PDB/UniProt Mapping

------------------------------------------------
         PDB             ||      UniProt        
-------------------------||---------------------
PDB  Chn  SeqNo Res ResNo||Accession Res  Number
------------------------------------------------
3s5p A        1 PRO -2                          
3s5p A        2 GLY -1                          
3s5p A        3 SER 0                           
3s5p A        4 MET 1      A8B2K2    M         1
3s5p A        5 LYS 2      A8B2K2    K         2
3s5p A        6 VAL 3      A8B2K2    V         3
3s5p A        7 ALA 4      A8B2K2    A         4
3s5p A        8 PHE 5      A8B2K2    F         5
3s5p A        9 ALA 6      A8B2K2    A         6
3s5p A       10 SER 7      A8B2K2    S         7
3s5p A       11 ASP 8      A8B2K2    D         8
3s5p A       12 HIS 9      A8B2K2    H         9
3s5p A       13 GLY 10     A8B2K2    G        10
3s5p A       14 GLY 11     A8B2K2    G        11
3s5p A       15 ARG 12     A8B2K2    R        12
3s5p A       16 ASP 13     A8B2K2    D        13
3s5p A       17 LEU 14     A8B2K2    L        14
3s5p A       18 ARG 15     A8B2K2    R        15
3s5p A       19 MET 16     A8B2K2    M        16
3s5p A       20 PHE 17     A8B2K2    F        17
3s5p A       21 LEU 18     A8B2K2    L        18
3s5p A       22 GLN 19     A8B2K2    Q        19
3s5p A       23 GLN 20     A8B2K2    Q        20
3s5p A       24 ARG 21     A8B2K2    R        21
3s5p A       25 ALA 22     A8B2K2    A        22
3s5p A       26 SER 23     A8B2K2    S        23
3s5p A       27 ALA 24     A8B2K2    A        24
3s5p A       28 HIS 25     A8B2K2    H        25
3s5p A       29 GLY 26     A8B2K2    G        26
3s5p A       30 TYR 27     A8B2K2    Y        27
3s5p A       31 GLU 28     A8B2K2    E        28
3s5p A       32 VAL 29     A8B2K2    V        29
3s5p A       33 MET 30     A8B2K2    M        30
3s5p A       34 ASP 31     A8B2K2    D        31
3s5p A       35 LEU 32     A8B2K2    L        32
3s5p A       36 GLY 33     A8B2K2    G        33
3s5p A       37 THR 34     A8B2K2    T        34
3s5p A       38 PRO 43     A8B2K2    P        43
3s5p A       39 ASP 44     A8B2K2    D        44
3s5p A       40 PHE 45     A8B2K2    F        45
3s5p A       41 ALA 46     A8B2K2    A        46
3s5p A       42 LYS 47     A8B2K2    K        47
3s5p A       43 ILE 48     A8B2K2    I        48
3s5p A       44 GLY 49     A8B2K2    G        49
3s5p A       45 CYS 50     A8B2K2    C        50
3s5p A       46 GLU 51     A8B2K2    E        51
3s5p A       47 ALA 52     A8B2K2    A        52
3s5p A       48 VAL 53     A8B2K2    V        53
3s5p A       49 THR 54     A8B2K2    T        54
3s5p A       50 SER 55     A8B2K2    S        55
3s5p A       51 GLY 56     A8B2K2    G        56
3s5p A       52 ARG 57     A8B2K2    R        57
3s5p A       53 ALA 58     A8B2K2    A        58
3s5p A       54 ASP 59     A8B2K2    D        59
3s5p A       55 CYS 60     A8B2K2    C        60
3s5p A       56 CYS 61     A8B2K2    C        61
3s5p A       57 ILE 62     A8B2K2    I        62
3s5p A       58 LEU 63     A8B2K2    L        63
3s5p A       59 VAL 64     A8B2K2    V        64
3s5p A       60 CYS 65     A8B2K2    C        65
3s5p A       61 GLY 66     A8B2K2    G        66
3s5p A       62 THR 67     A8B2K2    T        67
3s5p A       63 GLY 68     A8B2K2    G        68
3s5p A       64 ILE 69     A8B2K2    I        69
3s5p A       65 GLY 70     A8B2K2    G        70
3s5p A       66 ILE 71     A8B2K2    I        71
