FMO DATABASE

FMODB ID: RQRY8

Calculation Name: 2C95-A-Xray547

Preferred Name: Adenylate kinase 1

Target Type: SINGLE PROTEIN

Ligand Name: bis(adenosine)-5'-tetraphosphate | malonate ion

Ligand 3-letter code: B4P | MLI

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2C95

Chain ID: A

ChEMBL ID: CHEMBL4925

UniProt ID: P00568

Base Structure: X-ray

Registration Date: 2025-10-03

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	195
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2181073.386563
FMO2-HF: Nuclear repulsion	2104647.202469
FMO2-HF: Total energy	-76426.184094
FMO2-MP2: Total energy	-76648.065456

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:0:SER)

Summations of interaction energy for fragment #1(A:0:SER)

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.
37.105	40.464	7.134	-3.996	-6.496	0.002

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.892 / q_NPA : 0.938

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	2	GLU	-1	-0.745	-0.873	2.517	-36.326	-34.017	0.599	-1.133	-1.774	-0.002
4	A	3	GLU	-1	-0.875	-0.927	2.001	-55.068	-54.830	6.521	-2.587	-4.173	0.004
5	A	4	LYS	1	0.856	0.928	3.430	66.464	67.276	0.014	-0.276	-0.549	0.000
6	A	5	LEU	0	0.053	0.022	6.073	5.244	5.244	0.000	0.000	0.000	0.000
7	A	6	LYS	1	0.872	0.928	5.102	42.782	42.782	0.000	0.000	0.000	0.000
8	A	7	LYS	1	0.851	0.935	6.321	39.728	39.728	0.000	0.000	0.000	0.000
9	A	8	THR	0	-0.042	-0.011	10.386	1.680	1.680	0.000	0.000	0.000	0.000
10	A	9	ASN	0	0.057	0.042	12.547	-0.812	-0.812	0.000	0.000	0.000	0.000
11	A	10	ILE	0	-0.015	-0.002	11.003	-0.154	-0.154	0.000	0.000	0.000	0.000
12	A	11	ILE	0	0.039	0.021	15.545	0.589	0.589	0.000	0.000	0.000	0.000
13	A	12	PHE	0	0.000	0.005	15.840	-0.096	-0.096	0.000	0.000	0.000	0.000
14	A	13	VAL	0	0.009	0.000	20.504	0.611	0.611	0.000	0.000	0.000	0.000
15	A	14	VAL	0	0.002	-0.001	23.602	0.075	0.075	0.000	0.000	0.000	0.000
16	A	15	GLY	0	0.078	0.029	26.102	0.292	0.292	0.000	0.000	0.000	0.000
17	A	16	GLY	0	0.049	0.027	29.610	-0.201	-0.201	0.000	0.000	0.000	0.000
18	A	17	PRO	0	-0.024	0.004	32.137	-0.212	-0.212	0.000	0.000	0.000	0.000
19	A	18	GLY	0	0.074	0.021	33.213	0.241	0.241	0.000	0.000	0.000	0.000
20	A	19	SER	0	-0.018	-0.030	31.713	0.102	0.102	0.000	0.000	0.000	0.000
21	A	20	GLY	0	0.004	0.004	33.402	0.079	0.079	0.000	0.000	0.000	0.000
22	A	21	LYS	1	0.885	0.939	26.435	11.398	11.398	0.000	0.000	0.000	0.000
23	A	22	GLY	0	0.060	0.037	27.703	-0.296	-0.296	0.000	0.000	0.000	0.000
24	A	23	THR	0	-0.023	-0.021	28.770	-0.200	-0.200	0.000	0.000	0.000	0.000
