*HEADER   R1MRBMR   14-MAY-90 
*COMPND   CD-7 METALLOTHIONEIN-2A (/NMR$)
*SOURCE   RABBIT (ORYCTOLAGUS $CUNICULUS) LIVER
*EXPDTA   NMR
*AUTHOR   W.BRAUN,A.ARSENIEV,P.SCHULTZE,E.WOERGOETTER,G.WAGNER,        
*AUTHOR  2 M.VASAK,J.H.R.KAEGI,K.WUTHRICH                              
*COORDS   1MRB,2MRB
*REMARK                                                                         
*REMARK    HYDROGEN ATOMS IN THIS ENTRY HAVE BEEN ASSIGNED NAMES                
*REMARK    CONSISTENT WITH THE RECOMMENDATIONS OF THE IUPAC-IUB                 
*REMARK    COMMISSION ON BIOCHEMICAL NOMENCLATURE (SEE,E.G., J.MOL.             
*REMARK    BIOL. 52, 1 (1970)).  THE PROTEIN DATA BANK HAS FOLLOWED             
*REMARK    RULE 4.4 OF THE RECOMMENDATIONS WITH THE FOLLOWING                   
*REMARK    MODIFICATION - WHEN MORE THAN ONE HYDROGEN ATOM IS BONDED            
*REMARK    TO A SINGLE NON-HYDROGEN ATOM, THE HYDROGEN ATOM NUMBER              
*REMARK    DESIGNATION IS GIVEN AS THE FIRST CHARACTER OF THE ATOM              
*REMARK    NAME RATHER THAN AS THE LAST CHARACTER (E.G. H*BETA*1 IS             
*REMARK    DENOTED AS 1HB).  
*REMARK

HEADER    NMR DATA FOR 1MRB                        3-MAY-90   1MRB      1MRB   3
COMPND    CD-7 METALLOTHIONEIN-2A                                       1MRB   4
SOURCE    RABBIT LIVER                                                  1MRB   5
AUTHOR    W.BRAUN,A.ARSENIEV,P.SCHULTZE,E.WORGOTTER,G.WAGNER,           1MRB   6
AUTHOR    M.VASAK,J.H.R.KAGI,K.WUTHRICH                                 1MRB   7
COORDS    1MRB                                                          1MRB   8
REMARK   1                                                              1MRB   9
REMARK   1 REFERENCE 1                                                  1MRB  10
REMARK   1  AUTH   G.WAGNER,D.NEUHAUS,E.WORGOTTER,                      1MRB  11
REMARK   1  AUTH 2 M.VASAK,J.H.R.KAGI,K.WUTHRICH                        1MRB  12
REMARK   1  TITL   SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS IN RABBIT-LIVER 1MRB  13
REMARK   1  TITL 2 METALLOTHIONEIN-2                                    1MRB  14
REMARK   1  REF    EUR.J.BIOCHEM.                V. 157   275 1986      1MRB  15
REMARK   1  REFN   ASTM EJBCAI  IX ISSN 0014-2956                  262  1MRB  16
REMARK   2                                                              1MRB  17
REMARK   2 THIS FILE CONTAINS DATA THAT WAS USED IN THE DETERMINATION   1MRB  18
REMARK   2 OF THE THREE-DIMENSIONAL STRUCTURE OF 1MRB BY NUCLEAR        1MRB  19
REMARK   2 MAGNETIC RESONANCE IN SOLUTION.                              1MRB  20
REMARK   3                                                              1MRB  21
REMARK   3 INPUT DATA. 129 UPPER LIMIT DISTANCE CONSTRAINTS FROM NOESY  1MRB  22
REMARK   3 SPECTRA IN H2O AND D2O AT 14 DEGREES CELSIUS AND PH 7.0.     1MRB  23
REMARK   3 IN ADDITION UPPER AND LOWER DISTANCE CONSTRAINTS             1MRB  24
REMARK   3 WERE USED TO ENSURE THE CD-CYS CO-ORDINATIVE BONDS           1MRB  25
REMARK   3 WITH TETRAHEDRAL CO-ORDINATION GEOMETRY AT EACH METAL ION    1MRB  26
REMARK   3 AS DESCRIBED IN TABLE 1 OF ARSENIEV ET AL., J.MOL.BIOL.      1MRB  27
REMARK   3 (1988), VOL. 201, p.637. A LIST OF THE CHEMICAL SHIFTS       1MRB  28
