FMO DATABASE

FMODB ID: 3J83L

Calculation Name: 2VPI-A-Xray372

Preferred Name: GMP synthase [glutamine-hydrolyzing]

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2VPI

Chain ID: A

ChEMBL ID: CHEMBL5721

UniProt ID: P49915

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	187
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2000364.609452
FMO2-HF: Nuclear repulsion	1929082.185222
FMO2-HF: Total energy	-71282.42423
FMO2-MP2: Total energy	-71489.967322

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:24:MET)

Summations of interaction energy for fragment #1(A:24:MET)

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.
-11.455	-4.924	7.079	-5.578	-8.032	-0.013

Interaction energy analysis for fragmet #1(A:24:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.023 / q_NPA : 0.010

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	26	GLY	0	-0.055	-0.023	3.670	-1.143	0.603	0.006	-0.952	-0.800	0.003
4	A	27	ALA	0	-0.019	-0.006	3.075	0.860	1.336	0.025	-0.144	-0.357	0.000
5	A	28	VAL	0	-0.028	-0.021	5.201	-0.202	-0.189	-0.001	-0.008	-0.004	0.000
6	A	29	VAL	0	0.020	0.024	5.786	0.227	0.227	0.000	0.000	0.000	0.000
7	A	30	ILE	0	-0.047	-0.026	7.452	0.148	0.148	0.000	0.000	0.000	0.000
8	A	31	LEU	0	0.014	0.016	10.376	0.157	0.157	0.000	0.000	0.000	0.000
9	A	32	ASP	-1	-0.808	-0.921	13.425	-0.147	-0.147	0.000	0.000	0.000	0.000
10	A	33	ALA	0	-0.010	0.002	16.984	0.054	0.054	0.000	0.000	0.000	0.000
11	A	34	GLY	0	-0.005	0.000	20.184	0.016	0.016	0.000	0.000	0.000	0.000
12	A	35	ALA	0	0.002	-0.010	21.041	0.012	0.012	0.000	0.000	0.000	0.000
13	A	36	GLN	0	-0.025	-0.017	20.071	0.006	0.006	0.000	0.000	0.000	0.000
14	A	37	TYR	0	-0.010	-0.002	17.254	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	38	GLY	0	0.061	0.019	14.528	0.018	0.018	0.000	0.000	0.000	0.000
16	A	39	LYS	1	0.956	0.977	15.323	-0.118	-0.118	0.000	0.000	0.000	0.000
17	A	40	VAL	0	-0.016	-0.003	16.682	-0.036	-0.036	0.000	0.000	0.000	0.000
18	A	41	ILE	0	0.042	0.011	14.296	-0.026	-0.026	0.000	0.000	0.000	0.000
19	A	42	ASP	-1	-0.750	-0.841	11.042	-0.533	-0.533	0.000	0.000	0.000	0.000
20	A	43	ARG	1	0.881	0.932	13.497	0.158	0.158	0.000	0.000	0.000	0.000
21	A	44	ARG	1	0.746	0.845	16.344	0.263	0.263	0.000	0.000	0.000	0.000
22	A	45	VAL	0	0.051	0.026	10.892	0.000	0.000	0.000	0.000	0.000	0.000
23	A	46	ARG	1	0.899	0.929	9.304	0.499	0.499	0.000	0.000	0.000	0.000
24	A	47	GLU	-1	-0.805	-0.853	14.001	-0.296	-0.296	0.000	0.000	0.000	0.000
25	A	48	LEU	0	-0.047	-0.028	15.707	0.055	0.055	0.000	0.000	0.000	0.000
26	A	49	PHE	0	-0.020	-0.007	14.093	-0.042	-0.042	0.000	0.000	0.000	0.000
27	A	50	VAL	0	0.022	0.031	9.490	-0.073	-0.073	0.000	0.000	0.000	0.000
28	A	51	GLN	0	-0.048	-0.030	3.591	-0.479	-0.224	0.002	-0.055	-0.202	0.000
29	A	52	SER	0	-0.033	-0.052	7.435	-0.393	-0.393	0.000	0.000	0.000	0.000
30	A	53	GLU	-1	-0.846	-0.914	3.755	-0.703	-0.491	0.000	-0.028	-0.184	0.000