25	A	24	GLN	0	0.032	0.006	29.622	-0.113	-0.113	0.000	0.000	0.000	0.000
26	A	25	CYS	0	-0.046	-0.017	25.125	-0.342	-0.342	0.000	0.000	0.000	0.000
27	A	26	GLU	-1	-0.838	-0.900	26.496	-12.105	-12.105	0.000	0.000	0.000	0.000
28	A	27	LYS	1	0.848	0.933	28.561	9.133	9.133	0.000	0.000	0.000	0.000
29	A	28	ILE	0	0.019	0.007	24.473	0.015	0.015	0.000	0.000	0.000	0.000
30	A	29	VAL	0	-0.032	-0.013	23.771	-0.277	-0.277	0.000	0.000	0.000	0.000
31	A	30	GLN	0	-0.049	-0.034	25.797	0.066	0.066	0.000	0.000	0.000	0.000
32	A	31	LYS	1	0.881	0.964	28.740	10.356	10.356	0.000	0.000	0.000	0.000
33	A	32	TYR	0	-0.028	-0.062	24.080	0.098	0.098	0.000	0.000	0.000	0.000
34	A	33	GLY	0	-0.004	0.012	23.100	-0.534	-0.534	0.000	0.000	0.000	0.000
35	A	34	TYR	0	-0.017	-0.007	19.319	-1.005	-1.005	0.000	0.000	0.000	0.000
36	A	35	THR	0	-0.026	-0.024	16.747	0.667	0.667	0.000	0.000	0.000	0.000
37	A	36	HIS	1	0.779	0.854	19.045	12.356	12.356	0.000	0.000	0.000	0.000
38	A	37	LEU	0	-0.017	-0.005	15.566	-0.050	-0.050	0.000	0.000	0.000	0.000
39	A	38	SER	0	-0.030	-0.021	20.090	0.056	0.056	0.000	0.000	0.000	0.000
40	A	39	THR	0	0.058	0.020	19.172	0.196	0.196	0.000	0.000	0.000	0.000
41	A	40	GLY	0	0.002	-0.002	21.651	0.211	0.211	0.000	0.000	0.000	0.000
42	A	41	ASP	-1	-0.776	-0.859	24.560	-11.197	-11.197	0.000	0.000	0.000	0.000
43	A	42	LEU	0	-0.020	0.019	18.387	0.161	0.161	0.000	0.000	0.000	0.000
44	A	43	LEU	0	0.038	0.006	22.607	0.217	0.217	0.000	0.000	0.000	0.000
45	A	44	ARG	1	0.886	0.925	24.769	11.350	11.350	0.000	0.000	0.000	0.000
46	A	45	SER	0	-0.024	-0.004	24.232	0.397	0.397	0.000	0.000	0.000	0.000
47	A	46	GLU	-1	-0.769	-0.856	23.641	-12.590	-12.590	0.000	0.000	0.000	0.000
48	A	47	VAL	0	-0.035	-0.004	25.915	0.279	0.279	0.000	0.000	0.000	0.000
49	A	48	SER	0	-0.034	-0.035	29.274	0.409	0.409	0.000	0.000	0.000	0.000
50	A	49	SER	0	-0.074	-0.045	27.014	0.205	0.205	0.000	0.000	0.000	0.000
51	A	50	GLY	0	0.024	0.019	29.160	0.150	0.150	0.000	0.000	0.000	0.000
52	A	51	SER	0	-0.031	-0.016	26.567	0.298	0.298	0.000	0.000	0.000	0.000
53	A	52	ALA	0	0.045	0.007	29.667	0.120	0.120	0.000	0.000	0.000	0.000
54	A	53	ARG	1	0.805	0.895	19.909	13.950	13.950	0.000	0.000	0.000	0.000
55	A	54	GLY	0	0.072	0.027	27.524	0.043	0.043	0.000	0.000	0.000	0.000
56	A	55	LYS	0	0.036	0.025	28.790	0.166	0.166	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.966	0.969	28.811	10.426	10.426	0.000	0.000	0.000	0.000
58	A	57	LEU	0	-0.043	-0.015	24.612	-0.107	-0.107	0.000	0.000	0.000	0.000
59	A	58	SER	0	-0.004	-0.008	28.906	-0.004	-0.004	0.000	0.000	0.000	0.000
