FMO DATABASE

FMODB ID: 7KV5K

Calculation Name: 4CQL-G-Xray547

Preferred Name:

Target Type:

Ligand Name: nicotinamide-adenine-dinucleotide

Ligand 3-letter code: NAD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4CQL

Chain ID: G

ChEMBL ID:

UniProt ID: Q8N4T8

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	231
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2639357.109423
FMO2-HF: Nuclear repulsion	2552865.10835
FMO2-HF: Total energy	-86492.001073
FMO2-MP2: Total energy	-86743.780809

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:7:VAL)

Summations of interaction energy for fragment #1(A:7: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.
145.498	156.874	24.643	-14.42	-21.599	-0.153

Interaction energy analysis for fragmet #1(A:7:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.755 / q_NPA : 0.877

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	9	GLY	0	0.061	0.011	2.799	1.410	3.605	0.495	-1.130	-1.559	-0.008
4	A	10	GLY	0	-0.050	-0.023	2.754	1.840	2.857	0.627	-0.659	-0.984	0.000
5	A	11	SER	0	-0.032	-0.007	3.359	4.151	3.958	0.054	0.456	-0.317	0.000
9	A	15	GLY	0	0.062	0.028	2.335	-1.372	-1.581	1.749	-0.744	-0.796	0.001
10	A	16	ARG	1	0.891	0.951	2.532	17.884	18.038	1.239	0.341	-1.733	-0.020
11	A	17	ALA	0	-0.026	-0.001	5.224	1.217	1.270	-0.001	-0.003	-0.050	0.000
12	A	18	VAL	0	0.010	-0.006	2.430	0.190	0.880	1.546	-0.431	-1.805	-0.002
13	A	19	ALA	0	0.022	0.011	2.607	-1.044	0.459	0.459	-0.621	-1.341	-0.006
14	A	20	GLN	0	0.032	0.012	3.494	4.051	4.134	0.035	0.032	-0.150	0.000
23	A	29	LEU	0	0.046	0.028	2.564	-5.046	-4.033	1.028	-0.496	-1.545	-0.006
24	A	30	ALA	0	-0.052	-0.033	3.035	8.856	9.811	0.090	-0.413	-0.632	-0.001
25	A	31	VAL	0	-0.028	0.013	1.774	-41.994	-43.411	11.901	-6.374	-4.109	-0.072
26	A	32	ILE	0	0.048	0.040	3.478	8.485	9.129	0.002	-0.176	-0.470	-0.001
43	A	49	ASP	0	-0.023	0.020	4.135	-5.258	-5.022	0.000	-0.032	-0.204	0.000
74	A	80	LEU	0	-0.012	-0.002	3.885	-9.600	-9.388	0.000	-0.038	-0.174	0.000
75	A	81	VAL	0	0.013	0.001	2.314	2.531	3.654	2.298	-0.930	-2.492	-0.003
76	A	82	ASN	0	0.005	-0.007	2.354	-21.408	-18.656	2.678	-2.991	-2.440	-0.035
77	A	83	ALA	0	0.017	-0.003	2.656	4.691	5.208	0.444	-0.207	-0.755	0.000
78	A	84	ALA	0	-0.035	-0.007	4.528	2.856	2.904	-0.001	-0.004	-0.043	0.000
6	A	12	ARG	1	0.990	0.974	6.779	22.985	22.985	0.000	0.000	0.000	0.000
7	A	13	GLY	0	0.035	0.021	6.752	-2.165	-2.165	0.000	0.000	0.000	0.000
8	A	14	ILE	0	0.077	0.017	5.326	-0.031	-0.031	0.000	0.000	0.000	0.000