REMARK   3 FOR THIS PROTEIN CAN BE FOUND IN REFERENCE 1.                1MRB  29
REMARK   4                                                              1MRB  30
REMARK   4 THE DIFFERENT KINDS OF DATA TOGETHER WITH THE CORRESPONDING  1MRB  31
REMARK   4 RECORD IDENTIFIERS ARE GIVEN IN THE FOLLOWING TABLE.         1MRB  32
REMARK   4                                                              1MRB  33
REMARK   4 RECORD CONTENT                                     UNIT      1MRB  34
REMARK   4 ------ ------------------------------------------- --------- 1MRB  35
REMARK   4 NOEUPP UPPER LIMITS FOR INTERATOMIC DISTANCES      ANGSTROMS 1MRB  36
REMARK   4        DETERMINED FROM NUCLEAR OVERHAUSER EFFECTS            1MRB  37
REMARK   4 ANGLE  TORSION ANGLE CONSTRAINTS IN THE FORM OF    DEGREES   1MRB  38
REMARK   4        AN ALLOWED INTERVAL                                   1MRB  39
REMARK   4                                                              1MRB  40
REMARK   4 THE NEXT TABLE CONTAINS A DETAILED DESCRIPTION OF THE        1MRB  41
REMARK   4 CONTENTS AND FORMATS OF THE VARIOUS DATA RECORDS AND THE     1MRB  42
REMARK   4 MASTER RECORD.                                               1MRB  43
REMARK   4                                                              1MRB  44
REMARK   4 RECORD CONTENTS (FORTRAN FORMAT)                             1MRB  45
REMARK   4 ------ ----------------------------------------------------- 1MRB  46
REMARK   4 NOEUPP FIRST RESIDUE NAME, FIRST RESIDUE NUMBER, FIRST ATOM  1MRB  47
REMARK   4        NAME, SECOND RESIDUE NAME, SECOND RESIDUE NUMBER,     1MRB  48
REMARK   4        SECOND ATOM NAME, UPPER DISTANCE LIMIT, FIRST ATOM    1MRB  49
REMARK   4        NAME, SECOND RESIDUE NAME, SECOND RESIDUE NUMBER,     1MRB  50
REMARK   4        SECOND ATOM NAME, UPPER DISTANCE LIMIT                1MRB  51
REMARK   4        ('NOEUPP',2X,A4,I4,1X,2(A4,1X,A4,I4,1X,A4,F6.2,5X))   1MRB  52
REMARK   4 ANGLE  RESIDUE NAME, RESIDUE NUMBER, ANGLE NAME, LOWER AND   1MRB  53
REMARK   4        UPPER BOUND, ANGLE NAME, LOWER AND UPPER BOUND        1MRB  54
REMARK   4        ('ANGLE',3X,A4,I4,1X,2(A5,2F8.2,8X))                  1MRB  55
REMARK   4 MASTER NUMBER OF REMARK RECORDS, NUMBER OF FTNOTE RECORDS,   1MRB  56
REMARK   4        NUMBER OF SHIFTS RECORDS, NUMBER OF JCOUPL RECORDS,   1MRB  57
REMARK   4        NUMBER OF NOEUPP, HBUPP AND SSUPP RECORDS, NUMBER OF  1MRB  58
REMARK   4        NOELOW, HBLOW AND SSLOW RECORDS, NUMBER OF ANGLE      1MRB  59
REMARK   4        RECORDS                                               1MRB  60
REMARK   4        ('MASTER',4X,7I5)                                     1MRB  61
REMARK   5                                                              1MRB  62
REMARK   5 ATOM NAMES HAVE BEEN ASSIGNED FOLLOWING THE RECOMMENDATIONS  1MRB  63
REMARK   5 OF THE IUPAC-IUB COMMISSION AS PUBLISHED IN BIOCHEMISTRY     1MRB  64
REMARK   5 (1970) VOL. 9, 3471-3479, EXCEPT THAT BACKBONE AMIDE         1MRB  65
REMARK   5 HYDROGENS ARE DENOTED BY HN INSTEAD OF H. THE HYDROGEN ATOM  1MRB  66
REMARK   5 NUMBERS OF THOSE HYDROGEN ATOMS WHICH ARE CONNECTED TO THE   1MRB  67
REMARK   5 SAME NON-HYDROGEN ATOM ARE WRITTEN AS THE FIRST CHARACTER    1MRB  68
