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Database: PDB
Entry: 2CRI
LinkDB: 2CRI
Original site: 2CRI 
HEADER    TRANSPORT PROTEIN                       20-MAY-05   2CRI              
TITLE     SOLUTION STRUCTURE OF THE MSP DOMAIN OF MOUSE VAMP-                   
TITLE    2 ASSOCIATED PROTEINA                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED             
COMPND   3 PROTEIN A;                                                           
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: MSP (RESIDUES 1-147);                                      
COMPND   6 SYNONYM: VAMP- ASSOCIATED PROTEIN A, VAMP-A, VAP-A, 33 KDA           
COMPND   7 VAMP-ASSOCIATED PROTEIN, VAP-33;                                     
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: VAPA, VAP33;                                                   
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: P040329-04;                               
SOURCE   8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS                           
KEYWDS    VAP-A, VAP-33, BETA SANDWITCH FOLD, STRUCTURAL GENOMICS,              
KEYWDS   2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND                   
KEYWDS   3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS            
KEYWDS   4 INITIATIVE, RSGI, TRANSPORT PROTEIN                                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL                
AUTHOR   2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)                                
REVDAT   2   24-FEB-09 2CRI    1       VERSN                                    
REVDAT   1   20-NOV-05 2CRI    0                                                
JRNL        AUTH   H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA                        
JRNL        TITL   SOLUTION STRUCTURE OF THE MSP DOMAIN OF MOUSE                
JRNL        TITL 2 VAMP-ASSOCIATED PROTEINA                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CYANA 2.0.17                                         
REMARK   3   AUTHORS     : GUNTERT,P.                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2CRI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024544.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 120 MM                             
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 0.52MM 13C,15N-LABELED             
REMARK 210                                   PROTEIN; 20MM D-TRIS-              
REMARK 210                                   HCL(PH7.0); 100MM NACL; 1MM D-     
REMARK 210                                   DTT; 0.02% NAN3                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_15N-SEPARATED_NOESY, 3D_        
REMARK 210                                   13C-SEPARATED_NOESY                
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ, 900 MHZ                   
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMR 6.1C, NMRPIPE 20031121,       
REMARK 210                                   NMRVIEW 5.0.4, KUJIRA 0.9296,      
REMARK 210                                   CYANA 2.0.17                       
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS             
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : TARGET FUNCTION, STRUCTURES        
REMARK 210                                   WITH THE LOWEST ENERGY,            
REMARK 210                                   STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 SER A  21      -75.29    -76.56                                   
REMARK 500  1 PRO A  28     -177.25    -69.77                                   
REMARK 500  1 ASP A  69      151.73    -41.71                                   
REMARK 500  1 ASP A  84       95.76    -68.92                                   
REMARK 500  1 LYS A  92      -64.47    -99.86                                   
REMARK 500  1 HIS A  93      148.31    -37.97                                   
REMARK 500  1 ILE A 106       97.20    -47.51                                   
REMARK 500  1 ASN A 134       87.35    -52.61                                   
REMARK 500  1 LYS A 138      141.49    -39.54                                   
REMARK 500  1 SER A 142       35.04    -94.23                                   
REMARK 500  1 SER A 146      157.68    -46.14                                   
REMARK 500  2 SER A  21      -75.62    -77.99                                   
REMARK 500  2 ALA A  55       67.15   -115.41                                   
REMARK 500  2 ASP A  69      149.86    -36.90                                   
REMARK 500  2 TYR A  85      101.31    -57.03                                   
REMARK 500  2 GLU A  89       57.43   -108.96                                   
REMARK 500  2 LYS A  90       42.53    -93.71                                   
REMARK 500  2 LYS A  92      117.14   -172.37                                   
REMARK 500  2 SER A 107      -61.26   -106.93                                   
REMARK 500  2 LYS A 138      109.17    -37.52                                   
REMARK 500  3 HIS A  11       54.48    -95.98                                   
REMARK 500  3 SER A  21      -76.47    -82.73                                   
REMARK 500  3 PHE A  29       30.65    -92.13                                   
REMARK 500  3 LYS A  46      150.45    -45.54                                   
REMARK 500  3 ASP A  84      105.74    -59.35                                   
REMARK 500  3 LYS A  90       51.04     39.78                                   
REMARK 500  3 ILE A 106       99.63    -50.52                                   
REMARK 500  3 PRO A 133        0.06    -69.75                                   
REMARK 500  3 ASN A 140       32.67     38.86                                   
REMARK 500  4 SER A  21      -74.66    -80.58                                   
REMARK 500  4 LYS A  46      135.28    -39.87                                   
REMARK 500  4 SER A  65      147.48   -172.02                                   