15	A	21	LEU	0	0.013	0.017	6.816	2.201	2.201	0.000	0.000	0.000	0.000
16	A	22	MET	0	-0.037	-0.006	5.158	2.450	2.450	0.000	0.000	0.000	0.000
17	A	23	ALA	0	-0.003	-0.001	6.756	2.511	2.511	0.000	0.000	0.000	0.000
18	A	24	ARG	1	0.825	0.905	8.566	26.542	26.542	0.000	0.000	0.000	0.000
19	A	25	LYS	1	0.819	0.909	10.587	24.980	24.980	0.000	0.000	0.000	0.000
20	A	26	GLY	0	0.018	0.013	11.514	0.582	0.582	0.000	0.000	0.000	0.000
21	A	27	TYR	0	0.000	-0.005	8.096	0.309	0.309	0.000	0.000	0.000	0.000
22	A	28	ARG	1	0.871	0.910	7.435	24.420	24.420	0.000	0.000	0.000	0.000
27	A	33	ALA	0	0.007	-0.008	5.594	-2.939	-2.939	0.000	0.000	0.000	0.000
28	A	34	ARG	1	0.863	0.917	8.043	22.600	22.600	0.000	0.000	0.000	0.000
29	A	35	ASN	0	-0.013	-0.020	11.146	1.704	1.704	0.000	0.000	0.000	0.000
30	A	36	LEU	0	0.103	0.064	11.284	-2.265	-2.265	0.000	0.000	0.000	0.000
31	A	37	GLU	-1	-0.798	-0.882	12.887	-18.597	-18.597	0.000	0.000	0.000	0.000
32	A	38	GLY	0	0.043	0.011	11.341	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	39	ALA	0	-0.036	-0.017	8.402	-2.191	-2.191	0.000	0.000	0.000	0.000
34	A	40	LYS	1	0.850	0.896	9.396	16.697	16.697	0.000	0.000	0.000	0.000
35	A	41	ALA	0	-0.006	0.009	12.330	0.713	0.713	0.000	0.000	0.000	0.000
36	A	42	ALA	0	0.023	0.013	7.764	0.170	0.170	0.000	0.000	0.000	0.000
37	A	43	ALA	0	-0.048	-0.055	9.597	-1.345	-1.345	0.000	0.000	0.000	0.000
38	A	44	GLY	0	0.000	0.022	10.564	0.897	0.897	0.000	0.000	0.000	0.000
39	A	45	ASP	-1	-0.888	-0.940	11.771	-22.915	-22.915	0.000	0.000	0.000	0.000
40	A	46	LEU	0	-0.082	-0.036	5.798	-1.349	-1.349	0.000	0.000	0.000	0.000
41	A	47	GLY	0	0.083	0.039	9.155	-1.035	-1.035	0.000	0.000	0.000	0.000
42	A	48	GLY	0	0.071	0.024	8.366	-2.664	-2.664	0.000	0.000	0.000	0.000
44	A	50	HIS	1	0.826	0.910	6.021	39.244	39.244	0.000	0.000	0.000	0.000
45	A	51	LEU	0	0.064	0.025	6.008	-7.165	-7.165	0.000	0.000	0.000	0.000
46	A	52	ALA	0	0.005	0.033	7.885	1.200	1.200	0.000	0.000	0.000	0.000
47	A	53	PHE	0	-0.015	-0.019	5.853	-0.545	-0.545	0.000	0.000	0.000	0.000
48	A	54	SER	0	-0.049	-0.033	9.426	1.417	1.417	0.000	0.000	0.000	0.000
49	A	55	CYS	0	-0.038	-0.002	9.115	-0.841	-0.841	0.000	0.000	0.000	0.000
50	A	56	ASP	-1	-0.732	-0.885	11.184	-19.124	-19.124	0.000	0.000	0.000	0.000
51	A	57	VAL	0	0.004	0.003	9.465	-0.535	-0.535	0.000	0.000	0.000	0.000
52	A	58	ALA	0	0.002	0.016	12.422	0.445	0.445	0.000	0.000	0.000	0.000
53	A	59	LYS	1	0.868	0.932	16.013	18.992	18.992	0.000	0.000	0.000	0.000
54	A	60	GLU	-1	-0.828	-0.924	14.945	-17.482	-17.482	0.000	0.000	0.000	0.000
55	A	61	HIS	0	0.053	0.014	14.986	-1.659	-1.659	0.000	0.000	0.000	0.000