REMARK   5 RATHER THAN THE LAST CHARACTER OF THE ATOM NAMES.            1MRB  69
REMARK   5 THEY ARE IDENTICAL WITH THE ATOM NAMES USED IN THE CO-       1MRB  70
REMARK   5 ORDINATE FILE 1MRB.                                          1MRB  71
REMARK   6                                                              1MRB  72
REMARK   6 PSEUDO-ATOMS DESIGNATED AS Q ARE DIMENSIONLESS REFERENCE     1MRB  73
REMARK   6 POINTS REPRESENTING A GROUP OF HYDROGEN ATOMS                1MRB  74
REMARK   6 (K.WUTHRICH, M.BILLETER AND W.BRAUN, J. MOL. BIOL. (1983)    1MRB  75
REMARK   6 VOL. 169, 949-961). THEY ARE USED TO DESCRIBE ALL METHYL     1MRB  76
REMARK   6 GROUPS, AND THOSE GROUPS OF PROCHIRAL HYDROGEN ATOMS FOR     1MRB  77
REMARK   6 WHICH NO STEREOSPECIFIC ASSIGNMENTS HAD BEEN OBTAINED.       1MRB  78
REMARK   7                                                              1MRB  79
REMARK   7 DETAILS OF THE NOMENCLATURE FOR THE PSEUDO-ATOMS ARE         1MRB  80
REMARK   7 AS FOLLOWS: QA REPRESENTS THE TWO METHYLENE HYDROGEN         1MRB  81
REMARK   7 ATOMS OF GLY. QB, QG, ... REPRESENT BETA, GAMMA, ...         1MRB  82
REMARK   7 METHYLENE OR METHYL GROUPS IN THE SIDE CHAINS. IN CASE OF    1MRB  83
REMARK   7 BRANCHES IN THE SIDE CHAINS THE NUMBERS OF THE PSEUDO-ATOMS  1MRB  84
REMARK   7 ARE THE SAME AS THE NUMBERS OF THE CARBONS TO WHICH THE      1MRB  85
REMARK   7 HYDROGEN  ATOMS ARE ATTACHED.                                1MRB  86
REMARK   7 QQG DENOTES THE PSEUDO-ATOM FOR THE 6 HYDROGEN               1MRB  87
REMARK   7 ATOMS OF THE ISOPROPYL METHYL GROUPS OF VAL.                 1MRB  88
REMARK   7                                                              1MRB  89
NOEUPP  MET    1  HA  ASP    2  HN   2.40                               1MRB  90
NOEUPP  ASN    4  HN  CYS    5  HN   2.70      HN  ALA   24  QB   5.50  1MRB  91
NOEUPP  ASN    4  HA  LYS   23  HN   5.50      HA  LYS   23  QB   5.00  1MRB  92
NOEUPP  ASN    4  HA  ALA   24  QB   5.00      QB  ALA   24  HN   4.10  1MRB  93
NOEUPP  ASN    4  QB  ALA   24  QB   5.00      ND2 ALA   24  QB   5.10  1MRB  94
NOEUPP  CYS    5  HN  ALA   24  QB   6.50      HA  SER    6  HN   2.40  1MRB  95
NOEUPP  CYS    5  HA  CYS    7  HN   4.00      HA  CYS   22  HN   4.00  1MRB  96
NOEUPP  CYS    5  HA  CYS   22  HA   5.50      HA  CYS   22  QB   4.00  1MRB  97
NOEUPP  CYS    5  HA  LYS   23  HN   5.50      HA  CYS   25  HA   4.00  1MRB  98
NOEUPP  CYS    5  HA  CYS   25  QB   6.50      HA  LYS   26  HN   5.50  1MRB  99
NOEUPP  CYS    5  QB  CYS   22  QB   6.00      QB  CYS   25  HA   4.00  1MRB 100
NOEUPP  CYS    5  QB  LYS   26  HN   4.10      QB  LYS   26  QB   7.50  1MRB 101
NOEUPP  SER    6  HN  CYS   22  QB   4.10                               1MRB 102
NOEUPP  ALA    8  HA  ALA    9  HN   2.70                               1MRB 103
NOEUPP  GLY   11  QA  ASP   12  HN   3.70                               1MRB 104
NOEUPP  SER   13  HA  CYS   14  HN   2.70                               1MRB 105
NOEUPP  CYS   16  HN  ALA   17  HN   3.10      QB  CYS   20  HA   5.00  1MRB 106
NOEUPP  CYS   16  QB  THR   21  HN   6.50                               1MRB 107
NOEUPP  ALA   17  QB  ASN   18  HN   4.10                               1MRB 108