REMARK 500  4 LYS A  92      -55.78   -131.30                                   
REMARK 500  4 SER A 107      -65.24   -102.28                                   
REMARK 500  4 PRO A 133     -168.74    -69.76                                   
REMARK 500  4 PRO A 144        0.26    -69.76                                   
REMARK 500  4 SER A 145      139.91    -35.58                                   
REMARK 500  5 LYS A  10       47.34   -102.09                                   
REMARK 500  5 SER A  21      -76.34    -67.06                                   
REMARK 500  5 ALA A  55       79.89   -108.58                                   
REMARK 500  5 ASP A  84       92.40    -64.63                                   
REMARK 500  5 TYR A  85      104.28    -59.53                                   
REMARK 500  5 LYS A  92      -63.90   -129.42                                   
REMARK 500  5 ASN A 105       65.48   -117.75                                   
REMARK 500  5 LEU A 139      -69.21   -126.27                                   
REMARK 500  5 SER A 146      173.58    -48.66                                   
REMARK 500  6 SER A  21      -75.70    -70.23                                   
REMARK 500  6 PRO A  28     -174.50    -69.69                                   
REMARK 500  6 SER A  43     -177.77    -61.89                                   
REMARK 500  6 ILE A 106       52.13     34.44                                   
REMARK 500  6 LYS A 138      104.13    -38.91                                   
REMARK 500  7 SER A   3       47.79     38.36                                   
REMARK 500  7 SER A   5       49.18     37.88                                   
REMARK 500  7 SER A  21      -75.77    -77.64                                   
REMARK 500  7 PHE A  29       32.27    -93.32                                   
REMARK 500  7 ALA A  55       70.33   -111.93                                   
REMARK 500  7 ASP A  69      150.72    -40.21                                   
REMARK 500  7 ILE A 106      112.87    -37.79                                   
REMARK 500  7 SER A 107      -73.05   -125.85                                   
REMARK 500  7 ASN A 140      149.40    -36.25                                   
REMARK 500  8 SER A   2      131.27    -35.99                                   
REMARK 500  8 GLU A  12       46.56    -88.82                                   
REMARK 500  8 SER A  21      -74.99    -73.66                                   
REMARK 500  8 ASP A  44       36.80    -98.54                                   
REMARK 500  8 ASP A  69      155.90    -48.87                                   
REMARK 500  8 ASP A  84      105.43    -59.15                                   
REMARK 500  8 PHE A 101      162.49    -45.90                                   
REMARK 500  8 SER A 107      -66.24   -125.42                                   
REMARK 500  8 ASN A 134       87.86    -49.46                                   
REMARK 500  9 SER A   2      124.34   -173.25                                   
REMARK 500  9 GLU A  12       37.58    -86.48                                   
REMARK 500  9 SER A  21      -75.69    -71.62                                   
REMARK 500  9 SER A  43      173.16    -54.27                                   
REMARK 500  9 ASP A  84       94.14    -46.85                                   
REMARK 500  9 LYS A  92       70.81   -107.82                                   
REMARK 500  9 SER A 107      -53.66   -130.54                                   
REMARK 500  9 PRO A 133        0.78    -69.78                                   
REMARK 500  9 ASN A 136       91.19    -53.06                                   
REMARK 500 10 SER A  21      -75.50    -69.35                                   
REMARK 500 10 SER A  43      174.79    -59.77                                   
REMARK 500 10 ASP A  84       87.24    -67.39                                   
REMARK 500 10 ASN A 105       43.51    -87.03                                   
REMARK 500 10 LYS A 138      105.01    -48.01                                   
REMARK 500 10 LEU A 139      155.68    -39.37                                   
REMARK 500 10 PRO A 144     -175.23    -69.79                                   
REMARK 500 10 SER A 145      -45.75   -131.04                                   
REMARK 500 11 SER A   5       41.86    -84.61                                   
REMARK 500 11 SER A  21      -74.13    -77.80                                   
REMARK 500 11 ALA A  55       58.72   -118.26                                   
REMARK 500 11 SER A  65      145.98   -171.65                                   
REMARK 500 11 ASP A  84       92.55    -67.14                                   
REMARK 500 11 SER A  91      -74.82    -83.90                                   
REMARK 500 11 HIS A  93      118.19   -174.89                                   
REMARK 500 11 ILE A 106       51.97     33.64                                   
REMARK 500 11 LEU A 139     -178.16    -54.04                                   
REMARK 500 12 SER A   2      109.03   -172.13                                   
REMARK 500 12 ALA A   9      130.17   -172.78                                   
REMARK 500 12 GLU A  12       79.13   -102.37                                   
REMARK 500 12 SER A  21      -75.93    -70.19                                   
REMARK 500 12 PRO A  28     -178.78    -69.78                                   
REMARK 500 12 ASP A  69      151.39    -46.40                                   
REMARK 500 12 ASP A  84       93.33    -58.83                                   
REMARK 500 12 TYR A  85       99.39    -53.69                                   
REMARK 500 12 ASN A 105      -67.49   -109.68                                   
REMARK 500 12 ILE A 106       44.48     37.60                                   
REMARK 500 12 LEU A 139       70.85   -100.03                                   
REMARK 500 12 SER A 142      116.28   -160.51                                   
REMARK 500 12 PRO A 144     -175.39    -69.75                                   