56	A	62	ASP	-1	-0.868	-0.914	13.384	-21.094	-21.094	0.000	0.000	0.000	0.000
57	A	63	VAL	0	0.003	0.017	9.710	-2.027	-2.027	0.000	0.000	0.000	0.000
58	A	64	GLN	0	0.034	0.008	10.978	-2.213	-2.213	0.000	0.000	0.000	0.000
59	A	65	ASN	0	-0.010	-0.001	13.530	0.400	0.400	0.000	0.000	0.000	0.000
60	A	66	THR	0	-0.049	-0.040	7.392	-1.135	-1.135	0.000	0.000	0.000	0.000
61	A	67	PHE	0	-0.044	-0.059	7.361	-2.321	-2.321	0.000	0.000	0.000	0.000
62	A	68	GLU	-1	-0.902	-0.923	10.486	-18.067	-18.067	0.000	0.000	0.000	0.000
63	A	69	GLU	0	-0.071	-0.031	11.050	0.599	0.599	0.000	0.000	0.000	0.000
64	A	70	LEU	0	-0.047	-0.009	7.003	-1.859	-1.859	0.000	0.000	0.000	0.000
65	A	71	GLU	-1	-0.739	-0.850	10.452	-21.958	-21.958	0.000	0.000	0.000	0.000
66	A	72	LYS	1	0.944	0.987	13.872	16.898	16.898	0.000	0.000	0.000	0.000
67	A	73	HIS	1	0.852	0.907	11.736	22.560	22.560	0.000	0.000	0.000	0.000
68	A	74	LEU	0	-0.038	-0.022	6.684	-0.186	-0.186	0.000	0.000	0.000	0.000
69	A	75	GLY	0	0.072	0.055	10.951	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	76	ARG	1	0.929	0.954	12.805	19.089	19.089	0.000	0.000	0.000	0.000
71	A	77	VAL	0	0.024	0.016	6.932	-0.323	-0.323	0.000	0.000	0.000	0.000
72	A	78	ASN	0	0.011	-0.002	8.762	-1.933	-1.933	0.000	0.000	0.000	0.000
73	A	79	PHE	0	0.019	0.017	6.415	1.274	1.274	0.000	0.000	0.000	0.000
79	A	85	GLY	0	-0.005	-0.019	6.499	1.382	1.382	0.000	0.000	0.000	0.000
80	A	86	ILE	0	-0.036	-0.009	10.119	-0.244	-0.244	0.000	0.000	0.000	0.000
81	A	87	ASN	0	0.016	0.008	13.471	-0.072	-0.072	0.000	0.000	0.000	0.000
82	A	88	ARG	1	0.833	0.903	16.016	13.128	13.128	0.000	0.000	0.000	0.000
83	A	89	ASP	-1	-0.797	-0.891	19.556	-13.008	-13.008	0.000	0.000	0.000	0.000
84	A	90	GLY	0	-0.015	-0.016	22.377	0.266	0.266	0.000	0.000	0.000	0.000
85	A	91	LEU	0	0.032	0.017	25.768	-0.102	-0.102	0.000	0.000	0.000	0.000
86	A	92	LEU	0	0.011	0.004	27.570	-0.103	-0.103	0.000	0.000	0.000	0.000
87	A	93	VAL	0	0.071	0.033	29.159	-0.063	-0.063	0.000	0.000	0.000	0.000
88	A	94	ARG	1	0.905	0.958	29.363	9.049	9.049	0.000	0.000	0.000	0.000
89	A	95	THR	0	-0.017	-0.013	24.504	-0.151	-0.151	0.000	0.000	0.000	0.000
90	A	96	LYS	1	0.981	0.996	26.696	9.758	9.758	0.000	0.000	0.000	0.000
91	A	97	THR	0	0.075	0.013	25.838	-0.419	-0.419	0.000	0.000	0.000	0.000
92	A	98	GLU	-1	-0.861	-0.916	24.460	-11.727	-11.727	0.000	0.000	0.000	0.000
93	A	99	ASP	-1	-0.815	-0.884	21.303	-14.209	-14.209	0.000	0.000	0.000	0.000
94	A	100	MET	0	-0.045	-0.024	20.715	-0.667	-0.667	0.000	0.000	0.000	0.000
