*HEADER   R1MHUMR   14-MAY-90 
*COMPND   CD-7 METALLOTHIONEIN-2 (/NMR$)
*SOURCE   HUMAN (HOMO $SAPIENS) LIVER                                    
*EXPDTA   NMR
*AUTHOR   W.BRAUN,B.A.MESSERLE,A.SCHAEFFER,M.VASAK,J.H.R.KAEGI,         
*AUTHOR  2 K.WUTHRICH                                                   
*COORDS   1MHU,2MHU
*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).  

HEADER    NMR DATA FOR 1MHU                        3-MAY-90   1MHU      1MHU   3
COMPND    CD-7 METALLOTHIONEIN-2                                        1MHU   4
AUTHOR    W.BRAUN,B.A.MESSERLE,A.SCHAEFFER,M.VASAK,                     1MHU   5
AUTHOR    J.H.R.KAGI,K.WUTHRICH                                         1MHU   6
COORDS    1MHU                                                          1MHU   7
REMARK   1                                                              1MHU   8
REMARK   1 REFERENCE 1                                                  1MHU   9
REMARK   1  AUTH   B.A.MESSERLE,A.SCHAEFFER,                            1MHU  10
REMARK   1  AUTH 2 M.VASAK,J.H.R.KAGI,K.WUTHRICH                        1MHU  11
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF HUMAN 113CD_7     1MHU  12
REMARK   1  TITL 2 METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY          1MHU  13
REMARK   1  TITL 3 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY              1MHU  14
REMARK   1  REF    J.MOL.BIOL.                   V. ???   ??? 1990      1MHU  15
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2863                  070  1MHU  16
REMARK   2                                                              1MHU  17
REMARK   2 THIS FILE CONTAINS DATA THAT WAS USED IN THE DETERMINATION   1MHU  18
REMARK   2 OF THE THREE-DIMENSIONAL STRUCTURE OF 1MHU BY NUCLEAR        1MHU  19
REMARK   2 MAGNETIC RESONANCE IN SOLUTION.                              1MHU  20
REMARK   3                                                              1MHU  21
REMARK   3 INPUT DATA. 116 UPPER LIMIT DISTANCE CONSTRAINTS FOR THE     1MHU  22
REMARK   3 BETA DOMAIN AND 143 UPPER LIMIT DISTANCE CONSTRAINTS FOR     1MHU  23
REMARK   3 THE ALPHA DOMAIN. IN ADDITION UPPER AND LOWER DISTANCE       1MHU  24
REMARK   3 CONSTRAINTS WERE USED TO ENSURE THE CD-CYS CO-ORDINATIVE     1MHU  25
REMARK   3 BONDS WITH TETRAHEDRAL CO-ORDINATION GEOMETRY AT EACH METAL  1MHU  26
REMARK   3 ION AS DESCRIBED IN TABLE 1 ARSENIEV ET AL., J.MOL.BIOL.     1MHU  27
REMARK   3 (1988), VOL. 201, p.637. A LIST OF THE CHEMICAL SHIFTS       1MHU  28
REMARK   3 FOR THIS PROTEIN CAN BE FOUND IN REFERENCE 1.                1MHU  29
REMARK   4                                                              1MHU  30
REMARK   4 THE DIFFERENT KINDS OF DATA TOGETHER WITH THE CORRESPONDING  1MHU  31
REMARK   4 RECORD IDENTIFIERS ARE GIVEN IN THE FOLLOWING TABLE.         1MHU  32
REMARK   4                                                              1MHU  33
REMARK   4 RECORD CONTENT                                     UNIT      1MHU  34
REMARK   4 ------ ------------------------------------------- --------- 1MHU  35
REMARK   4 NOEUPP UPPER LIMITS FOR INTERATOMIC DISTANCES      ANGSTROMS 1MHU  36
REMARK   4        DETERMINED FROM NUCLEAR OVERHAUSER EFFECTS            1MHU  37
REMARK   4 ANGLE  TORSION ANGLE CONSTRAINTS IN THE FORM OF    DEGREES   1MHU  38
REMARK   4        AN ALLOWED INTERVAL                                   1MHU  39
REMARK   4                                                              1MHU  40
REMARK   4 THE NEXT TABLE CONTAINS A DETAILED DESCRIPTION OF THE        1MHU  41
REMARK   4 CONTENTS AND FORMATS OF THE VARIOUS DATA RECORDS AND THE     1MHU  42
REMARK   4 MASTER RECORD.                                               1MHU  43
REMARK   4                                                              1MHU  44
REMARK   4 RECORD CONTENTS (FORTRAN FORMAT)                             1MHU  45
REMARK   4 ------ ----------------------------------------------------- 1MHU  46
REMARK   4 NOEUPP FIRST RESIDUE NAME, FIRST RESIDUE NUMBER, FIRST ATOM  1MHU  47
REMARK   4        NAME, SECOND RESIDUE NAME, SECOND RESIDUE NUMBER,     1MHU  48
REMARK   4        SECOND ATOM NAME, UPPER DISTANCE LIMIT, FIRST ATOM    1MHU  49
REMARK   4        NAME, SECOND RESIDUE NAME, SECOND RESIDUE NUMBER,     1MHU  50
REMARK   4        SECOND ATOM NAME, UPPER DISTANCE LIMIT                1MHU  51
REMARK   4        ('NOEUPP',2X,A4,I4,1X,2(A4,1X,A4,I4,1X,A4,F6.2,5X))   1MHU  52
REMARK   4 ANGLE  RESIDUE NAME, RESIDUE NUMBER, ANGLE NAME, LOWER AND   1MHU  53
REMARK   4        UPPER BOUND, ANGLE NAME, LOWER AND UPPER BOUND        1MHU  54
REMARK   4        ('ANGLE',3X,A4,I4,1X,2(A5,2F8.2,8X))                  1MHU  55
REMARK   4 MASTER NUMBER OF REMARK RECORDS, NUMBER OF FTNOTE RECORDS,   1MHU  56