60	A	59	GLU	-1	-0.945	-0.959	32.322	-8.827	-8.827	0.000	0.000	0.000	0.000
61	A	60	ILE	0	0.003	-0.004	27.991	0.111	0.111	0.000	0.000	0.000	0.000
62	A	61	MET	0	-0.052	-0.026	28.695	-0.028	-0.028	0.000	0.000	0.000	0.000
63	A	62	GLU	-1	-0.902	-0.965	31.868	-8.474	-8.474	0.000	0.000	0.000	0.000
64	A	63	LYS	0	-0.028	-0.010	34.846	0.373	0.373	0.000	0.000	0.000	0.000
65	A	64	GLY	0	-0.025	-0.019	33.645	0.095	0.095	0.000	0.000	0.000	0.000
66	A	65	GLN	0	-0.046	-0.018	31.176	-0.160	-0.160	0.000	0.000	0.000	0.000
67	A	66	LEU	0	-0.018	-0.016	25.670	-0.271	-0.271	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.004	0.005	23.256	0.173	0.173	0.000	0.000	0.000	0.000
69	A	68	PRO	0	0.019	-0.001	23.457	-0.369	-0.369	0.000	0.000	0.000	0.000
70	A	69	LEU	0	0.041	0.023	17.256	-0.447	-0.447	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.798	-0.886	15.775	-17.792	-17.792	0.000	0.000	0.000	0.000
72	A	71	THR	0	-0.023	-0.005	17.191	-0.479	-0.479	0.000	0.000	0.000	0.000
73	A	72	VAL	0	-0.012	-0.011	19.025	-0.265	-0.265	0.000	0.000	0.000	0.000
74	A	73	LEU	0	-0.009	0.002	12.923	-0.578	-0.578	0.000	0.000	0.000	0.000
75	A	74	ASP	-1	-0.858	-0.937	13.027	-21.952	-21.952	0.000	0.000	0.000	0.000
76	A	75	MET	0	-0.060	-0.023	14.303	-0.503	-0.503	0.000	0.000	0.000	0.000
77	A	76	LEU	0	-0.005	-0.001	14.541	-0.290	-0.290	0.000	0.000	0.000	0.000
78	A	77	ARG	1	0.875	0.931	5.972	30.418	30.418	0.000	0.000	0.000	0.000
79	A	78	ASP	-1	-0.876	-0.938	11.259	-24.131	-24.131	0.000	0.000	0.000	0.000
80	A	79	ALA	0	-0.034	-0.017	12.975	-0.332	-0.332	0.000	0.000	0.000	0.000
81	A	80	MET	0	-0.020	-0.007	11.173	0.110	0.110	0.000	0.000	0.000	0.000
82	A	81	VAL	0	-0.024	-0.018	7.615	-1.798	-1.798	0.000	0.000	0.000	0.000
83	A	82	ALA	0	-0.011	-0.002	10.033	-0.676	-0.676	0.000	0.000	0.000	0.000
84	A	83	LYS	1	0.940	0.964	12.694	19.296	19.296	0.000	0.000	0.000	0.000
85	A	84	VAL	0	0.004	0.008	7.557	-0.061	-0.061	0.000	0.000	0.000	0.000
86	A	85	ASN	0	-0.032	-0.021	7.949	-3.841	-3.841	0.000	0.000	0.000	0.000
87	A	86	THR	0	-0.072	-0.039	10.438	1.780	1.780	0.000	0.000	0.000	0.000
88	A	87	SER	0	-0.010	0.011	13.338	1.915	1.915	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.980	0.984	14.427	17.310	17.310	0.000	0.000	0.000	0.000
90	A	89	GLY	0	0.041	0.030	15.761	0.287	0.287	0.000	0.000	0.000	0.000
91	A	90	PHE	0	-0.044	-0.029	12.109	0.188	0.188	0.000	0.000	0.000	0.000
92	A	91	LEU	0	0.006	0.012	17.032	0.376	0.376	0.000	0.000	0.000	0.000
93	A	92	ILE	0	0.028	0.005	15.391	0.042	0.042	0.000	0.000	0.000	0.000