95	A	101	VAL	0	0.038	0.020	21.001	-0.564	-0.564	0.000	0.000	0.000	0.000
96	A	102	SER	0	0.012	-0.003	18.393	-0.904	-0.904	0.000	0.000	0.000	0.000
97	A	103	GLN	0	-0.050	-0.021	16.268	-1.586	-1.586	0.000	0.000	0.000	0.000
98	A	104	LEU	0	0.018	0.010	15.816	-1.161	-1.161	0.000	0.000	0.000	0.000
99	A	105	HIS	0	0.019	-0.005	16.619	-1.148	-1.148	0.000	0.000	0.000	0.000
100	A	106	THR	0	-0.031	-0.017	11.563	-1.462	-1.462	0.000	0.000	0.000	0.000
101	A	107	ASN	0	-0.025	-0.021	11.604	-3.237	-3.237	0.000	0.000	0.000	0.000
102	A	108	LEU	0	-0.006	0.016	12.100	-1.324	-1.324	0.000	0.000	0.000	0.000
103	A	109	LEU	0	0.040	0.016	13.918	-0.925	-0.925	0.000	0.000	0.000	0.000
104	A	110	GLY	0	0.071	0.039	11.773	-0.457	-0.457	0.000	0.000	0.000	0.000
105	A	111	SER	0	-0.044	-0.022	9.472	-3.298	-3.298	0.000	0.000	0.000	0.000
106	A	112	MET	0	-0.034	-0.011	10.534	-0.703	-0.703	0.000	0.000	0.000	0.000
107	A	113	LEU	0	-0.001	0.004	13.031	0.108	0.108	0.000	0.000	0.000	0.000
108	A	114	THR	0	-0.014	-0.013	6.613	-0.749	-0.749	0.000	0.000	0.000	0.000
109	A	115	CYS	0	-0.077	-0.037	9.849	-1.014	-1.014	0.000	0.000	0.000	0.000
110	A	116	LYS	1	0.930	0.969	11.441	17.509	17.509	0.000	0.000	0.000	0.000
111	A	117	ALA	0	0.009	0.005	11.041	0.872	0.872	0.000	0.000	0.000	0.000
112	A	118	ALA	0	0.001	-0.010	8.981	0.006	0.006	0.000	0.000	0.000	0.000
113	A	119	MET	0	-0.040	-0.019	10.874	0.967	0.967	0.000	0.000	0.000	0.000
114	A	120	ARG	1	0.837	0.913	12.207	22.838	22.838	0.000	0.000	0.000	0.000
115	A	121	THR	0	-0.009	-0.019	11.519	1.505	1.505	0.000	0.000	0.000	0.000
116	A	122	MET	0	-0.061	-0.003	8.612	0.837	0.837	0.000	0.000	0.000	0.000
117	A	123	ILE	0	-0.019	0.002	13.918	0.663	0.663	0.000	0.000	0.000	0.000
118	A	124	GLN	0	0.001	-0.014	15.975	-0.170	-0.170	0.000	0.000	0.000	0.000
119	A	125	GLN	0	0.066	0.028	17.839	-0.880	-0.880	0.000	0.000	0.000	0.000
120	A	126	GLN	0	0.003	0.002	16.167	-0.257	-0.257	0.000	0.000	0.000	0.000
121	A	127	GLY	0	-0.007	0.023	14.446	-1.176	-1.176	0.000	0.000	0.000	0.000
122	A	128	GLY	0	0.072	0.014	11.785	-1.619	-1.619	0.000	0.000	0.000	0.000
123	A	129	SER	0	-0.059	-0.037	9.839	1.974	1.974	0.000	0.000	0.000	0.000
124	A	130	ILE	0	0.021	0.002	7.838	-4.218	-4.218	0.000	0.000	0.000	0.000
125	A	131	VAL	0	-0.013	0.006	6.747	2.943	2.943	0.000	0.000	0.000	0.000
126	A	132	ASN	0	0.004	-0.002	6.318	-7.615	-7.615	0.000	0.000	0.000	0.000
127	A	133	VAL	0	0.001	0.002	5.618	2.019	2.019	0.000	0.000	0.000	0.000
128	A	134	GLY	0	0.056	0.031	8.327	0.437	0.437	0.000	0.000	0.000	0.000
129	A	135	SER	0	-0.042	-0.041	11.903	-0.308	-0.308	0.000	0.000	0.000	0.000