REMARK   4        NUMBER OF SHIFTS RECORDS, NUMBER OF JCOUPL RECORDS,   1MHU  57
REMARK   4        NUMBER OF NOEUPP, HBUPP AND SSUPP RECORDS, NUMBER OF  1MHU  58
REMARK   4        NOELOW, HBLOW AND SSLOW RECORDS, NUMBER OF ANGLE      1MHU  59
REMARK   4        RECORDS                                               1MHU  60
REMARK   4        ('MASTER',4X,7I5)                                     1MHU  61
REMARK   5                                                              1MHU  62
REMARK   5 ATOM NAMES HAVE BEEN ASSIGNED FOLLOWING THE RECOMMENDATIONS  1MHU  63
REMARK   5 OF THE IUPAC-IUB COMMISSION AS PUBLISHED IN BIOCHEMISTRY     1MHU  64
REMARK   5 (1970) VOL. 9, 3471-3479, EXCEPT THAT BACKBONE AMIDE         1MHU  65
REMARK   5 HYDROGENS ARE DENOTED BY HN INSTEAD OF H. THE HYDROGEN ATOM  1MHU  66
REMARK   5 NUMBERS OF THOSE HYDROGEN ATOMS WHICH ARE CONNECTED TO THE   1MHU  67
REMARK   5 SAME NON-HYDROGEN ATOM ARE WRITTEN AS THE FIRST CHARACTER    1MHU  68
REMARK   5 RATHER THAN THE LAST CHARACTER OF THE ATOM NAMES.            1MHU  69
REMARK   5 THEY ARE IDENTICAL WITH THE ATOM NAMES USED IN THE CO-       1MHU  70
REMARK   5 ORDINATE FILE 1MHU.                                          1MHU  71
REMARK   6                                                              1MHU  72
REMARK   6 PSEUDO-ATOMS DESIGNATED AS Q ARE DIMENSIONLESS REFERENCE     1MHU  73
REMARK   6 POINTS REPRESENTING A GROUP OF HYDROGEN ATOMS                1MHU  74
REMARK   6 (K.WUTHRICH, M.BILLETER AND W.BRAUN, J. MOL. BIOL. (1983)    1MHU  75
REMARK   6 VOL. 169, 949-961). THEY ARE USED TO DESCRIBE ALL METHYL     1MHU  76
REMARK   6 GROUPS, AND THOSE GROUPS OF PROCHIRAL HYDROGEN ATOMS FOR     1MHU  77
REMARK   6 WHICH NO STEREOSPECIFIC ASSIGNMENTS HAD BEEN OBTAINED.       1MHU  78
REMARK   7                                                              1MHU  79
REMARK   7 DETAILS OF THE NOMENCLATURE FOR THE PSEUDO-ATOMS ARE         1MHU  80
REMARK   7 AS FOLLOWS: QA REPRESENTS THE TWO METHYLENE HYDROGEN         1MHU  81
REMARK   7 ATOMS OF GLY. QB, QG, ... REPRESENT BETA, GAMMA, ...         1MHU  82
REMARK   7 METHYLENE OR METHYL GROUPS IN THE SIDE CHAINS. IN CASE OF    1MHU  83
REMARK   7 BRANCHES IN THE SIDE CHAINS THE NUMBERS OF THE PSEUDO-ATOMS  1MHU  84
REMARK   7 ARE THE SAME AS THE NUMBERS OF THE CARBONS TO WHICH THE      1MHU  85
REMARK   7 HYDROGEN  ATOMS ARE ATTACHED.                                1MHU  86
REMARK   7 QQG DENOTES THE PSEUDO-ATOM FOR THE 6 HYDROGEN               1MHU  87
REMARK   7 ATOMS OF THE ISOPROPYL METHYL GROUPS OF VAL.                 1MHU  88
REMARK   7                                                              1MHU  89
NOEUPP  ASP    2  HN  ASP    2  QB   3.70      HA  ASP    2  QB   3.70  1MHU  90
NOEUPP  ASP    2  HA  PRO    3  QG   6.00      HA  PRO    3  QD   6.00  1MHU  91
NOEUPP  ASP    2  QB  PRO    3  QD   7.00      QB  CYS    5  HN   6.00  1MHU  92
NOEUPP  PRO    3  QB  CYS    5  HN   6.00      QG  ASN    4  HN   6.00  1MHU  93
NOEUPP  PRO    3  QG  ASN    4  QD   7.00      QD  ASN    4  HN   5.00  1MHU  94
NOEUPP  ASN    4  HN  ASN    4  QB   4.10      HN  CYS    5  HN   3.10  1MHU  95
NOEUPP  ASN    4  HA  ASN    4  QB   3.70      HA  LYS   22  QB   6.00  1MHU  96
NOEUPP  ASN    4  HA  GLU   23  HN   5.00      QB  CYS    5  HN   5.00  1MHU  97
NOEUPP  ASN    4  QB  LYS   22  HA   6.00      QB  GLU   23  HN   6.00  1MHU  98
NOEUPP  ASN    4  QB  GLU   23  QB   7.00      QD  LYS   22  QD   7.00  1MHU  99
NOEUPP  ASN    4  QD  GLU   23  QG   7.00                               1MHU 100
NOEUPP  CYS    5  HN  CYS    5  QB   4.10      HN  LYS   22  QB   6.00  1MHU 101
NOEUPP  CYS    5  HA  CYS    5  QB   4.10      HA  SER    6  HN   2.40  1MHU 102
NOEUPP  CYS    5  HA  CYS    7  HN   4.00      HA  CYS   21  HA   5.00  1MHU 103
NOEUPP  CYS    5  HA  CYS   21 1HB   5.00      HA  CYS   21 2HB   5.00  1MHU 104
NOEUPP  CYS    5  HA  CYS   24  HA   5.00      HA  LYS   25  HN   5.00  1MHU 105
NOEUPP  CYS    5  QB  SER    6  HN   5.00      QB  CYS   24  HN   6.00  1MHU 106
NOEUPP  CYS    5  QB  CYS   24  HA   6.00      QB  LYS   25  HN   6.00  1MHU 107
NOEUPP  CYS    5 1HB  LYS   25  QD   6.00     2HB  LYS   25  QG   6.00  1MHU 108
NOEUPP  SER    6  HN  SER    6  QB   4.00      HN  CYS    7  HN   3.10  1MHU 109
NOEUPP  SER    6  HA  SER    6  QB   3.70                               1MHU 110
NOEUPP  CYS    7  HA  ALA    8  HN   3.10                               1MHU 111
NOEUPP  ALA    8  HN  ALA    8  QB   3.70      HN  ALA    9  HN   4.00  1MHU 112
NOEUPP  ALA    9  HN  ALA    9  QB   3.30                               1MHU 113
NOEUPP  ASP   11  HA  SER   12  HN   3.50                               1MHU 114
NOEUPP  SER   12  HN  SER   12  QB   3.70      HA  CYS   13  HN   3.10  1MHU 115
NOEUPP  SER   12  QB  CYS   13  HN   5.00                               1MHU 116