94	A	93	ASP	-1	-0.756	-0.861	19.439	-11.498	-11.498	0.000	0.000	0.000	0.000
95	A	94	GLY	0	-0.045	-0.036	23.070	0.166	0.166	0.000	0.000	0.000	0.000
96	A	95	TYR	0	-0.018	-0.007	16.731	0.278	0.278	0.000	0.000	0.000	0.000
97	A	96	PRO	0	0.021	0.019	19.058	-0.270	-0.270	0.000	0.000	0.000	0.000
98	A	97	ARG	1	0.898	0.916	21.024	12.081	12.081	0.000	0.000	0.000	0.000
99	A	98	GLU	-1	-0.806	-0.877	22.969	-11.918	-11.918	0.000	0.000	0.000	0.000
100	A	99	VAL	0	0.039	0.017	22.497	-0.547	-0.547	0.000	0.000	0.000	0.000
101	A	100	GLN	0	0.060	0.022	20.835	-0.631	-0.631	0.000	0.000	0.000	0.000
102	A	101	GLN	0	-0.019	-0.012	18.723	-0.902	-0.902	0.000	0.000	0.000	0.000
103	A	102	GLY	0	0.026	0.021	17.318	-0.997	-0.997	0.000	0.000	0.000	0.000
104	A	103	GLU	-1	-0.912	-0.961	16.004	-15.038	-15.038	0.000	0.000	0.000	0.000
105	A	104	GLU	-1	-0.801	-0.876	15.067	-18.907	-18.907	0.000	0.000	0.000	0.000
106	A	105	PHE	0	-0.008	-0.013	12.807	-1.658	-1.658	0.000	0.000	0.000	0.000
107	A	106	GLU	-1	-0.733	-0.828	11.353	-19.450	-19.450	0.000	0.000	0.000	0.000
108	A	107	ARG	1	0.821	0.908	10.958	17.893	17.893	0.000	0.000	0.000	0.000
109	A	108	ARG	1	0.782	0.873	8.632	18.818	18.818	0.000	0.000	0.000	0.000
110	A	109	ILE	0	-0.079	-0.026	7.371	-3.325	-3.325	0.000	0.000	0.000	0.000
111	A	110	GLY	0	0.077	0.036	7.248	-3.822	-3.822	0.000	0.000	0.000	0.000
112	A	111	GLN	0	-0.073	-0.055	8.749	1.717	1.717	0.000	0.000	0.000	0.000
113	A	112	PRO	0	-0.055	-0.008	12.651	-0.397	-0.397	0.000	0.000	0.000	0.000
114	A	113	THR	0	-0.009	-0.018	15.965	-0.021	-0.021	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.018	-0.010	17.680	0.836	0.836	0.000	0.000	0.000	0.000
116	A	115	LEU	0	-0.012	0.005	20.368	-0.538	-0.538	0.000	0.000	0.000	0.000
117	A	116	LEU	0	0.012	0.010	22.885	0.496	0.496	0.000	0.000	0.000	0.000
118	A	117	TYR	0	0.006	-0.025	25.657	-0.056	-0.056	0.000	0.000	0.000	0.000
119	A	118	VAL	0	-0.053	-0.034	28.446	0.322	0.322	0.000	0.000	0.000	0.000
120	A	119	ASP	-1	-0.829	-0.904	30.977	-8.814	-8.814	0.000	0.000	0.000	0.000
121	A	120	ALA	0	0.001	-0.003	34.072	0.142	0.142	0.000	0.000	0.000	0.000
122	A	121	GLY	0	0.071	0.049	37.208	-0.071	-0.071	0.000	0.000	0.000	0.000
123	A	122	PRO	0	0.012	0.000	39.442	-0.107	-0.107	0.000	0.000	0.000	0.000
124	A	123	GLU	-1	-0.862	-0.923	40.416	-7.262	-7.262	0.000	0.000	0.000	0.000
125	A	124	THR	0	-0.036	-0.051	39.623	0.085	0.085	0.000	0.000	0.000	0.000
126	A	125	MET	0	-0.085	-0.021	35.612	-0.213	-0.213	0.000	0.000	0.000	0.000
127	A	126	THR	0	0.019	-0.010	38.892	-0.079	-0.079	0.000	0.000	0.000	0.000