130	A	136	ILE	0	0.045	0.030	14.603	0.260	0.260	0.000	0.000	0.000	0.000
131	A	137	VAL	0	0.065	0.031	17.592	0.456	0.456	0.000	0.000	0.000	0.000
132	A	138	GLY	0	-0.050	-0.020	17.468	0.410	0.410	0.000	0.000	0.000	0.000
133	A	139	LEU	0	-0.079	-0.049	18.100	0.129	0.129	0.000	0.000	0.000	0.000
134	A	140	LYS	1	0.826	0.910	20.800	11.862	11.862	0.000	0.000	0.000	0.000
135	A	141	GLY	0	0.028	0.036	22.322	0.493	0.493	0.000	0.000	0.000	0.000
136	A	142	ASN	0	0.013	-0.016	22.459	0.036	0.036	0.000	0.000	0.000	0.000
137	A	143	SER	0	0.034	0.028	24.289	0.041	0.041	0.000	0.000	0.000	0.000
138	A	144	GLY	0	0.012	0.004	25.498	-0.161	-0.161	0.000	0.000	0.000	0.000
139	A	145	GLN	0	0.061	0.035	20.213	-0.718	-0.718	0.000	0.000	0.000	0.000
140	A	146	SER	0	0.021	0.017	21.649	-0.510	-0.510	0.000	0.000	0.000	0.000
141	A	147	VAL	0	0.034	0.023	19.861	-0.205	-0.205	0.000	0.000	0.000	0.000
142	A	148	TYR	0	0.042	0.027	13.031	-1.191	-1.191	0.000	0.000	0.000	0.000
143	A	149	SER	0	0.028	-0.002	17.522	-0.717	-0.717	0.000	0.000	0.000	0.000
144	A	150	ALA	0	0.008	0.000	19.252	-0.378	-0.378	0.000	0.000	0.000	0.000
145	A	151	SER	0	-0.053	-0.032	15.591	-0.573	-0.573	0.000	0.000	0.000	0.000
146	A	152	LYS	1	0.838	0.917	9.657	23.708	23.708	0.000	0.000	0.000	0.000
147	A	153	GLY	0	0.074	0.046	15.172	-0.471	-0.471	0.000	0.000	0.000	0.000
148	A	154	GLY	0	-0.022	-0.003	18.078	0.082	0.082	0.000	0.000	0.000	0.000
149	A	155	LEU	0	-0.002	-0.014	11.079	0.010	0.010	0.000	0.000	0.000	0.000
150	A	156	VAL	0	-0.001	0.022	14.897	-0.709	-0.709	0.000	0.000	0.000	0.000
151	A	157	GLY	0	0.023	0.011	16.685	0.128	0.128	0.000	0.000	0.000	0.000
152	A	158	PHE	0	0.030	0.013	13.193	0.230	0.230	0.000	0.000	0.000	0.000
153	A	159	SER	0	0.021	-0.010	13.715	-0.651	-0.651	0.000	0.000	0.000	0.000
154	A	160	ARG	1	0.879	0.931	15.845	14.894	14.894	0.000	0.000	0.000	0.000
155	A	161	ALA	0	-0.014	0.003	19.320	0.599	0.599	0.000	0.000	0.000	0.000
156	A	162	LEU	0	0.052	0.021	14.253	0.261	0.261	0.000	0.000	0.000	0.000
157	A	163	ALA	0	0.011	-0.009	17.640	0.049	0.049	0.000	0.000	0.000	0.000
158	A	164	LYS	1	0.925	0.962	18.444	12.824	12.824	0.000	0.000	0.000	0.000
159	A	165	GLU	-1	-0.931	-0.944	20.476	-13.966	-13.966	0.000	0.000	0.000	0.000
160	A	166	VAL	0	-0.035	-0.033	15.927	0.323	0.323	0.000	0.000	0.000	0.000
161	A	167	ALA	0	0.072	0.050	19.293	-0.101	-0.101	0.000	0.000	0.000	0.000
162	A	168	ARG	1	0.986	0.988	20.350	12.108	12.108	0.000	0.000	0.000	0.000
163	A	169	LYS	1	0.862	0.930	19.073	15.171	15.171	0.000	0.000	0.000	0.000