NOEUPP  ASN   18  QB  SER   19  HN   4.10                               1MRB 109
NOEUPP  CYS   20  HA  THR   21  HN   2.40      HA  CYS   22  HN   4.00  1MRB 110
NOEUPP  THR   21  HN  CYS   22  HN   2.70                               1MRB 111
NOEUPP  CYS   22  QB  LYS   23  HN   4.10      QB  ALA   24  HN   4.10  1MRB 112
NOEUPP  CYS   22  QB  CYS   25  HA   6.50      QB  CYS   25  QB   6.00  1MRB 113
NOEUPP  ALA   24  HA  CYS   25  HN   2.40                               1MRB 114
NOEUPP  CYS   25  HA  LYS   26  HN   2.40                               1MRB 115
NOEUPP  LYS   26  HN  CYS   27  HN   2.70                               1MRB 116
NOEUPP  CYS   27  HA  THR   28  HN   2.40      QB  THR   28  HN   4.10  1MRB 117
NOEUPP  CYS   27  QB  SER   29  HN   5.00                               1MRB 118
NOEUPP  THR   28  HA  CYS   30  HN   4.00      HA  LYS   31  QB   5.00  1MRB 119
NOEUPP  SER   29  HN  CYS   30  HN   2.70                               1MRB 120
NOEUPP  CYS   30  HA  LYS   31  HN   2.70                               1MRB 121
NOEUPP  LYS   32  HA  SER   33  HN   2.40      QB  SER   33  HN   4.10  1MRB 122
NOEUPP  SER   33  HN  PRO   40  QG   6.50      HA  PRO   40  HA   5.50  1MRB 123
NOEUPP  SER   33  HA  PRO   40  QB   4.00      QB  CYS   35  HN   4.10  1MRB 124
NOEUPP  SER   33  QB  PRO   40  HA   6.50      QB  PRO   40  QB   6.00  1MRB 125
NOEUPP  CYS   34  HA  CYS   49  QB   6.50      QB  CYS   49  HN   6.50  1MRB 126
NOEUPP  CYS   35  HA  SER   36  HN   2.40      HA  CYS   51  QB   6.50  1MRB 127
NOEUPP  CYS   35  QB  SER   36  HN   3.70      QB  CYS   37  HN   4.10  1MRB 128
NOEUPP  CYS   35  QB  CYS   51  QB   6.00                               1MRB 129
NOEUPP  SER   36  HN  CYS   37  HN   2.70                               1MRB 130
NOEUPP  CYS   37  HN  CYS   38  HN   2.70      HA  LYS   57  HA   4.00  1MRB 131
NOEUPP  CYS   37  HA  CYS   58  QB   6.50      QB  LYS   57  HA   4.00  1MRB 132
NOEUPP  CYS   37  QB  CYS   58  HN   4.10      QB  CYS   58  HA   5.00  1MRB 133
NOEUPP  CYS   37  QB  CYS   58  QB   6.00                               1MRB 134
NOEUPP  CYS   38  HA  CYS   42  HN   5.50      HA  CYS   42  QB   5.00  1MRB 135
NOEUPP  PRO   40  HA  GLY   41  HN   2.40      HA  CYS   42  HN   4.00  1MRB 136
NOEUPP  GLY   41  HN  CYS   42  HN   2.70                               1MRB 137
NOEUPP  CYS   42  HN  CYS   45  QB   5.00      HA  ALA   43  HN   2.40  1MRB 138
NOEUPP  CYS   42  QB  CYS   45  HN   5.00      QB  CYS   45  QB   6.00  1MRB 139
NOEUPP  ALA   43  HN  LYS   44  HN   2.70                               1MRB 140
NOEUPP  LYS   44  HN  CYS   45  HN   2.40      HN  ALA   46  HN   4.00  1MRB 141
NOEUPP  LYS   44  HN  ILE   50  QD1  6.50      HA  ILE   50  QG1  6.50  1MRB 142
NOEUPP  LYS   44  HA  ILE   50  QD1  5.00      QB  ILE   50  QD1  5.00  1MRB 143
NOEUPP  LYS   44  QB  CYS   61  HA   6.50                               1MRB 144
NOEUPP  CYS   45  HN  ALA   46  HN   2.40      HN  ILE   50  QD1  6.50  1MRB 145
NOEUPP  CYS   45  HA  GLY   48  HN   5.50      HA  CYS   49  HA   5.50  1MRB 146
NOEUPP  CYS   45  HA  ILE   50  HN   4.00      HA  ILE   50  QG2  5.00  1MRB 147
NOEUPP  CYS   45  HA  ILE   50  QD1  5.00      QB  CYS   49  HA   4.00  1MRB 148