128	A	127	GLN	0	0.013	0.013	41.341	0.045	0.045	0.000	0.000	0.000	0.000
129	A	128	ARG	1	0.788	0.884	37.148	8.332	8.332	0.000	0.000	0.000	0.000
130	A	129	LEU	0	-0.077	-0.032	35.299	-0.120	-0.120	0.000	0.000	0.000	0.000
131	A	130	LEU	0	0.033	0.009	39.264	0.009	0.009	0.000	0.000	0.000	0.000
132	A	131	LYS	1	0.786	0.887	42.394	6.891	6.891	0.000	0.000	0.000	0.000
133	A	132	ARG	1	0.811	0.874	33.810	8.905	8.905	0.000	0.000	0.000	0.000
134	A	133	GLY	0	0.033	0.021	40.545	-0.023	-0.023	0.000	0.000	0.000	0.000
135	A	134	GLU	-1	-0.841	-0.892	42.108	-6.657	-6.657	0.000	0.000	0.000	0.000
136	A	135	THR	0	-0.094	-0.043	41.186	0.048	0.048	0.000	0.000	0.000	0.000
137	A	136	SER	0	0.018	0.004	41.338	-0.113	-0.113	0.000	0.000	0.000	0.000
138	A	137	GLY	0	0.027	0.009	37.384	-0.111	-0.111	0.000	0.000	0.000	0.000
139	A	138	ARG	1	0.748	0.835	31.370	9.297	9.297	0.000	0.000	0.000	0.000
140	A	139	VAL	0	0.096	0.051	36.280	0.139	0.139	0.000	0.000	0.000	0.000
141	A	140	ASP	-1	-0.752	-0.835	33.148	-9.313	-9.313	0.000	0.000	0.000	0.000
142	A	141	ASP	-1	-0.773	-0.858	36.237	-8.771	-8.771	0.000	0.000	0.000	0.000
143	A	142	ASN	0	0.051	0.030	38.608	0.223	0.223	0.000	0.000	0.000	0.000
144	A	143	GLU	-1	-0.827	-0.926	40.801	-7.016	-7.016	0.000	0.000	0.000	0.000
145	A	144	GLU	-1	-0.849	-0.903	42.467	-7.263	-7.263	0.000	0.000	0.000	0.000
146	A	145	THR	0	-0.059	-0.036	36.405	-0.037	-0.037	0.000	0.000	0.000	0.000
147	A	146	ILE	0	-0.038	-0.028	37.417	-0.269	-0.269	0.000	0.000	0.000	0.000
148	A	147	LYS	1	0.840	0.918	38.088	6.916	6.916	0.000	0.000	0.000	0.000
149	A	148	LYS	1	1.017	1.024	36.592	7.644	7.644	0.000	0.000	0.000	0.000
150	A	149	ARG	1	0.746	0.884	33.247	8.682	8.682	0.000	0.000	0.000	0.000
151	A	150	LEU	0	-0.047	-0.018	33.666	-0.307	-0.307	0.000	0.000	0.000	0.000
152	A	151	GLU	-1	-0.910	-0.959	35.323	-8.061	-8.061	0.000	0.000	0.000	0.000
153	A	152	THR	0	-0.036	-0.034	30.186	-0.179	-0.179	0.000	0.000	0.000	0.000
154	A	153	TYR	0	-0.047	-0.017	29.950	-0.462	-0.462	0.000	0.000	0.000	0.000
155	A	154	TYR	0	0.039	0.004	31.515	-0.178	-0.178	0.000	0.000	0.000	0.000
156	A	155	LYS	1	0.915	0.976	32.818	9.120	9.120	0.000	0.000	0.000	0.000
157	A	156	ALA	0	-0.043	-0.020	27.964	-0.087	-0.087	0.000	0.000	0.000	0.000
158	A	157	THR	0	-0.035	-0.042	26.543	-0.334	-0.334	0.000	0.000	0.000	0.000
159	A	158	GLU	-1	-0.868	-0.938	27.871	-9.268	-9.268	0.000	0.000	0.000	0.000
160	A	159	PRO	0	0.003	-0.010	28.346	-0.119	-0.119	0.000	0.000	0.000	0.000
161	A	160	VAL	0	-0.019	-0.004	22.893	-0.246	-0.246	0.000	0.000	0.000	0.000
162	A	161	ILE	0	0.004	0.008	24.998	-0.380	-0.380	0.000	0.000	0.000	0.000