164	A	170	LYS	1	0.872	0.936	19.340	13.180	13.180	0.000	0.000	0.000	0.000
165	A	171	ILE	0	0.006	0.032	13.649	-0.757	-0.757	0.000	0.000	0.000	0.000
166	A	172	ARG	1	0.888	0.936	13.337	21.129	21.129	0.000	0.000	0.000	0.000
167	A	173	VAL	0	0.005	0.015	11.800	-1.996	-1.996	0.000	0.000	0.000	0.000
168	A	174	ASN	0	-0.004	-0.004	11.702	2.863	2.863	0.000	0.000	0.000	0.000
169	A	175	VAL	0	-0.013	-0.012	10.951	-1.943	-1.943	0.000	0.000	0.000	0.000
170	A	176	VAL	0	0.009	0.011	9.234	0.922	0.922	0.000	0.000	0.000	0.000
171	A	177	ALA	0	-0.001	-0.011	11.095	-0.811	-0.811	0.000	0.000	0.000	0.000
172	A	178	PRO	0	-0.032	-0.012	11.046	0.828	0.828	0.000	0.000	0.000	0.000
173	A	179	GLY	0	0.103	0.050	13.816	0.427	0.427	0.000	0.000	0.000	0.000
174	A	180	PHE	0	0.013	0.009	16.127	-0.826	-0.826	0.000	0.000	0.000	0.000
175	A	181	VAL	0	-0.047	-0.027	11.756	-0.145	-0.145	0.000	0.000	0.000	0.000
176	A	182	HIS	0	0.055	0.025	15.159	-0.637	-0.637	0.000	0.000	0.000	0.000
177	A	183	THR	0	-0.055	-0.037	16.783	-0.397	-0.397	0.000	0.000	0.000	0.000
178	A	184	ASP	-1	-0.822	-0.933	18.420	-11.596	-11.596	0.000	0.000	0.000	0.000
179	A	185	MET	0	0.035	0.044	21.222	0.539	0.539	0.000	0.000	0.000	0.000
180	A	186	THR	0	-0.058	-0.041	22.723	-0.132	-0.132	0.000	0.000	0.000	0.000
181	A	187	LYS	1	0.808	0.879	24.387	10.397	10.397	0.000	0.000	0.000	0.000
182	A	188	ASP	-1	-0.805	-0.896	22.126	-12.841	-12.841	0.000	0.000	0.000	0.000
183	A	189	LEU	0	-0.022	-0.006	24.289	0.325	0.325	0.000	0.000	0.000	0.000
184	A	190	LYS	1	0.743	0.838	23.326	12.284	12.284	0.000	0.000	0.000	0.000
185	A	191	GLU	-1	-0.815	-0.891	28.051	-9.224	-9.224	0.000	0.000	0.000	0.000
186	A	192	GLU	-1	-0.814	-0.892	28.081	-10.619	-10.619	0.000	0.000	0.000	0.000
187	A	193	HIS	0	-0.023	-0.015	28.462	0.384	0.384	0.000	0.000	0.000	0.000
188	A	194	LEU	0	0.071	0.049	24.446	0.065	0.065	0.000	0.000	0.000	0.000
189	A	195	LYS	1	0.794	0.878	24.369	11.181	11.181	0.000	0.000	0.000	0.000
190	A	196	LYS	1	0.955	0.984	26.058	8.390	8.390	0.000	0.000	0.000	0.000
191	A	197	ASN	0	0.018	0.008	27.360	0.405	0.405	0.000	0.000	0.000	0.000
192	A	198	ILE	0	-0.045	-0.008	21.792	-0.184	-0.184	0.000	0.000	0.000	0.000
193	A	199	PRO	0	0.012	0.010	25.397	0.098	0.098	0.000	0.000	0.000	0.000
194	A	200	LEU	0	-0.027	-0.001	21.165	0.152	0.152	0.000	0.000	0.000	0.000
195	A	201	GLY	0	0.020	0.028	23.827	-0.364	-0.364	0.000	0.000	0.000	0.000
196	A	202	ARG	1	0.796	0.869	18.511	13.888	13.888	0.000	0.000	0.000	0.000
197	A	203	PHE	0	0.066	0.043	18.634	-0.343	-0.343	0.000	0.000	0.000	0.000