NOEUPP  CYS   45  QB  ILE   50  HN   5.00                               1MRB 149
NOEUPP  ALA   46  HN  GLN   47  HN   3.10      HA  GLY   48  HN   4.00  1MRB 150
NOEUPP  GLN   47  HN  GLY   48  HN   2.40                               1MRB 151
NOEUPP  GLY   48  QA  CYS   49  HN   3.40                               1MRB 152
NOEUPP  CYS   49  HA  ILE   50  HN   2.40      HA  CYS   51  HN   4.00  1MRB 153
NOEUPP  ILE   50  HN  CYS   51  HN   2.40      QD1 CYS   60  HN   6.50  1MRB 154
NOEUPP  ILE   50  QD1 CYS   60  HA   5.00      QD1 CYS   60  QB   6.00  1MRB 155
NOEUPP  ILE   50  QD1 CYS   61  HN   6.50                               1MRB 156
NOEUPP  CYS   51  HA  LYS   52  HN   2.80      QB  LYS   52  HN   4.10  1MRB 157
NOEUPP  LYS   52  HA  GLY   53  HN   3.10      QB  GLY   53  HN   4.10  1MRB 158
NOEUPP  GLY   53  QA  ALA   54  HN   3.70                               1MRB 159
NOEUPP  ALA   54  HA  SER   55  HN   2.80      QB  CYS   58  HA   5.00  1MRB 160
NOEUPP  ALA   54  QB  CYS   58  QB   7.50                               1MRB 161
NOEUPP  SER   55  HA  ASP   56  HN   2.70                               1MRB 162
NOEUPP  ASP   56  HN  LYS   57  HN   2.70      QB  LYS   57  HN   4.10  1MRB 163
NOEUPP  LYS   57  HA  CYS   58  HN   2.40      QB  CYS   58  HN   4.10  1MRB 164
NOEUPP  SER   58  HN  CYS   58  QB   4.10      HA  SER   59  HN   2.70  1MRB 165
NOEUPP  SER   58  QB  CYS   60  HN   4.10      QB  CYS   61  HN   6.50  1MRB 166
NOEUPP  SER   59  HN  ALA   60  HN   3.10      HA  ALA   62  QB   4.00  1MRB 167
NOEUPP  CYS   60  HN  CYS   61  HN   2.40      HN  ALA   62  HN   4.00  1MRB 168
ANGLE   MET    1 PHI   -180.00  -40.00                                  1MRB 169
ANGLE   ASP    2 CHI1   150.00  210.00                                  1MRB 170
ANGLE   ASN    4 PHI   -160.00  -80.00        CHI1   -90.00  -30.00     1MRB 171
ANGLE   CYS    5 PHI   -170.00  -40.00        CHI1   150.00  210.00     1MRB 172
ANGLE   SER    6 PHI   -140.00 -100.00                                  1MRB 173
ANGLE   CYS    7 PHI   -170.00  -40.00        CHI1   -90.00  -30.00     1MRB 174
ANGLE   ASP   12 PHI   -180.00  -40.00                                  1MRB 175
ANGLE   CYS   14 PHI   -180.00  -40.00                                  1MRB 176
ANGLE   THR   15 PHI   -150.00  -90.00        CHI1    30.00   90.00     1MRB 177
ANGLE   CYS   16 PHI   -170.00  -70.00        CHI1   -90.00  -30.00     1MRB 178
ANGLE   ALA   17 PHI   -180.00  -40.00                                  1MRB 179
ANGLE   ASN   18 PHI   -180.00  -40.00                                  1MRB 180
ANGLE   SER   19 PHI   -180.00  -40.00                                  1MRB 181
ANGLE   CYS   20 PHI   -110.00  -60.00        CHI1   150.00  210.00     1MRB 182
ANGLE   THR   21 PHI   -140.00 -100.00        CHI1    30.00   90.00     1MRB 183
ANGLE   CYS   22 PHI   -100.00  -40.00        CHI1   -90.00  -30.00     1MRB 184
ANGLE   LYS   23 PHI   -180.00  -40.00                                  1MRB 185
ANGLE   ALA   24 PHI   -180.00  -40.00                                  1MRB 186
ANGLE   CYS   25 PHI   -100.00  -50.00        CHI1   150.00  210.00     1MRB 187
ANGLE   LYS   26 PHI   -130.00  -80.00        CHI1   150.00  210.00     1MRB 188