31	A	54	ILE	0	-0.045	-0.016	7.024	-0.060	-0.060	0.000	0.000	0.000	0.000
32	A	55	PHE	0	-0.005	-0.006	5.785	0.141	0.141	0.000	0.000	0.000	0.000
33	A	56	PRO	0	0.001	0.008	10.549	-0.135	-0.135	0.000	0.000	0.000	0.000
34	A	57	LEU	0	0.013	0.026	12.884	-0.019	-0.019	0.000	0.000	0.000	0.000
35	A	58	GLU	-1	-0.888	-0.966	15.177	0.275	0.275	0.000	0.000	0.000	0.000
36	A	59	THR	0	-0.061	-0.046	8.869	0.130	0.130	0.000	0.000	0.000	0.000
37	A	60	PRO	0	-0.003	-0.003	12.139	-0.124	-0.124	0.000	0.000	0.000	0.000
38	A	61	ALA	0	0.002	-0.009	10.695	0.051	0.051	0.000	0.000	0.000	0.000
39	A	62	PHE	0	-0.018	-0.012	10.573	-0.141	-0.141	0.000	0.000	0.000	0.000
40	A	63	ALA	0	0.082	0.050	8.747	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	64	ILE	0	0.007	0.000	6.169	0.333	0.333	0.000	0.000	0.000	0.000
42	A	65	LYS	1	0.913	0.937	6.094	-0.568	-0.568	0.000	0.000	0.000	0.000
43	A	66	GLU	-1	-0.923	-0.968	7.474	0.592	0.592	0.000	0.000	0.000	0.000
44	A	67	GLN	0	-0.012	-0.009	2.300	-7.338	-5.686	2.296	-1.488	-2.460	0.012
45	A	68	GLY	0	0.014	0.007	2.351	-4.643	-4.078	3.746	-2.140	-2.171	-0.023
46	A	69	PHE	0	-0.036	-0.001	2.967	-3.286	-1.799	1.006	-0.750	-1.743	-0.005
47	A	70	ARG	1	0.858	0.937	4.492	3.267	3.392	-0.001	-0.013	-0.111	0.000
48	A	71	ALA	0	-0.015	-0.012	7.891	0.575	0.575	0.000	0.000	0.000	0.000
49	A	72	ILE	0	0.008	0.011	8.331	-0.297	-0.297	0.000	0.000	0.000	0.000
50	A	73	ILE	0	-0.018	-0.009	10.728	0.099	0.099	0.000	0.000	0.000	0.000
51	A	74	ILE	0	0.012	0.018	13.187	0.047	0.047	0.000	0.000	0.000	0.000
52	A	75	SER	0	0.022	0.005	15.761	0.006	0.006	0.000	0.000	0.000	0.000
53	A	76	GLY	0	0.034	0.023	18.899	0.030	0.030	0.000	0.000	0.000	0.000
54	A	86	ALA	0	0.011	0.002	26.235	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	87	PRO	0	-0.031	-0.026	21.569	0.015	0.015	0.000	0.000	0.000	0.000
56	A	88	TRP	0	0.033	0.025	17.253	-0.029	-0.029	0.000	0.000	0.000	0.000
57	A	89	PHE	0	0.016	0.004	16.501	0.007	0.007	0.000	0.000	0.000	0.000
58	A	90	ASP	-1	-0.744	-0.858	14.737	0.116	0.116	0.000	0.000	0.000	0.000
59	A	91	PRO	0	0.005	-0.006	16.272	-0.059	-0.059	0.000	0.000	0.000	0.000
60	A	92	ALA	0	0.034	0.008	16.049	-0.051	-0.051	0.000	0.000	0.000	0.000
61	A	93	ILE	0	-0.005	-0.001	12.177	-0.067	-0.067	0.000	0.000	0.000	0.000
62	A	94	PHE	0	-0.010	0.000	14.080	-0.102	-0.102	0.000	0.000	0.000	0.000
63	A	95	THR	0	-0.037	-0.037	16.338	0.000	0.000	0.000	0.000	0.000	0.000
64	A	96	ILE	0	-0.047	-0.019	10.512	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	97	GLY	0	-0.012	-0.002	13.732	-0.055	-0.055	0.000	0.000	0.000	0.000
66	A	98	LYS	1	0.836	0.935	7.425	1.705	1.705	0.000	0.000	0.000	0.000
67	A	99	PRO	0	0.027	0.013	12.062	0.113	0.113	0.000	0.000	0.000	0.000
68	A	100	VAL	0	-0.018	-0.016	12.724	-0.106	-0.106	0.000	0.000	0.000	0.000
69	A	101	LEU	0	0.000	0.008	14.925	0.068	0.068	0.000	0.000	0.000	0.000
70	A	102	GLY	0	0.011	0.001	16.532	0.000	0.000	0.000	0.000	0.000	0.000