NOEUPP  CYS   13  HN  CYS   13  QB   3.30      HA  CYS   15  HN   4.00  1MHU 117
NOEUPP  THR   14  HA  ALA   16  HN   4.00      QG  CYS   15  HN   5.00  1MHU 118
NOEUPP  THR   14  QG  ALA   16  HN   6.00                               1MHU 119
NOEUPP  CYS   15  HN  CYS   15  QB   4.10      HN  ALA   16  HN   3.50  1MHU 120
NOEUPP  CYS   15  HN  ALA   16  QB   6.00      HA  CYS   15  QB   4.50  1MHU 121
NOEUPP  CYS   15  QB  ALA   16  HA   5.00                               1MHU 122
NOEUPP  ALA   16  HN  ALA   16  QB   4.10      HN  GLY   17  HN   4.00  1MHU 123
NOEUPP  ALA   16  HA  SER   18  HN   4.00      QB  GLY   17  HN   5.00  1MHU 124
NOEUPP  ALA   16  QB  SER   18  HN   5.00                               1MHU 125
NOEUPP  SER   18  HN  SER   18  QB   3.70      HN  CYS   19  HN   4.00  1MHU 126
NOEUPP  SER   18  HN  CYS   19 2HB   5.00      HA  CYS   19  HN   3.10  1MHU 127
NOEUPP  SER   18  QB  CYS   19  HN   5.00                               1MHU 128
NOEUPP  CYS   19  HN  CYS   19 1HB   3.10      HN  CYS   19 2HB   3.10  1MHU 129
NOEUPP  LYS   20  HN  LYS   20  QB   3.70      HN  LYS   20  QG   5.00  1MHU 130
NOEUPP  LYS   20  HN  CYS   21  HN   3.10      HA  LYS   20  QB   3.70  1MHU 131
NOEUPP  LYS   20  QG  CYS   21  HN   6.00                               1MHU 132
NOEUPP  CYS   21  HN  CYS   21 1HB   3.10      HN  CYS   24 1HB   5.00  1MHU 133
NOEUPP  CYS   21  HA  CYS   21 2HB   3.50     1HB  CYS   24 1HB   5.00  1MHU 134
NOEUPP  CYS   21 1HB  CYS   24 2HB   5.00     2HB  CYS   24  HN   5.00  1MHU 135
NOEUPP  CYS   21 2HB  CYS   24 2HB   5.00                               1MHU 136
NOEUPP  LYS   22  HN  LYS   22  QB   3.30      HN  LYS   22  QG   5.00  1MHU 137
NOEUPP  LYS   22  HN  LYS   22  QD   5.00                               1MHU 138
NOEUPP  GLU   23  HN  GLU   23  QB   4.50                               1MHU 139
NOEUPP  CYS   24  HN  CYS   24 1HB   2.70      HA  CYS   24 1HB   3.50  1MHU 140
NOEUPP  CYS   24  HA  CYS   24 2HB   3.50      HA  LYS   25  HN   2.40  1MHU 141
NOEUPP  CYS   24  HA  CYS   26  QB   6.00     2HB  LYS   25  HN   4.00  1MHU 142
NOEUPP  CYS   24 2HB  CYS   26  HN   5.00                               1MHU 143
NOEUPP  LYS   25  HN  LYS   25  QB   4.10      HN  LYS   25  QD   5.00  1MHU 144
NOEUPP  LYS   25  HN  CYS   26  HN   3.10      QG  CYS   26  HN   6.00  1MHU 145
NOEUPP  CYS   26  HN  CYS   26  QB   3.70      HN  CYS   29  HN   5.00  1MHU 146
NOEUPP  CYS   26  HA  THR   27  HN   2.70      QB  SER   28  HN   6.00  1MHU 147
NOEUPP  CYS   26  QB  CYS   29  HN   6.00                               1MHU 148
NOEUPP  THR   27  HN  THR   27  HB   3.50      HN  SER   28  HN   4.00  1MHU 149
NOEUPP  THR   27  HA  LYS   30  QB   6.00      HA  LYS   30  QG   6.00  1MHU 150
NOEUPP  THR   27  QG  SER   28  HN   6.00      QG  LYS   30  HN   6.00  1MHU 151
NOEUPP  SER   28  HN  CYS   29  HN   3.50      QB  LYS   30  HN   6.00  1MHU 152
NOEUPP  CYS   29  HN  CYS   29  QB   3.70      HN  LYS   30  QB   6.00  1MHU 153
NOEUPP  CYS   29  HA  LYS   30  HN   3.10                               1MHU 154
NOEUPP  LYS   30  HN  LYS   30  QB   4.10      HN  LYS   30  QG   5.00  1MHU 155
NOEUPP  LYS   30  HN  LYS   30  QD   5.00                               1MHU 156
NOEUPP  LYS   31  HA  LYS   31  QB   3.70      HA  VAL   39  QG2  6.00  1MHU 157
NOEUPP  SER   32  HN  LYS   31  HA   2.40      HN  SER   32 1HB   3.10  1MHU 158
NOEUPP  SER   32  HN  SER   32 2HB   2.70      HN  LYS   31  QB   4.10  1MHU 159
NOEUPP  SER   32  HN  LYS   31  QG   6.00      HN  VAL   39  QG2  6.00  1MHU 160
NOEUPP  SER   32 1HB  LYS   31  HA   5.00     1HB  VAL   39  QG2  6.00  1MHU 161
NOEUPP  SER   32 2HB  VAL   39  QG2  6.00      HA  VAL   39  QG2  6.00  1MHU 162
NOEUPP  CYS   33  HN  CYS   33  QB   3.70      HA  CYS   33  QB   3.70  1MHU 163
NOEUPP  CYS   33  HN  VAL   39  HA   5.00      HN  VAL   39  QG2  6.00  1MHU 164
NOEUPP  CYS   34  HA  CYS   34  QB   3.70      HN  SER   32 1HB   5.00  1MHU 165
NOEUPP  CYS   34  HN  SER   32 2HB   5.00      HN  SER   32  HA   4.00  1MHU 166
NOEUPP  SER   35  HN  CYS   34  QB   4.50      HN  CYS   36  HN   3.10  1MHU 167
NOEUPP  CYS   36  HN  CYS   37  HN   3.10      HN  CYS   34  HA   4.00  1MHU 168
NOEUPP  CYS   36  HN  CYS   34  QB   6.00      HA  CYS   36  QB   4.10  1MHU 169
NOEUPP  CYS   37  HN  CYS   37  QB   3.30      HN  SER   35  HA   4.00  1MHU 170
NOEUPP  CYS   37  HA  PRO   38  QD   6.00      QB  PRO   38  QD   7.00  1MHU 171
NOEUPP  CYS   37  HA  PRO   38  QG   6.00      HA  CYS   41  QB   6.00  1MHU 172
NOEUPP  PRO   38  HA  PRO   38  QB   3.70      QD  CYD   41  QB   7.00  1MHU 173
NOEUPP  VAL   39  HA  VAL   39  QG1  4.00      HA  VAL   39  QG2  3.70  1MHU 174
NOEUPP  GLY   40  HN  VAL   39  HB   4.00      HN  VAL   39  QG1  4.10  1MHU 175
