PRO	0	-0.002	-0.016	14.270	-0.491	-0.491	0.000	0.000	0.000	0.000
166	A	175	GLN	0	0.001	-0.008	15.477	0.181	0.181	0.000	0.000	0.000	0.000
167	A	176	LEU	0	-0.013	0.021	8.900	-0.102	-0.102	0.000	0.000	0.000	0.000
168	A	177	GLU	-1	-0.821	-0.919	13.031	-15.378	-15.378	0.000	0.000	0.000	0.000
169	A	178	PHE	0	-0.029	-0.024	10.749	-1.461	-1.461	0.000	0.000	0.000	0.000
170	A	179	VAL	0	-0.020	-0.010	10.169	1.384	1.384	0.000	0.000	0.000	0.000
171	A	180	ALA	0	0.001	0.005	12.109	-0.727	-0.727	0.000	0.000	0.000	0.000
172	A	181	SER	0	0.014	0.012	10.384	-0.835	-0.835	0.000	0.000	0.000	0.000
173	A	182	PRO	0	-0.032	-0.029	9.695	1.419	1.419	0.000	0.000	0.000	0.000
174	A	183	ALA	0	0.008	0.014	12.589	-0.168	-0.168	0.000	0.000	0.000	0.000
175	A	184	LEU	0	-0.016	-0.012	13.066	0.455	0.455	0.000	0.000	0.000	0.000
176	A	185	ALA	0	0.002	0.006	16.936	0.474	0.474	0.000	0.000	0.000	0.000
177	A	186	PRO	0	-0.017	-0.001	20.445	-0.407	-0.407	0.000	0.000	0.000	0.000
178	A	187	PRO	0	0.000	0.005	21.572	0.227	0.227	0.000	0.000	0.000	0.000
179	A	188	GLU	-1	-0.891	-0.968	24.515	-10.963	-10.963	0.000	0.000	0.000	0.000
180	A	189	VAL	0	-0.075	-0.028	25.096	0.272	0.272	0.000	0.000	0.000	0.000
181	A	190	GLN	0	0.035	0.004	26.996	0.009	0.009	0.000	0.000	0.000	0.000
182	A	191	VAL	0	-0.020	0.006	30.447	0.110	0.110	0.000	0.000	0.000	0.000
183	A	192	ASP	-1	-0.872	-0.956	34.092	-7.949	-7.949	0.000	0.000	0.000	0.000
184	A	193	GLU	-1	-0.838	-0.901	36.894	-7.405	-7.405	0.000	0.000	0.000	0.000
185	A	194	GLN	0	-0.035	-0.019	29.884	0.179	0.179	0.000	0.000	0.000	0.000
186	A	195	LEU	0	-0.008	-0.010	33.622	-0.050	-0.050	0.000	0.000	0.000	0.000
187	A	196	MET	0	-0.014	-0.016	35.413	0.139	0.139	0.000	0.000	0.000	0.000
188	A	197	GLN	0	-0.099	-0.063	38.320	0.013	0.013	0.000	0.000	0.000	0.000
189	A	198	GLN	0	-0.052	-0.029	33.233	-0.186	-0.186	0.000	0.000	0.000	0.000
190	A	199	TYR	0	-0.027	-0.002	31.072	-0.232	-0.232	0.000	0.000	0.000	0.000
191	A	200	GLN	0	0.008	0.018	35.089	-0.122	-0.122	0.000	0.000	0.000	0.000
192	A	201	GLN	0	0.019	0.003	38.483	0.026	0.026	0.000	0.000	0.000	0.000
193	A	202	GLU	-1	-0.973	-0.985	31.042	-9.613	-9.613	0.000	0.000	0.000	0.000
194	A	203	MET	0	0.029	0.008	35.194	-0.106	-0.106	0.000	0.000	0.000	0.000
195	A	204	GLU	-1	-0.906	-0.928	36.799	-7.092	-7.092	0.000	0.000	0.000	0.000
196	A	205	GLN	0	-0.033	-0.022	35.316	0.231	0.231	0.000	0.000	0.000	0.000
197	A	206	ALA	0	-0.034	-0.022	34.079	-0.019	-0.019	0.000	0.000	0.000	0.000
198	A	207	THR	0	-0.071	-0.050	35.971	0.035	0.035	0.000	0.000	0.000	0.000
199	A	208	ALA	0	-0.025	-0.001	38.621	0.137	0.137	0.000	0.000	0.000	0.000
200	A	209	LEU	0	-0.054	-0.015	34.648	0.124	0.124	0.000	0.000	0.000	0.000
201	A	210	PRO	0	-0.027	-0.017	37.410	-0.112	-0.112	0.000	0.000	0.000	0.000
202	A	211	LEU	0	0.037	0.029	32.758	-0.233	-0.233	0.000	0.000	0.000	0.000
203	A	212	PRO	0	-0.093	-0.052	31.387	0.174	0.174	0.000	0.000	0.000	0.000
204	A	213	ASP	-1	-0.842	-0.924	32.426	-9.280	-9.280	0.000	0.000	0.000	0.000
205	A	214	GLU	-1	-0.876	-0.933	35.232	-8.227	-8.227	0.000	0.000	0.000	0.000
206	A	215	ASP	-1	-0.902	-0.952	37.279	-7.189	-7.189	0.000	0.000	0.000	0.000
207	A	216	ASP	-1	-1.079	-1.028	34.988	-8.508	-8.508	0.000	0.000	0.000	0.000
208	A	217	ALA	-1	-0.971	-0.976	33.881	-8.648	-8.648	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:10:VAL)