ANGLE   CYS   27 PHI   -100.00  -40.00        CHI1   -90.00  -30.00     1MRB 189
ANGLE   THR   28 CHI1    30.00   90.00                                  1MRB 190
ANGLE   CYS   30 PHI   -170.00  -70.00                                  1MRB 191
ANGLE   LYS   31 PHI   -170.00  -70.00                                  1MRB 192
ANGLE   LYS   32 PHI   -170.00  -70.00                                  1MRB 193
ANGLE   SER   33 PHI   -170.00  -70.00        CHI1   150.00  210.00     1MRB 194
ANGLE   CYS   35 PHI   -170.00  -70.00                                  1MRB 195
ANGLE   SER   36 PHI   -180.00  -60.00                                  1MRB 196
ANGLE   CYS   37 PHI   -170.00  -70.00                                  1MRB 197
ANGLE   CYS   38 PHI   -140.00 -100.00        PSI     60.00  180.00     1MRB 198
ANGLE   PRO   39 PSI     60.00  180.00                                  1MRB 199
ANGLE   CYS   42 PHI   -180.00  -60.00                                  1MRB 200
ANGLE   ALA   43 PHI   -180.00  -40.00                                  1MRB 201
ANGLE   LYS   44 PHI   -180.00  -60.00                                  1MRB 202
ANGLE   CYS   45 PHI   -150.00  -80.00        CHI1   150.00  330.00     1MRB 203
ANGLE   GLN   47 PHI   -150.00  -90.00                                  1MRB 204
ANGLE   CYS   49 PHI    -90.00  -40.00        CHI1   150.00  210.00     1MRB 205
ANGLE   ILE   50 PHI   -140.00 -100.00        CHI1    30.00   90.00     1MRB 206
ANGLE   CYS   51 PHI   -170.00  -60.00        CHI1   150.00  330.00     1MRB 207
ANGLE   SER   55 PHI   -170.00  -60.00                                  1MRB 208
ANGLE   LYS   57 PHI   -170.00  -70.00                                  1MRB 209
ANGLE   SER   58 PHI   -140.00 -100.00                                  1MRB 210
ANGLE   SER   59 PHI   -140.00 -100.00                                  1MRB 211
ANGLE   CYS   61 PHI   -140.00 -100.00        CHI1   150.00  330.00     1MRB 212
ANGLE   ALA   62 PHI   -180.00  -40.00                                  1MRB 213

*REMARK
*REMARK    THE FOLLOWING IS A LIST OF ALL HYDROGEN ATOMS WITH THEIR 
*REMARK    NAMES IN THE ENTRY AND THE ORIGINAL DATA:
  Entry H atom name              Orig H atom name
  Start of MODEL            1
 Raw file had 108 H/Q atoms
    1    H    LYS  31           HN   LYS  32  -0.338   0.478   0.828
    2    HA   LYS  31           HA   LYS  32   1.780  -0.894   0.531
    3    QB   LYS  31           QB   LYS  32   1.685   0.130  -1.953
    4    QG   LYS  31           QG   LYS  32   3.570  -1.188  -0.975
    5    QD   LYS  31           QD   LYS  32   4.690  -0.431  -2.837
    6    QE   LYS  31           QE   LYS  32   2.869  -1.298  -4.182
    7    H    SER  32           HN   SER  33   3.336   0.086   1.778
    8    HA   SER  32           HA   SER  33   2.668   2.595   2.839
    9    QB   SER  32           QB   SER  33   4.620   0.901   3.552
   10    H    CYS  33           HN   CYS  34   6.070   1.983   1.975
   11    HA   CYS  33           HA   CYS  34   6.540   3.083  -0.337
   12    QB   CYS  33           QB   CYS  34   6.006   5.270  -0.063
   13    H    CYS  34           HN   CYS  35   7.139   2.865   3.089
   14    HA   CYS  34           HA   CYS  35   9.934   2.562   2.597