NOEUPP  GLY   40  CA  VAL   39  QG1  7.00      HN  CYS   41  HN   2.70  1MHU 176
NOEUPP  CYS   41  HA  CYS   41  QB   3.30      HN  CYS   37  QB   6.00  1MHU 177
NOEUPP  CYS   41  HN  PRO   38  QG   6.00      HN  CYS   44  QB   6.00  1MHU 178
NOEUPP  CYS   41  HN  VAL   39  HA   4.00      HN  VAL   39  QG1  6.00  1MHU 179
NOEUPP  CYS   41  HN  PRO   38  QB   6.00                               1MHU 180
NOEUPP  ALA   42  HN  CYS   41  HA   2.40      HN  LYS   43  HN   3.10  1MHU 181
NOEUPP  ALA   42  HN  CYS   44  HN   4.00      QB  LYS   43  HA   5.00  1MHU 182
NOEUPP  LYS   43  HN  ALA   42  HA   3.50      HN  LYS   43  QD   4.10  1MHU 183
NOEUPP  LYS   43  HN  CYS   44  QB   6.00      HN  CYS   44  HN   2.40  1MHU 184
NOEUPP  LYS   43  HN  ALA   45  HN   4.00      QB  ILE   49  QD   7.00  1MHU 185
NOEUPP  CYS   44  HN  ALA   42  QB   6.00      HN  ALA   45  QB   6.00  1MHU 186
NOEUPP  CYS   44  HN  ALA   45  HN   2.70      HN  CYS   44  QB   3.30  1MHU 187
NOEUPP  CYS   44  HN  LYS   43  QB   3.70      HN  LYS   43  HA   3.50  1MHU 188
NOEUPP  CYS   44  HN  CYS   41  QB   6.00      HN  ILE   49  QG2  6.00  1MHU 189
NOEUPP  CYS   44  HN  ILE   49  QD   6.00     1HB  CYS   48  HA   5.00  1MHU 190
NOEUPP  CYS   44 1HB  CYS   41  QB   6.00                               1MHU 191
NOEUPP  ALA   45  HN  ALA   45  QB   3.30      HN  CYS   44  HA   3.50  1MHU 192
NOEUPP  ALA   45  HN  LYS   43  HA   4.00      QB  GLN   46  QG   7.00  1MHU 193
NOEUPP  ALA   45  HN  CYS   41  QB   6.00      HN  LYS   43  QB   6.00  1MHU 194
NOEUPP  ALA   45  QB  CYS   44  QB   7.00                               1MHU 195
NOEUPP  GLN   46  HN  ALA   45  HA   3.50      HN  CYS   44  HA   4.00  1MHU 196
NOEUPP  GLN   46  HN  GLN   46  QB   3.70      HN  ILE   49  QG2  6.00  1MHU 197
NOEUPP  GLN   46  HN  ALA   45  QB   4.10      HN  ALA   45  HN   3.10  1MHU 198
NOEUPP  GLN   46  HN  GLY   47  HN   2.70      HA  GLN   46  QB   4.10  1MHU 199
NOEUPP  GLY   47  HN  GLN   46  HA   3.10      HN  ALA   45  HA   4.00  1MHU 200
NOEUPP  GLY   47  HN  ALA   45  QB   6.00      HN  ILE   49  QG2  6.00  1MHU 201
NOEUPP  GLY   47  HN  CYS   44  HA   4.00      HN  ALA   45  HN   4.00  1MHU 202
NOEUPP  CYS   48  HN  GLY   47  HN   4.00                               1MHU 203
NOEUPP  ILE   49  HA  ILE   49  HB   2.70      HN  CYS   44  HA   5.00  1MHU 204
NOEUPP  ILE   49  HN  CYS   44  QB   6.00      HN  CYS   48  HA   2.40  1MHU 205
NOEUPP  ILE   49  QD  LYS   43  QB   7.00      QD  CYS   44  HA   6.00  1MHU 206
NOEUPP  ILE   49  QG2 CYS   44  HA   6.00                               1MHU 207
NOEUPP  CYS   50  HN  ILE   49  HA   3.50      HN  CYS   48  HA   4.00  1MHU 208
NOEUPP  CYS   50  HN  CYS   50 2HB   2.70      HN  CYS   50 1HB   3.50  1MHU 209
NOEUPP  CYS   50  HA  CYS   50 2HB   3.50      HN  ILE   49  QG1  6.00  1MHU 210
NOEUPP  CYS   50  HN  ILE   49  HN   2.70                               1MHU 211
NOEUPP  LYS   51  HN  CYS   50 1HB   4.00                               1MHU 212
NOEUPP  GLY   52  HN  LYS   51  QB   4.10                               1MHU 213
NOEUPP  ALA   53  QB  CYS   57 2HB   6.00      QB  CYS   57 1HB   6.00  1MHU 214
NOEUPP  ASP   55  HN  LYS   56  HN   3.10                               1MHU 215
NOEUPP  LYS   56  HN  ASP   55  HA   3.50      HN  LYS   56  QG   5.00  1MHU 216
NOEUPP  LYS   56  HN  CYS   36  HA   5.00      HN  SER   54  HA   4.00  1MHU 217
NOEUPP  LYS   56  HN  SER   54  QB   6.00      HA  CYS   36  HA   5.00  1MHU 218
NOEUPP  LYS   56  HA  CYS   36  QB   6.00      HN  CYS   36  QB   6.00  1MHU 219
NOEUPP  CYS   57  HN  CYS   36  QB   5.00      HA  ALA   53  QB   6.00  1MHU 220
NOEUPP  CYS   57  HA  CYS   36  QB   6.00      QB  CYS   36  QB   7.00  1MHU 221
NOEUPP  SER   58  HN  CYS   57  HA   3.50      HA  SER   58  QB   4.10  1MHU 222
NOEUPP  CYS   59  HN  CYS   60  HN   2.70      HN  ALA   61  HN   4.00  1MHU 223
NOEUPP  CYS   59  HN  CYS   57 1HB   5.00      HN  CYS   57 2HB   5.00  1MHU 224
NOEUPP  CYS   59  HN  CYS   60 1HB   5.00      QB  ILE   49  QD   7.00  1MHU 225
NOEUPP  CYS   59  HA  ILE   49  QD   6.00                               1MHU 226
NOEUPP  CYS   60  HN  CYS   59  HA   3.50      HN  CYS   60 1HB   3.10  1MHU 227
NOEUPP  CYS   60  HN  ALA   61  HA   4.00      HN  ALA   61  QB   6.00  1MHU 228
NOEUPP  CYS   60  HN  ALA   61  HN   2.70      HN  SER   58  HA   4.00  1MHU 229
NOEUPP  CYS   60  HN  CYS   57 2HB   5.00      HA  CYS   60 2HB   2.70  1MHU 230
NOEUPP  CYS   60  HA  CYS   60 1HB   3.10                               1MHU 231
NOEUPP  ALA   61  HN  CYS   60  HA   3.10      HN  ALA   61  QB   3.30  1MHU 232
NOEUPP  ALA   61  HN  CYS   59  HA   4.00      HN  SER   58  HA   4.00  1MHU 233
ANGLE   ASP    2 PHI     35.00  295.00        CHI1   -15.00  175.00     1MHU 234
ANGLE   ASN    4 CHI1  -255.00   15.00                                  1MHU 235