163	A	162	ALA	0	0.040	0.018	26.951	-0.134	-0.134	0.000	0.000	0.000	0.000
164	A	163	PHE	0	-0.071	-0.026	19.873	0.085	0.085	0.000	0.000	0.000	0.000
165	A	164	TYR	0	-0.033	-0.064	17.760	-0.197	-0.197	0.000	0.000	0.000	0.000
166	A	165	GLU	-1	-0.923	-0.958	23.647	-10.437	-10.437	0.000	0.000	0.000	0.000
167	A	166	LYS	1	0.927	0.970	24.703	11.649	11.649	0.000	0.000	0.000	0.000
168	A	167	ARG	1	0.765	0.846	16.519	15.706	15.706	0.000	0.000	0.000	0.000
169	A	168	GLY	0	0.030	0.022	23.372	-0.299	-0.299	0.000	0.000	0.000	0.000
170	A	169	ILE	0	-0.035	-0.011	19.384	-0.016	-0.016	0.000	0.000	0.000	0.000
171	A	170	VAL	0	-0.011	0.001	23.331	-0.307	-0.307	0.000	0.000	0.000	0.000
172	A	171	ARG	1	0.914	0.954	25.985	11.332	11.332	0.000	0.000	0.000	0.000
173	A	172	LYS	1	0.885	0.945	28.081	8.802	8.802	0.000	0.000	0.000	0.000
174	A	173	VAL	0	-0.023	-0.005	30.874	0.163	0.163	0.000	0.000	0.000	0.000
175	A	174	ASN	0	0.045	0.021	33.142	-0.028	-0.028	0.000	0.000	0.000	0.000
176	A	175	ALA	0	0.018	-0.003	34.089	-0.026	-0.026	0.000	0.000	0.000	0.000
177	A	176	GLU	-1	-0.759	-0.849	36.105	-7.748	-7.748	0.000	0.000	0.000	0.000
178	A	177	GLY	0	-0.006	0.007	39.676	-0.055	-0.055	0.000	0.000	0.000	0.000
179	A	178	SER	0	0.004	-0.004	40.823	-0.132	-0.132	0.000	0.000	0.000	0.000
180	A	179	VAL	0	0.055	0.017	35.192	-0.125	-0.125	0.000	0.000	0.000	0.000
181	A	180	ASP	-1	-0.809	-0.901	36.249	-8.603	-8.603	0.000	0.000	0.000	0.000
182	A	181	SER	0	-0.044	-0.028	37.727	-0.044	-0.044	0.000	0.000	0.000	0.000
183	A	182	VAL	0	0.004	0.016	33.493	-0.090	-0.090	0.000	0.000	0.000	0.000
184	A	183	PHE	0	0.040	0.003	29.960	-0.154	-0.154	0.000	0.000	0.000	0.000
185	A	184	SER	0	0.018	0.020	33.413	-0.251	-0.251	0.000	0.000	0.000	0.000
186	A	185	GLN	0	-0.001	0.000	34.281	-0.159	-0.159	0.000	0.000	0.000	0.000
187	A	186	VAL	0	-0.014	-0.009	28.406	-0.233	-0.233	0.000	0.000	0.000	0.000
188	A	187	CYS	0	-0.038	-0.017	29.644	-0.344	-0.344	0.000	0.000	0.000	0.000
189	A	188	THR	0	-0.019	-0.014	30.869	-0.095	-0.095	0.000	0.000	0.000	0.000
190	A	189	HIS	0	-0.036	-0.023	28.322	-0.249	-0.249	0.000	0.000	0.000	0.000
191	A	190	LEU	0	-0.038	-0.011	24.254	-0.372	-0.372	0.000	0.000	0.000	0.000
192	A	191	ASP	-1	-0.772	-0.873	26.693	-10.806	-10.806	0.000	0.000	0.000	0.000
193	A	192	ALA	0	-0.069	-0.022	29.100	0.137	0.137	0.000	0.000	0.000	0.000
194	A	193	LEU	0	-0.114	-0.068	23.353	-0.082	-0.082	0.000	0.000	0.000	0.000
195	A	194	LEU	-1	-0.976	-0.955	21.586	-13.154	-13.154	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:0:SER)