   15    QB   CYS  34           QB   CYS  35  10.323   4.592   3.513
   16    H    SER  35           HN   SER  36  10.939   2.366   5.106
   17    HA   SER  35           HA   SER  36   8.962   0.750   6.517
   18    QB   SER  35           QB   SER  36  11.566  -0.056   6.213
   19    H    CYS  36           HN   CYS  37  10.328   3.665   6.602
   20    HA   CYS  36           HA   CYS  37  11.095   3.513   9.422
   21    QB   CYS  36           QB   CYS  37  12.375   5.282   8.672
   22    H    CYS  37           HN   CYS  38   8.574   4.257   7.246
   23    HA   CYS  37           HA   CYS  38   7.256   5.815   9.321
   24    QB   CYS  37           QB   CYS  38   6.755   7.015   7.088
   25    HA   PRO  38           HA   PRO  39   4.338   2.688   8.162
   26    QB   PRO  38           QB   PRO  39   3.063   2.892  10.209
   27    QG   PRO  38           QG   PRO  39   3.946   4.445  11.598
   28    QD   PRO  38           QD   PRO  39   5.586   5.581  10.380
   29    HA   PRO  39           HA   PRO  40   1.337   4.529   5.670
   30    QB   PRO  39           QB   PRO  40  -0.306   2.752   5.614
   31    QG   PRO  39           QG   PRO  40   0.203   1.092   7.065
   32    QD   PRO  39           QD   PRO  40   1.963   1.872   8.390
   33    H    GLY  40           HN   GLY  41   1.710   6.194   7.710
   34    QA   GLY  40           QA   GLY  41  -0.597   7.186   8.600
   35    H    CYS  41           HN   CYS  42   2.261   7.763   7.260
   36    HA   CYS  41           HA   CYS  42   3.176   9.547   9.308
   37    QB   CYS  41           QB   CYS  42   4.864   8.608   8.063
   38    H    ALA  42           HN   ALA  43   3.735  11.843   8.848
   39    HA   ALA  42           HA   ALA  43   1.969  12.956   6.777
   40    QB   ALA  42           QB   ALA  43   2.007  14.189   8.917
   41    H    LYS  43           HN   LYS  44   4.504  11.960   6.038
   42    HA   LYS  43           HA   LYS  44   5.680  14.394   5.086
   43    QB   LYS  43           QB   LYS  44   7.655  13.344   6.381
   44    QG   LYS  43           QG   LYS  44   6.418  14.018   8.289
   45    QD   LYS  43           QD   LYS  44   6.083  16.172   7.357
   46    QE   LYS  43           QE   LYS  44   8.445  16.470   7.223
   47    H    CYS  44           HN   CYS  45   4.260  11.853   4.212
   48    HA   CYS  44           HA   CYS  45   6.174  11.229   2.137
   49    QB   CYS  44           QB   CYS  45   5.285   8.992   3.327
   50    H    ALA  45           HN   ALA  46   3.699  12.828   2.388
   51    HA   ALA  45           HA   ALA  46   1.788  11.141   0.940
   52    QB   ALA  45           QB   ALA  46   0.856  12.985   2.294
   53    H    GLN  46           HN   GLN  47   4.423  12.613   0.054
   54    HA   GLN  46           HA   GLN  47   3.225  13.580  -2.368
   55    QB   GLN  46           QB   GLN  47   4.500  15.456  -0.859
   56    QG   GLN  46           QG   GLN  47   3.849  15.933  -3.191
   57    H    GLY  47           HN   GLY  48   4.637  11.202  -1.898
   58    QA   GLY  47           QA   GLY  48   6.593  10.895  -3.400
   59    H    CYS  48           HN   CYS  49   7.058   8.770  -1.707
   60    HA   CYS  48           HA   CYS  49   8.058   9.309   0.687
   61    QB   CYS  48           QB   CYS  49   8.554   7.190  -0.786