ANGLE   CYS    5 PHI   -155.00  -85.00        CHI1   145.00  335.00     1MHU 236
ANGLE   SER    6 PHI   -145.00  -95.00        CHI1    35.00  245.00     1MHU 237
ANGLE   CYS    7 PHI     35.00  285.00                                  1MHU 238
ANGLE   ASP   11 CHI1  -255.00   15.00                                  1MHU 239
ANGLE   SER   12 PHI   -145.00  -95.00                                  1MHU 240
ANGLE   CYS   13 PHI   -145.00  -95.00                                  1MHU 241
ANGLE   CYS   15 PHI   -165.00  -75.00        CHI1  -125.00   55.00     1MHU 242
ANGLE   SER   18 PHI     55.00  275.00                                  1MHU 243
ANGLE   CYS   19 CHI1   155.00  205.00                                  1MHU 244
ANGLE   LYS   20 CHI1  -105.00  125.00                                  1MHU 245
ANGLE   CYS   21 PHI   -165.00   75.00        CHI1   175.00  215.00     1MHU 246
ANGLE   LYS   22 PHI   -135.00  -75.00                                  1MHU 247
ANGLE   GLU   23 PHI   -155.00  -85.00                                  1MHU 248
ANGLE   CYS   24 CHI1   165.00  215.00                                  1MHU 249
ANGLE   CYS   26 PHI   -175.00   55.00        CHI1  -235.00   25.00     1MHU 250
ANGLE   LYS   31 PHI   -155.00  -85.00        CHI1   -55.00   35.00     1MHU 251
ANGLE   SER   32 PHI   -135.00  -75.00        CHI1   145.00  185.00     1MHU 252
ANGLE   CYS   33 PHI   -165.00  -75.00        CHI1    65.00  235.00     1MHU 253
ANGLE   CYS   34 PHI     55.00  275.00        CHI1    35.00   85.00     1MHU 254
ANGLE   SER   35 PHI     45.00  285.00                                  1MHU 255
ANGLE   CYS   36 PHI     45.00  285.00        CHI1     5.00  115.00     1MHU 256
ANGLE   CYS   37 PHI   -155.00  -85.00                                  1MHU 257
ANGLE   VAL   39 PHI     35.00  295.00        CHI1  -235.00   45.00     1MHU 258
ANGLE   CYS   41 PHI     45.00  285.00        CHI1   -55.00  175.00     1MHU 259
ANGLE   LYS   43 PHI     75.00  285.00                                  1MHU 260
ANGLE   CYS   44 PHI   -145.00  -85.00        CHI1   165.00  305.00     1MHU 261
ANGLE   GLN   46 PHI   -155.00  -85.00        CHI1    -5.00  215.00     1MHU 262
ANGLE   CYS   48 PHI   -155.00  -85.00                                  1MHU 263
ANGLE   ILE   49 PHI   -145.00  -95.00                                  1MHU 264
ANGLE   CYS   50 PHI   -155.00  -75.00        CHI1   145.00  325.00     1MHU 265
ANGLE   LYS   51 PHI   -155.00  -85.00                                  1MHU 266
ANGLE   SER   54 PHI     55.00  275.00                                  1MHU 267
ANGLE   ASP   55 PHI   -155.00  -85.00        CHI1  -135.00 -105.00     1MHU 268
ANGLE   LYS   56 PHI   -155.00  -85.00                                  1MHU 269
ANGLE   CYS   57 PHI   -155.00  -85.00        CHI1    35.00  245.00     1MHU 270
ANGLE   CYS   59 PHI     45.00  285.00                                  1MHU 271
ANGLE   CYS   60 PHI   -155.00  -85.00        CHI1   290.00  330.00     1MHU 272



*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 235 H/Q atoms
    1    H    LYS  31           HN   LYS  31  -0.338   0.478   0.828
    2    HA   LYS  31           HA   LYS  31   1.780  -1.018  -0.214
    3   1HB   LYS  31          1HB   LYS  31   1.741   1.933  -0.913
    4   2HB   LYS  31          2HB   LYS  31   3.076   0.825  -1.156
    5   1HG   LYS  31          1HG   LYS  31   0.692  -0.330  -2.336
    6   2HG   LYS  31          2HG   LYS  31   0.851   1.320  -2.903
    7   1HD   LYS  31          1HD   LYS  31   2.221   0.296  -4.462
    8   2HD   LYS  31          2HD   LYS  31   3.423   0.594  -3.222
    9   1HE   LYS  31          1HE   LYS  31   2.599  -1.788  -2.305
   10   2HE   LYS  31          2HE   LYS  31   2.060  -2.001  -3.958
   11   1HZ   LYS  31          1HZ   LYS  31   4.682  -0.942  -3.966
   12   2HZ   LYS  31          2HZ   LYS  31   4.178  -2.371  -4.561
   13    QB   LYS  31           QB   LYS  31   2.409   1.379  -1.035
   14    QG   LYS  31           QG   LYS  31   0.771   0.495  -2.619
   15    QD   LYS  31           QD   LYS  31   2.822   0.445  -3.842
   16    QE   LYS  31           QE   LYS  31   2.330  -1.895  -3.131
   17    QZ   LYS  31           QZ   LYS  31   4.430  -1.656  -4.264
   18    H    SER  32           HN   SER  32   3.769  -0.524   1.037
   19    HA   SER  32           HA   SER  32   3.031   0.081   3.695
   20   1HB   SER  32          1HB   SER  32   4.674  -1.598   3.509
   21   2HB   SER  32          2HB   SER  32   5.578  -0.727   2.285
   22    HG   SER  32           HG   SER  32   5.769  -0.600   5.063
   23    QB   SER  32           QB   SER  32   5.126  -1.162   2.897
   24    H    CYS  33           HN   CYS  33   3.222   2.020   4.795
   25    HA   CYS  33           HA   CYS  33   3.922   4.320   3.291