198	A	204	GLY	0	0.039	0.046	16.064	-0.025	-0.025	0.000	0.000	0.000	0.000
199	A	205	GLU	0	0.023	-0.007	14.263	-0.385	-0.385	0.000	0.000	0.000	0.000
200	A	206	THR	0	0.008	-0.005	8.801	-0.860	-0.860	0.000	0.000	0.000	0.000
201	A	207	ILE	0	0.052	0.024	9.166	-1.835	-1.835	0.000	0.000	0.000	0.000
202	A	208	GLU	0	0.064	0.043	10.802	-0.216	-0.216	0.000	0.000	0.000	0.000
203	A	209	VAL	0	0.014	0.003	8.885	-0.092	-0.092	0.000	0.000	0.000	0.000
204	A	210	ALA	0	-0.015	-0.006	7.186	-1.143	-1.143	0.000	0.000	0.000	0.000
205	A	211	HIS	0	0.022	-0.010	8.065	-0.717	-0.717	0.000	0.000	0.000	0.000
206	A	212	ALA	0	0.021	0.020	11.175	0.408	0.408	0.000	0.000	0.000	0.000
207	A	213	VAL	0	-0.023	-0.020	5.035	-0.333	-0.333	0.000	0.000	0.000	0.000
208	A	214	VAL	0	0.014	0.004	8.003	-0.554	-0.554	0.000	0.000	0.000	0.000
209	A	215	PHE	0	0.047	0.029	8.808	0.761	0.761	0.000	0.000	0.000	0.000
210	A	216	LEU	0	-0.023	-0.007	10.573	0.967	0.967	0.000	0.000	0.000	0.000
211	A	217	LEU	0	-0.075	-0.021	5.123	-0.158	-0.158	0.000	0.000	0.000	0.000
212	A	218	GLU	-1	-0.780	-0.884	9.848	-22.927	-22.927	0.000	0.000	0.000	0.000
213	A	219	SER	0	-0.002	0.004	12.678	1.776	1.776	0.000	0.000	0.000	0.000
214	A	220	PRO	0	-0.031	-0.025	15.657	-0.372	-0.372	0.000	0.000	0.000	0.000
215	A	221	TYR	0	-0.018	-0.016	18.168	0.210	0.210	0.000	0.000	0.000	0.000
216	A	222	ILE	0	0.022	0.034	16.350	0.434	0.434	0.000	0.000	0.000	0.000
217	A	223	THR	0	0.005	-0.010	16.151	-1.561	-1.561	0.000	0.000	0.000	0.000
218	A	224	GLY	0	0.030	0.019	16.400	0.968	0.968	0.000	0.000	0.000	0.000
219	A	225	HIS	0	0.019	0.021	16.583	0.784	0.784	0.000	0.000	0.000	0.000
220	A	226	VAL	0	-0.022	-0.027	15.029	-1.236	-1.236	0.000	0.000	0.000	0.000
221	A	227	LEU	0	0.002	0.018	13.917	0.919	0.919	0.000	0.000	0.000	0.000
222	A	228	VAL	0	0.036	0.015	14.302	-1.210	-1.210	0.000	0.000	0.000	0.000
223	A	229	VAL	0	-0.065	-0.028	12.329	0.208	0.208	0.000	0.000	0.000	0.000
224	A	230	ASP	-1	-0.790	-0.902	15.508	-13.353	-13.353	0.000	0.000	0.000	0.000
225	A	231	GLY	0	0.009	0.008	18.846	0.117	0.117	0.000	0.000	0.000	0.000
226	A	232	GLY	0	0.043	0.007	21.233	0.494	0.494	0.000	0.000	0.000	0.000
227	A	233	LEU	0	0.021	0.014	20.185	0.319	0.319	0.000	0.000	0.000	0.000
228	A	234	GLN	0	-0.019	-0.025	21.498	0.009	0.009	0.000	0.000	0.000	0.000
229	A	235	LEU	0	-0.041	-0.019	23.515	0.220	0.220	0.000	0.000	0.000	0.000
230	A	236	ILE	0	-0.026	0.004	26.422	0.389	0.389	0.000	0.000	0.000	0.000
231	A	237	LEU	-1	-0.930	-0.953	24.280	-11.944	-11.944	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:7:VAL)