   62    H    ILE  49           HN   ILE  50   9.588  10.745   1.412
   63    HA   ILE  49           HA   ILE  50  11.694  11.514  -0.465
   64    HB   ILE  49           HB   ILE  50  11.737  13.558   0.512
   65    QG1  ILE  49           QG1  ILE  50  11.801  13.396   2.783
   66    QG2  ILE  49           QG2  ILE  50   9.295  13.392   0.563
   67    QD1  ILE  49           QD1  ILE  50  10.063  12.059   3.548
   68    H    CYS  50           HN   CYS  51  11.105   9.316   2.012
   69    HA   CYS  50           HA   CYS  51  13.545   9.630   3.435
   70    QB   CYS  50           QB   CYS  51  12.472   7.467   4.095
   71    H    LYS  51           HN   LYS  52  15.476   9.297   2.371
   72    HA   LYS  51           HA   LYS  52  15.946   6.756   1.164
   73    QB   LYS  51           QB   LYS  52  15.880   8.725  -0.715
   74    QG   LYS  51           QG   LYS  52  15.864   6.460  -1.486
   75    QD   LYS  51           QD   LYS  52  13.534   6.756  -0.727
   76    QE   LYS  51           QE   LYS  52  13.288   5.749  -2.856
   77    H    GLY  52           HN   GLY  53  18.102   6.226   1.344
   78    QA   GLY  52           QA   GLY  53  20.184   7.631   1.628
   79    H    ALA  53           HN   ALA  54  17.928   6.411   3.604
   80    HA   ALA  53           HA   ALA  54  19.871   5.483   5.546
   81    QB   ALA  53           QB   ALA  54  18.634   7.339   6.606
   82    H    SER  54           HN   SER  55  19.266   3.464   6.146
   83    HA   SER  54           HA   SER  55  16.483   2.779   5.661
   84    QB   SER  54           QB   SER  55  17.664   0.878   5.086
   85    H    ASP  55           HN   ASP  56  15.179   1.931   7.334
   86    HA   ASP  55           HA   ASP  56  14.669   1.143   9.331
   87    QB   ASP  55           QB   ASP  56  16.770   0.399  10.093
   88    H    LYS  56           HN   LYS  57  16.016   4.133   8.428
   89    HA   LYS  56           HA   LYS  57  14.425   5.589  10.230
   90    QB   LYS  56           QB   LYS  57  16.578   5.256  11.488
   91    QG   LYS  56           QG   LYS  57  17.198   7.512  11.075
   92    QD   LYS  56           QD   LYS  57  15.304   8.490  11.934
   93    QE   LYS  56           QE   LYS  57  15.384   7.056  13.854
   94    H    CYS  57           HN   CYS  58  14.548   7.936   9.773
   95    HA   CYS  57           HA   CYS  58  16.067   8.527   7.356
   96    QB   CYS  57           QB   CYS  58  13.984   8.630   6.471
   97    H    SER  58           HN   SER  59  15.237  11.171   6.998
   98    HA   SER  58           HA   SER  59  15.423  12.379   9.624
   99    QB   SER  58           QB   SER  59  17.327  13.103   7.784
  100    H    CYS  59           HN   CYS  60  13.524  11.981   7.130
  101    HA   CYS  59           HA   CYS  60  12.999  14.832   6.708
  102    QB   CYS  59           QB   CYS  60  12.322  13.935   4.678
  103    H    CYS  60           HN   CYS  61  12.101  12.040   8.419
  104    HA   CYS  60           HA   CYS  61   9.495  13.205   8.960
  105    QB   CYS  60           QB   CYS  61   9.053  10.690   8.616
  106    H    ALA  61           HN   ALA  62  12.309  12.917  10.182
  107    HA   ALA  61           HA   ALA  62  11.878  11.096  12.378
  108    QB   ALA  61           QB   ALA  62  14.116  12.087  12.044