   26   1HB   CYS  33          1HB   CYS  33   2.117   4.251   5.030
   27   2HB   CYS  33          2HB   CYS  33   3.352   4.107   6.265
   28    QB   CYS  33           QB   CYS  33   2.734   4.179   5.647
   29    H    CYS  34           HN   CYS  34   5.299   2.521   6.130
   30    HA   CYS  34           HA   CYS  34   7.919   3.467   5.344
   31   1HB   CYS  34          1HB   CYS  34   8.270   3.864   7.959
   32   2HB   CYS  34          2HB   CYS  34   7.764   5.145   6.875
   33    QB   CYS  34           QB   CYS  34   8.017   4.505   7.417
   34    H    SER  35           HN   SER  35   9.641   2.173   6.587
   35    HA   SER  35           HA   SER  35   8.654  -0.516   6.834
   36   1HB   SER  35          1HB   SER  35  11.162  -1.032   7.023
   37   2HB   SER  35          2HB   SER  35  10.622  -0.347   5.503
   38    HG   SER  35           HG   SER  35  11.420   1.515   7.489
   39    QB   SER  35           QB   SER  35  10.892  -0.689   6.263
   40    H    CYS  36           HN   CYS  36   8.021   1.570   8.901
   41    HA   CYS  36           HA   CYS  36   9.296   0.217  11.163
   42   1HB   CYS  36          1HB   CYS  36  10.141   2.139  11.905
   43   2HB   CYS  36          2HB   CYS  36   9.530   2.970  10.489
   44    QB   CYS  36           QB   CYS  36   9.836   2.554  11.197
   45    H    CYS  37           HN   CYS  37   6.484   1.876   9.675
   46    HA   CYS  37           HA   CYS  37   4.817   1.023  11.902
   47   1HB   CYS  37          1HB   CYS  37   4.321   2.921   9.592
   48   2HB   CYS  37          2HB   CYS  37   3.053   2.395  10.681
   49    QB   CYS  37           QB   CYS  37   3.687   2.658  10.137
   50    HA   PRO  38           HA   PRO  38   3.231  -2.279   9.480
   51   1HB   PRO  38          1HB   PRO  38   0.636  -2.471  10.501
   52   2HB   PRO  38          2HB   PRO  38   2.052  -3.112  11.310
   53   1HG   PRO  38          1HG   PRO  38   0.455  -0.719  11.988
   54   2HG   PRO  38          2HG   PRO  38   1.582  -1.607  12.994
   55   1HD   PRO  38          1HD   PRO  38   2.054   0.907  11.696
   56   2HD   PRO  38          2HD   PRO  38   3.217  -0.038  12.606
   57    QB   PRO  38           QB   PRO  38   1.344  -2.792  10.906
   58    QG   PRO  38           QG   PRO  38   1.019  -1.163  12.491
   59    QD   PRO  38           QD   PRO  38   2.635   0.434  12.151
   60    H    VAL  39           HN   VAL  39   0.012  -0.834   9.772
   61    HA   VAL  39           HA   VAL  39   0.151   0.475   7.250
   62    HB   VAL  39           HB   VAL  39  -0.893  -2.319   7.455
   63   1HG1  VAL  39          2HG1  VAL  39  -2.873  -0.976   6.867
   64   2HG1  VAL  39          3HG1  VAL  39  -1.975  -0.249   5.513
   65   3HG1  VAL  39          1HG1  VAL  39  -2.339  -1.992   5.507
   66   1HG2  VAL  39          1HG2  VAL  39   0.978  -0.769   5.770
   67   2HG2  VAL  39          2HG2  VAL  39   0.986  -2.493   6.215
   68   3HG2  VAL  39          3HG2  VAL  39  -0.055  -1.920   4.889
   69    QG1  VAL  39           QG1  VAL  39  -2.396  -1.072   5.962
   70    QG2  VAL  39           QG2  VAL  39   0.637  -1.727   5.625
   71    QQG  VAL  39           QQG  VAL  39  -0.880  -1.400   5.793
   72    H    GLY  40           HN   GLY  40  -1.993   1.446   6.687
   73   1HA   GLY  40          1HA   GLY  40  -3.810   2.622   7.287
   74   2HA   GLY  40          2HA   GLY  40  -4.266   1.240   8.263
   75    QA   GLY  40           QA   GLY  40  -4.038   1.931   7.775
   76    H    CYS  41           HN   CYS  41  -1.186   2.921   8.841
   77    HA   CYS  41           HA   CYS  41  -1.938   3.417  11.526
   78   1HB   CYS  41          1HB   CYS  41   0.353   2.845  11.031
   79   2HB   CYS  41          2HB   CYS  41   0.516   4.191   9.920
   80    QB   CYS  41           QB   CYS  41   0.434   3.518  10.475
   81    H    ALA  42           HN   ALA  42  -3.209   5.120  12.167
   82    HA   ALA  42           HA   ALA  42  -4.063   7.127  10.479
   83   1HB   ALA  42          2HB   ALA  42  -3.925   6.829  13.493
   84   2HB   ALA  42          3HB   ALA  42  -4.650   8.261  12.725
   85   3HB   ALA  42          1HB   ALA  42  -5.334   6.646  12.420
   86    QB   ALA  42           QB   ALA  42  -4.636   7.245  12.879
   87    H    LYS  43           HN   LYS  43  -1.113   6.821  12.428
   88    HA   LYS  43           HA   LYS  43  -0.472   9.611  12.178
   89   1HB   LYS  43          1HB   LYS  43   1.107   7.239  13.215
   90   2HB   LYS  43          2HB   LYS  43   1.663   8.900  13.261
   91   1HG   LYS  43          1HG   LYS  43  -0.764   7.722  14.678
   92   2HG   LYS  43          2HG   LYS  43   0.666   8.415  15.416
   93   1HD   LYS  43          1HD   LYS  43  -0.139  10.549  13.906
   94   2HD   LYS  43          2HD   LYS  43  -1.694   9.790  14.182
   95   1HE   LYS  43          1HE   LYS  43  -0.299   9.744  16.691