3s5p A       67 SER 72     A8B2K2    S        72
3s5p A       68 ILE 73     A8B2K2    I        73
3s5p A       69 ALA 74     A8B2K2    A        74
3s5p A       70 ALA 75     A8B2K2    A        75
3s5p A       71 ASN 76     A8B2K2    N        76
3s5p A       72 LYS 77     A8B2K2    K        77
3s5p A       73 MET 78     A8B2K2    M        78
3s5p A       74 LYS 79     A8B2K2    K        79
3s5p A       75 GLY 80     A8B2K2    G        80
3s5p A       76 ILE 81     A8B2K2    I        81
3s5p A       77 ARG 82     A8B2K2    R        82
3s5p A       78 CYS 83     A8B2K2    C        83
3s5p A       79 ALA 84     A8B2K2    A        84
3s5p A       80 LEU 85     A8B2K2    L        85
3s5p A       81 CYS 86     A8B2K2    C        86
3s5p A       82 SER 87     A8B2K2    S        87
3s5p A       83 THR 88     A8B2K2    T        88
3s5p A       84 GLU 89     A8B2K2    E        89
3s5p A       85 TYR 90     A8B2K2    Y        90
3s5p A       86 ASP 91     A8B2K2    D        91
3s5p A       87 ALA 92     A8B2K2    A        92
3s5p A       88 GLU 93     A8B2K2    E        93
3s5p A       89 MET 94     A8B2K2    M        94
3s5p A       90 ALA 95     A8B2K2    A        95
3s5p A       91 ARG 96     A8B2K2    R        96
3s5p A       92 LYS 97     A8B2K2    K        97
3s5p A       93 HIS 98     A8B2K2    H        98
3s5p A       94 ASN 99     A8B2K2    N        99
3s5p A       95 ASN 100    A8B2K2    N       100
3s5p A       96 ALA 101    A8B2K2    A       101
3s5p A       97 ASN 102    A8B2K2    N       102
3s5p A       98 ALA 103    A8B2K2    A       103
3s5p A       99 LEU 104    A8B2K2    L       104
3s5p A      100 ALA 105    A8B2K2    A       105
3s5p A      101 LEU 106    A8B2K2    L       106
3s5p A      102 GLY 107    A8B2K2    G       107
3s5p A      103 GLY 108    A8B2K2    G       108
3s5p A      104 ARG 109    A8B2K2    R       109
3s5p A      105 THR 110    A8B2K2    T       110
3s5p A      106 THR 111    A8B2K2    T       111
3s5p A      107 GLY 112    A8B2K2    G       112
3s5p A      108 PRO 113    A8B2K2    P       113
3s5p A      109 GLU 114    A8B2K2    E       114
3s5p A      110 VAL 115    A8B2K2    V       115
3s5p A      111 ALA 116    A8B2K2    A       116
3s5p A      112 ALA 117    A8B2K2    A       117
3s5p A      113 SER 118    A8B2K2    S       118
3s5p A      114 ILE 119    A8B2K2    I       119
3s5p A      115 LEU 120    A8B2K2    L       120
3s5p A      116 SER 121    A8B2K2    S       121
3s5p A      117 ARG 122    A8B2K2    R       122
3s5p A      118 PHE 123    A8B2K2    F       123
3s5p A      119 LEU 124    A8B2K2    L       124
3s5p A      120 SER 125    A8B2K2    S       125
3s5p A      121 THR 126    A8B2K2    T       126
3s5p A      122 ASN 127    A8B2K2    N       127
3s5p A      123 PHE 128    A8B2K2    F       128
3s5p A      124 GLU 129    A8B2K2    E       129
3s5p A      125 GLY 130    A8B2K2    G       130
3s5p A      126 GLY 131    A8B2K2    G       131
3s5p A      127 ARG 132    A8B2K2    R       132
3s5p A      128 HIS 133    A8B2K2    H       133
3s5p A      129 ALA 134    A8B2K2    A       134
3s5p A      130 ALA 135    A8B2K2    A       135
3s5p A      131 ARG 136    A8B2K2    R       136
3s5p A      132 ILE 137    A8B2K2    I       137
3s5p A      133 ALA 138    A8B2K2    A       138
3s5p A      134 LYS 139    A8B2K2    K       139

A total of 134 residues were displayed (of which 131 were aligned with UniProt) for 1 chains.

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