71	A	103	ILE	0	-0.010	-0.021	18.288	0.008	0.008	0.000	0.000	0.000	0.000
72	A	104	CYS	0	-0.015	-0.007	21.148	0.031	0.031	0.000	0.000	0.000	0.000
73	A	105	TYR	0	-0.021	-0.006	20.761	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	106	GLY	0	0.039	0.019	19.548	0.008	0.008	0.000	0.000	0.000	0.000
75	A	107	MET	0	-0.047	0.012	20.296	-0.019	-0.019	0.000	0.000	0.000	0.000
76	A	108	GLN	0	-0.012	-0.008	22.839	0.002	0.002	0.000	0.000	0.000	0.000
77	A	109	MET	0	-0.009	-0.004	21.180	0.013	0.013	0.000	0.000	0.000	0.000
78	A	110	MET	0	-0.029	0.008	18.300	0.014	0.014	0.000	0.000	0.000	0.000
79	A	111	ASN	0	-0.022	-0.015	21.614	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	112	LYS	1	0.948	0.977	25.093	0.051	0.051	0.000	0.000	0.000	0.000
81	A	113	VAL	0	-0.043	-0.014	20.479	0.017	0.017	0.000	0.000	0.000	0.000
82	A	114	PHE	0	-0.008	-0.007	20.703	0.001	0.001	0.000	0.000	0.000	0.000
83	A	115	GLY	0	0.024	0.015	25.744	0.000	0.000	0.000	0.000	0.000	0.000
84	A	116	GLY	0	0.018	0.022	28.218	0.007	0.007	0.000	0.000	0.000	0.000
85	A	117	THR	0	-0.080	-0.064	29.735	0.007	0.007	0.000	0.000	0.000	0.000
86	A	118	VAL	0	-0.001	-0.025	28.709	-0.011	-0.011	0.000	0.000	0.000	0.000
87	A	119	HIS	0	-0.033	0.001	31.950	0.007	0.007	0.000	0.000	0.000	0.000
88	A	120	LYS	1	0.870	0.904	30.259	0.037	0.037	0.000	0.000	0.000	0.000
89	A	121	LYS	1	0.923	0.955	33.926	0.022	0.022	0.000	0.000	0.000	0.000
90	A	122	SER	0	0.014	0.009	34.404	0.003	0.003	0.000	0.000	0.000	0.000
91	A	123	VAL	0	-0.014	0.008	32.328	0.000	0.000	0.000	0.000	0.000	0.000
92	A	124	ARG	1	0.839	0.892	34.935	0.054	0.054	0.000	0.000	0.000	0.000
93	A	125	GLU	-1	-0.827	-0.896	36.866	-0.048	-0.048	0.000	0.000	0.000	0.000
94	A	126	ASP	-1	-0.816	-0.884	32.066	-0.077	-0.077	0.000	0.000	0.000	0.000
95	A	127	GLY	0	0.007	-0.005	33.399	0.006	0.006	0.000	0.000	0.000	0.000
96	A	128	VAL	0	-0.027	-0.015	32.190	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	129	PHE	0	-0.007	0.001	33.620	0.008	0.008	0.000	0.000	0.000	0.000
98	A	130	ASN	0	0.001	-0.001	34.026	-0.018	-0.018	0.000	0.000	0.000	0.000
99	A	131	ILE	0	-0.070	-0.031	30.409	0.009	0.009	0.000	0.000	0.000	0.000
100	A	132	SER	0	0.001	-0.006	34.599	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	133	VAL	0	0.002	-0.016	30.079	-0.005	-0.005	0.000	0.000	0.000	0.000
102	A	134	ASP	-1	-0.819	-0.900	30.496	-0.212	-0.212	0.000	0.000	0.000	0.000
103	A	135	ASN	0	-0.058	-0.064	30.223	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	136	THR	0	-0.089	-0.053	30.745	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	137	CYS	0	-0.056	0.007	25.686	-0.020	-0.020	0.000	0.000	0.000	0.000
106	A	138	SER	0	0.008	-0.030	22.644	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	139	LEU	0	-0.018	-0.018	20.458	-0.023	-0.023	0.000	0.000	0.000	0.000
108	A	140	PHE	0	-0.022	-0.027	23.193	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	141	ARG	1	0.910	0.950	24.153	0.430	0.430	0.000	0.000	0.000	0.000