   96   2HE   LYS  43          2HE   LYS  43  -0.090  11.353  16.028
   97   1HZ   LYS  43          1HZ   LYS  43  -2.170  11.729  16.767
   98   2HZ   LYS  43          2HZ   LYS  43  -2.473  10.156  17.059
   99    QB   LYS  43           QB   LYS  43   1.385   8.069  13.238
  100    QG   LYS  43           QG   LYS  43  -0.049   8.068  15.047
  101    QD   LYS  43           QD   LYS  43  -0.916  10.169  14.044
  102    QE   LYS  43           QE   LYS  43  -0.194  10.549  16.360
  103    QZ   LYS  43           QZ   LYS  43  -2.321  10.943  16.913
  104    H    CYS  44           HN   CYS  44  -0.834   7.416   9.861
  105    HA   CYS  44           HA   CYS  44   1.212   8.637   8.250
  106   1HB   CYS  44          1HB   CYS  44   1.225   5.666   8.827
  107   2HB   CYS  44          2HB   CYS  44   1.942   6.340   7.377
  108    QB   CYS  44           QB   CYS  44   1.584   6.003   8.102
  109    H    ALA  45           HN   ALA  45  -1.813   8.453   8.654
  110    HA   ALA  45           HA   ALA  45  -2.659   6.993   6.295
  111   1HB   ALA  45          1HB   ALA  45  -3.934   8.257   8.692
  112   2HB   ALA  45          2HB   ALA  45  -4.908   8.146   7.206
  113   3HB   ALA  45          3HB   ALA  45  -4.235   6.671   7.941
  114    QB   ALA  45           QB   ALA  45  -4.359   7.691   7.946
  115    H    GLN  46           HN   GLN  46  -2.242  10.345   7.518
  116    HA   GLN  46           HA   GLN  46  -3.316  11.384   5.067
  117   1HB   GLN  46          1HB   GLN  46  -3.281  13.497   6.120
  118   2HB   GLN  46          2HB   GLN  46  -3.621  12.394   7.438
  119   1HG   GLN  46          1HG   GLN  46  -1.855  13.370   8.497
  120   2HG   GLN  46          2HG   GLN  46  -0.846  12.408   7.435
  121   1HE2  GLN  46          2HE   GLN  46   0.767  15.201   6.388
  122   2HE2  GLN  46          1HE   GLN  46   0.648  14.312   7.870
  123    QB   GLN  46           QB   GLN  46  -3.451  12.945   6.779
  124    QG   GLN  46           QG   GLN  46  -1.350  12.889   7.966
  125    QE2  GLN  46           QE   GLN  46   0.708  14.756   7.129
  126    H    GLY  47           HN   GLY  47  -0.712   9.715   5.320
  127   1HA   GLY  47          1HA   GLY  47   0.780  10.292   3.320
  128   2HA   GLY  47          2HA   GLY  47   1.201  11.700   4.275
  129    QA   GLY  47           QA   GLY  47   0.990  10.996   3.798
  130    H    CYS  48           HN   CYS  48   2.904  11.533   5.680
  131    HA   CYS  48           HA   CYS  48   3.411   9.035   6.990
  132   1HB   CYS  48          1HB   CYS  48   4.556   8.573   4.898
  133   2HB   CYS  48          2HB   CYS  48   5.403  10.106   4.966
  134    QB   CYS  48           QB   CYS  48   4.979   9.339   4.932
  135    H    ILE  49           HN   ILE  49   2.928  10.441   8.826
  136    HA   ILE  49           HA   ILE  49   4.692  12.714   9.204
  137    HB   ILE  49           HB   ILE  49   3.268  13.333  10.975
  138   1HG1  ILE  49          1HG1  ILE  49   1.380  11.102  10.954
  139   2HG1  ILE  49          2HG1  ILE  49   2.985  10.603  11.450
  140   1HG2  ILE  49          3HG2  ILE  49   1.709  12.215   8.636
  141   2HG2  ILE  49          1HG2  ILE  49   0.996  13.261   9.887
  142   3HG2  ILE  49          2HG2  ILE  49   2.318  13.872   8.864
  143   1HD1  ILE  49          1HD   ILE  49   1.477  12.986  12.623
  144   2HD1  ILE  49          2HD   ILE  49   1.594  11.378  13.378
  145   3HD1  ILE  49          3HD   ILE  49   3.056  12.371  13.167
  146    QG1  ILE  49           QG1  ILE  49   2.182  10.852  11.202
  147    QG2  ILE  49           QG2  ILE  49   1.674  13.116   9.129
  148    QD1  ILE  49           QD   ILE  49   2.043  12.245  13.056
  149    H    CYS  50           HN   CYS  50   5.482   9.705   9.216
  150    HA   CYS  50           HA   CYS  50   6.372   9.461  11.962
  151   1HB   CYS  50          1HB   CYS  50   5.415   7.480  10.874
  152   2HB   CYS  50          2HB   CYS  50   6.629   7.554   9.613
  153    QB   CYS  50           QB   CYS  50   6.022   7.517  10.244
  154    H    LYS  51           HN   LYS  51   8.307  10.393  12.526
  155    HA   LYS  51           HA   LYS  51  10.345  10.576  10.417
  156   1HB   LYS  51          1HB   LYS  51  11.042  12.694  11.279
  157   2HB   LYS  51          2HB   LYS  51   9.316  12.771  10.988
  158   1HG   LYS  51          1HG   LYS  51  10.411  12.031  13.728
  159   2HG   LYS  51          2HG   LYS  51  10.229  13.707  13.252
  160   1HD   LYS  51          1HD   LYS  51   7.773  12.511  12.527
  161   2HD   LYS  51          2HD   LYS  51   8.172  11.774  14.066
  162   1HE   LYS  51          1HE   LYS  51   8.076  14.779  13.512
  163   2HE   LYS  51          2HE   LYS  51   6.855  13.865  14.375
  164   1HZ   LYS  51          1HZ   LYS  51   9.385  14.812  15.339
  165   2HZ   LYS  51          2HZ   LYS  51   9.165  13.236  15.686
  166    QB   LYS  51           QB   LYS  51  10.179  12.733  11.134
  167    QG   LYS  51           QG   LYS  51  10.320  12.869  13.490
  168    QD   LYS  51           QD   LYS  51   7.972  12.142  13.297
  169    QE   LYS  51           QE   LYS  51   7.465  14.322  13.943
  170    QZ   LYS  51           QZ   LYS  51   9.275  14.024  15.513
  171    H    GLY  52           HN   GLY  52   9.374   9.372  13.505
  172   1HA   GLY  52          1HA   GLY  52  11.471   9.295  15.145
  173   2HA   GLY  52          2HA   GLY  52  10.483   7.884  14.821
  174    QA   GLY  52           QA   GLY  52  10.977   8.590  14.983
  175    H    ALA  53           HN   ALA  53  11.227   6.227  13.389
  176    HA   ALA  53           HA   ALA  53  13.828   6.620  12.159
  177   1HB   ALA  53          3HB   ALA  53  13.798   5.627  14.687
  178   2HB   ALA  53          1HB   ALA  53  13.567   4.123  13.763
  179   3HB   ALA  53          2HB   ALA  53  14.992   5.144  13.458
  180    QB   ALA  53           QB   ALA  53  14.119   4.965  13.969
  181    H    SER  54           HN   SER  54  13.965   3.566  11.944
  182    HA   SER  54           HA   SER  54  11.750   3.290  10.067
  183   1HB   SER  54          1HB   SER  54  13.407   1.795   8.753
  184   2HB   SER  54          2HB   SER  54  13.633   3.530   8.658
  185    HG   SER  54           HG   SER  54  15.637   3.088   9.278
  186    QB   SER  54           QB   SER  54  13.520   2.662   8.705
  187    H    ASP  55           HN   ASP  55  13.976   1.823  12.449
  188    HA   ASP  55           HA   ASP  55  12.547  -0.678  12.238
  189   1HB   ASP  55          1HB   ASP  55  15.216   0.016  12.803
  190   2HB   ASP  55          2HB   ASP  55  14.578  -0.446  14.368
  191    QB   ASP  55           QB   ASP  55  14.897  -0.215  13.585
  192    H    LYS  56           HN   LYS  56  12.827   2.269  14.138
  193    HA   LYS  56           HA   LYS  56  10.662   1.465  15.813
  194   1HB   LYS  56          1HB   LYS  56  12.589   0.380  16.959
  195   2HB   LYS  56          2HB   LYS  56  13.346   1.949  17.139
  196   1HG   LYS  56          1HG   LYS  56  10.673   2.273  18.081
  197   2HG   LYS  56          2HG   LYS  56  11.222   0.744  18.737
  198   1HD   LYS  56          1HD   LYS  56  13.226   2.946  18.893
  199   2HD   LYS  56          2HD   LYS  56  11.779   3.213  19.844
  200   1HE   LYS  56          1HE   LYS  56  13.649   1.990  21.070
  201   2HE   LYS  56          2HE   LYS  56  12.099   1.174  21.099
  202   1HZ   LYS  56          1HZ   LYS  56  14.143   0.541  19.049
  203   2HZ   LYS  56          2HZ   LYS  56  12.833  -0.343  19.441
  204    QB   LYS  56           QB   LYS  56  12.967   1.164  17.049
  205    QG   LYS  56           QG   LYS  56  10.948   1.508  18.409
  206    QD   LYS  56           QD   LYS  56  12.502   3.080  19.368
  207    QE   LYS  56           QE   LYS  56  12.874   1.582  21.085
  208    QZ   LYS  56           QZ   LYS  56  13.488   0.099  19.245
  209    H    CYS  57           HN   CYS  57   9.423   3.241  16.171
  210    HA   CYS  57           HA   CYS  57  10.773   5.821  15.833
  211   1HB   CYS  57          1HB   CYS  57   8.945   6.693  14.656
  212   2HB   CYS  57          2HB   CYS  57   9.162   5.094  13.973
  213    QB   CYS  57           QB   CYS  57   9.053   5.893  14.314
  214    H    SER  58           HN   SER  58   8.556   7.420  16.680
  215    HA   SER  58           HA   SER  58   7.672   6.357  19.181
  216   1HB   SER  58          1HB   SER  58   8.631   8.210  20.536
  217   2HB   SER  58          2HB   SER  58   9.879   7.197  19.837
  218    HG   SER  58           HG   SER  58  10.310   9.510  19.618
  219    QB   SER  58           QB   SER  58   9.255   7.703  20.187
  220    H    CYS  59           HN   CYS  59   6.673   7.442  16.510
  221    HA   CYS  59           HA   CYS  59   5.019   9.585  17.632
  222   1HB   CYS  59          1HB   CYS  59   4.899  10.037  14.931
  223   2HB   CYS  59          2HB   CYS  59   5.919  10.909  16.058
  224    QB   CYS  59           QB   CYS  59   5.409  10.473  15.494
  225    H    CYS  60           HN   CYS  60   5.159   6.384  16.834
  226    HA   CYS  60           HA   CYS  60   2.324   6.334  16.246
  227   1HB   CYS  60          1HB   CYS  60   4.223   4.701  14.542
  228   2HB   CYS  60          2HB   CYS  60   2.488   4.867  14.361
  229    QB   CYS  60           QB   CYS  60   3.356   4.784  14.452
  230    H    ALA  61           HN   ALA  61   4.387   5.771  18.471
  231    HA   ALA  61           HA   ALA  61   4.987   3.194  18.897
  232   1HB   ALA  61          3HB   ALA  61   3.909   5.329  20.760
  233   2HB   ALA  61          1HB   ALA  61   4.447   3.742  21.360
  234   3HB   ALA  61          2HB   ALA  61   5.595   4.811  20.520
  235    QB   ALA  61           QB   ALA  61   4.650   4.628  20.880