110	A	142	GLY	0	-0.020	-0.012	26.691	-0.016	-0.016	0.000	0.000	0.000	0.000
111	A	143	LEU	0	-0.049	-0.001	26.794	0.008	0.008	0.000	0.000	0.000	0.000
112	A	144	GLN	0	-0.006	0.007	30.307	0.015	0.015	0.000	0.000	0.000	0.000
113	A	145	LYS	1	0.964	0.967	33.086	0.151	0.151	0.000	0.000	0.000	0.000
114	A	146	GLU	-1	-0.935	-0.951	35.501	-0.124	-0.124	0.000	0.000	0.000	0.000
115	A	147	GLU	-1	-0.769	-0.871	30.557	-0.222	-0.222	0.000	0.000	0.000	0.000
116	A	148	VAL	0	0.054	0.035	32.626	0.009	0.009	0.000	0.000	0.000	0.000
117	A	149	VAL	0	-0.029	-0.026	28.845	-0.015	-0.015	0.000	0.000	0.000	0.000
118	A	150	LEU	0	0.012	0.007	27.070	0.015	0.015	0.000	0.000	0.000	0.000
119	A	151	LEU	0	-0.022	-0.018	28.324	-0.013	-0.013	0.000	0.000	0.000	0.000
120	A	152	THR	0	0.025	0.014	27.418	0.002	0.002	0.000	0.000	0.000	0.000
121	A	153	HIS	0	-0.083	-0.065	30.228	0.003	0.003	0.000	0.000	0.000	0.000
122	A	154	GLY	0	-0.008	-0.017	30.606	0.001	0.001	0.000	0.000	0.000	0.000
123	A	155	ASP	-1	-0.862	-0.917	29.952	-0.049	-0.049	0.000	0.000	0.000	0.000
124	A	156	SER	0	0.019	0.030	30.361	-0.007	-0.007	0.000	0.000	0.000	0.000
125	A	157	VAL	0	0.008	-0.002	28.023	0.010	0.010	0.000	0.000	0.000	0.000
126	A	158	ASP	-1	-0.826	-0.879	30.838	-0.067	-0.067	0.000	0.000	0.000	0.000
127	A	159	LYS	1	0.820	0.907	33.579	0.065	0.065	0.000	0.000	0.000	0.000
128	A	160	VAL	0	0.013	-0.002	29.107	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	161	ALA	0	0.018	0.017	27.060	0.008	0.008	0.000	0.000	0.000	0.000
130	A	162	ASP	-1	-0.860	-0.934	29.135	-0.127	-0.127	0.000	0.000	0.000	0.000
131	A	163	GLY	0	-0.040	-0.025	28.113	-0.011	-0.011	0.000	0.000	0.000	0.000
132	A	164	PHE	0	-0.079	-0.032	22.253	-0.025	-0.025	0.000	0.000	0.000	0.000
133	A	165	LYS	1	0.914	0.966	27.805	0.222	0.222	0.000	0.000	0.000	0.000
134	A	166	VAL	0	-0.002	-0.008	28.647	-0.010	-0.010	0.000	0.000	0.000	0.000
135	A	167	VAL	0	-0.047	-0.028	26.441	0.001	0.001	0.000	0.000	0.000	0.000
136	A	168	ALA	0	0.058	0.036	29.523	-0.006	-0.006	0.000	0.000	0.000	0.000
137	A	169	ARG	1	0.837	0.923	31.161	0.129	0.129	0.000	0.000	0.000	0.000
138	A	170	SER	0	0.072	0.052	33.985	-0.003	-0.003	0.000	0.000	0.000	0.000
139	A	171	GLY	0	0.042	0.027	36.910	0.005	0.005	0.000	0.000	0.000	0.000
140	A	172	ASN	0	0.001	-0.010	38.388	-0.006	-0.006	0.000	0.000	0.000	0.000
141	A	173	ILE	0	0.036	0.026	32.930	-0.003	-0.003	0.000	0.000	0.000	0.000
142	A	174	VAL	0	0.017	0.009	29.980	-0.008	-0.008	0.000	0.000	0.000	0.000
143	A	175	ALA	0	0.027	0.003	30.061	0.001	0.001	0.000	0.000	0.000	0.000
144	A	176	GLY	0	0.045	0.008	26.728	-0.015	-0.015	0.000	0.000	0.000	0.000
145	A	177	ILE	0	-0.042	-0.019	24.449	0.018	0.018	0.000	0.000	0.000	0.000
146	A	178	ALA	0	0.060	0.020	23.824	-0.029	-0.029	0.000	0.000	0.000	0.000
147	A	179	ASN	0	0.017	0.032	22.966	0.007	0.007	0.000	0.000	0.000	0.000
148	A	180	GLU	-1	-0.698	-0.817	22.224	-0.403	-0.403	0.000	0.000	0.000	0.000
149	A	181	SER	0	-0.082	-0.043	22.109	-0.027	-0.027	0.000	0.000	0.000	0.000
150	A	182	LYS	1	0.892	0.957	19.782	0.228	0.228	0.000	0.000	0.000	0.000
151	A	183	LYS	1	0.860	0.930	17.459	0.621	0.621	0.000	0.000	0.000	0.000
152	A	184	LEU	0	-0.009	0.009	16.980	-0.052	-0.052	0.000	0.000	0.000	0.000
153	A	185	TYR	0	-0.019	-0.052	18.675	0.031	0.031	0.000	0.000	0.000	0.000
154	A	186	GLY	0	0.028	0.008	20.043	-0.014	-0.014	0.000	0.000	0.000	0.000
155	A	187	ALA	0	0.006	0.003	22.549	0.009	0.009	0.000	0.000	0.000	0.000
156	A	188	GLN	0	0.000	-0.023	24.083	0.000	0.000	0.000	0.000	0.000	0.000
157	A	189	PHE	0	0.010	0.001	25.472	0.013	0.013	0.000	0.000	0.000	0.000
158	A	190	HIS	1	0.833	0.894	22.703	0.151	0.151	0.000	0.000	0.000	0.000
159	A	191	PRO	0	0.010	0.025	20.826	0.012	0.012	0.000	0.000	0.000	0.000
160	A	192	GLU	-1	-0.762	-0.872	19.366	-0.262	-0.262	0.000	0.000	0.000	0.000
161	A	193	VAL	0	-0.017	-0.014	21.016	0.011	0.011	0.000	0.000	0.000	0.000
162	A	194	GLY	0	0.027	0.006	24.483	-0.004	-0.004	0.000	0.000	0.000	0.000
163	A	195	LEU	0	0.001	0.002	26.819	0.006	0.006	0.000	0.000	0.000	0.000
164	A	196	THR	0	-0.049	-0.027	26.035	0.013	0.013	0.000	0.000	0.000	0.000
165	A	197	GLU	-1	-0.916	-0.934	27.124	-0.190	-0.190	0.000	0.000	0.000	0.000
166	A	198	ASN	0	-0.001	-0.017	27.367	-0.019	-0.019	0.000	0.000	0.000	0.000
167	A	199	GLY	0	0.008	-0.007	24.149	-0.026	-0.026	0.000	0.000	0.000	0.000
168	A	200	LYS	1	0.801	0.886	18.902	0.388	0.388	0.000	0.000	0.000	0.000
169	A	201	VAL	0	-0.010	0.005	21.501	-0.045	-0.045	0.000	0.000	0.000	0.000
170	A	202	ILE	0	0.034	0.024	21.356	-0.038	-0.038	0.000	0.000	0.000	0.000
171	A	203	LEU	0	0.010	-0.009	16.968	-0.042	-0.042	0.000	0.000	0.000	0.000
172	A	204	LYS	1	0.965	0.996	17.346	0.354	0.354	0.000	0.000	0.000	0.000
173	A	205	ASN	0	-0.042	-0.030	18.452	-0.072	-0.072	0.000	0.000	0.000	0.000
174	A	206	PHE	0	-0.007	-0.007	13.162	-0.027	-0.027	0.000	0.000	0.000	0.000
175	A	207	LEU	0	0.020	0.010	12.113	-0.092	-0.092	0.000	0.000	0.000	0.000
176	A	208	TYR	0	-0.048	-0.034	14.480	-0.061	-0.061	0.000	0.000	0.000	0.000
177	A	209	ASP	-1	-0.816	-0.887	17.012	-0.535	-0.535	0.000	0.000	0.000	0.000
178	A	210	ILE	0	-0.082	-0.030	16.271	0.005	0.005	0.000	0.000	0.000	0.000
179	A	211	ALA	0	0.024	0.009	12.171	-0.007	-0.007	0.000	0.000	0.000	0.000
180	A	212	GLY	0	0.034	0.030	13.091	-0.168	-0.168	0.000	0.000	0.000	0.000
181	A	213	CYS	0	-0.083	-0.033	11.301	-0.209	-0.209	0.000	0.000	0.000	0.000
182	A	214	SER	0	0.019	-0.004	12.375	0.121	0.121	0.000	0.000	0.000	0.000
183	A	215	GLY	0	0.022	0.017	12.879	-0.098	-0.098	0.000	0.000	0.000	0.000
184	A	216	THR	0	-0.058	-0.038	12.924	0.112	0.112	0.000	0.000	0.000	0.000
185	A	217	PHE	0	0.029	0.035	12.307	-0.139	-0.139	0.000	0.000	0.000	0.000
186	A	218	THR	0	0.009	-0.010	11.950	0.051	0.051	0.000	0.000	0.000	0.000
187	A	219	VAL	0	-0.011	0.008	14.221	0.033	0.033	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:MET)