REMARK 500 13 SER A   2      161.88    -46.59                                   
REMARK 500 13 SER A  21      -75.03    -89.38                                   
REMARK 500 13 ASP A  69      151.19    -47.80                                   
REMARK 500 13 ASP A  84       85.18    -65.13                                   
REMARK 500 13 TYR A  85      107.06    -50.89                                   
REMARK 500 13 ILE A 106      127.93    -39.59                                   
REMARK 500 13 PRO A 133       88.49    -69.74                                   
REMARK 500 13 SER A 146       87.55    -63.53                                   
REMARK 500 14 SER A   3      -54.62   -128.72                                   
REMARK 500 14 MET A   8       47.52     38.55                                   
REMARK 500 14 GLU A  12       36.10    -90.90                                   
REMARK 500 14 SER A  21      -75.34    -71.83                                   
REMARK 500 14 ASP A  44       42.07   -106.85                                   
REMARK 500 14 ASP A  69      153.66    -49.20                                   
REMARK 500 14 LYS A  90       45.94     33.74                                   
REMARK 500 14 ILE A 106      103.09    -39.28                                   
REMARK 500 14 SER A 107      -70.23    -91.05                                   
REMARK 500 14 SER A 145      140.18    -34.96                                   
REMARK 500 15 SER A  21      -76.38    -68.37                                   
REMARK 500 15 PHE A  29       33.58    -95.33                                   
REMARK 500 15 LYS A  46      153.33    -40.71                                   
REMARK 500 15 ASN A  88       34.36    -99.47                                   
REMARK 500 15 PRO A 133       98.29    -69.76                                   
REMARK 500 16 SER A   2      -55.22   -133.51                                   
REMARK 500 16 SER A   6      142.09   -170.85                                   
REMARK 500 16 LYS A  10       42.10     39.47                                   
REMARK 500 16 HIS A  11       41.86   -109.50                                   
REMARK 500 16 SER A  21      -75.40    -73.79                                   
REMARK 500 16 LYS A  46      147.52    -36.67                                   
REMARK 500 16 ALA A  55       73.46   -111.70                                   
REMARK 500 16 ASP A  69      152.18    -48.11                                   
REMARK 500 16 ASP A  84       86.91    -66.83                                   
REMARK 500 16 SER A 107      -69.63   -122.90                                   
REMARK 500 16 LEU A 139       33.73     34.09                                   
REMARK 500 17 GLU A  12       49.05   -108.82                                   
REMARK 500 17 SER A  21      -75.42    -72.04                                   
REMARK 500 17 ALA A  55       73.34   -112.12                                   
REMARK 500 17 ASP A  84       99.49    -69.45                                   
REMARK 500 17 TYR A  85      107.49    -58.13                                   
REMARK 500 17 ILE A 106       94.66    -37.20                                   
REMARK 500 17 LEU A 139      100.69    -36.81                                   
REMARK 500 17 SER A 142      175.22    -47.46                                   
REMARK 500 18 SER A  21      -77.17    -68.23                                   
REMARK 500 18 ALA A  55       62.17   -118.93                                   
REMARK 500 18 ASP A  69      151.03    -48.70                                   
REMARK 500 18 PRO A 144     -173.03    -69.77                                   
REMARK 500 19 SER A   2       99.62    -67.54                                   
REMARK 500 19 ALA A   9      126.34   -172.17                                   
REMARK 500 19 SER A  21      -76.23    -83.48                                   
REMARK 500 19 ARG A  58      -37.87    -38.74                                   
REMARK 500 19 PHE A  83      119.13   -161.74                                   
REMARK 500 19 ASP A  84       81.22    -57.02                                   
REMARK 500 19 LYS A  90      139.32   -172.13                                   
REMARK 500 19 ILE A 106      101.46    -51.27                                   
REMARK 500 19 SER A 107      -64.31    -95.42                                   
REMARK 500 19 PRO A 133        1.06    -69.76                                   
REMARK 500 19 ASP A 137       25.51     47.96                                   
REMARK 500 19 SER A 146      109.55   -170.78                                   
REMARK 500 20 SER A   5      -47.44   -130.76                                   
REMARK 500 20 SER A  21      -76.47    -67.96                                   
REMARK 500 20 SER A  43      176.99    -53.49                                   
REMARK 500 20 ASP A  84       88.04    -69.46                                   
REMARK 500 20 PHE A 101      154.55    -44.30                                   
REMARK 500 20 ILE A 106      104.10    -43.94                                   
REMARK 500 20 SER A 107      -54.46   -122.40                                   
REMARK 500 20 GLU A 135       99.80    -44.58                                   
REMARK 500 20 ASP A 137       93.46    -50.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MMT007116377.1   RELATED DB: TARGETDB                    
DBREF  2CRI A    8   141  UNP    Q9WV55   VAPA_MOUSE       1    134             
SEQADV 2CRI GLY A    1  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI SER A    2  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI SER A    3  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI GLY A    4  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI SER A    5  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI SER A    6  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI GLY A    7  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI SER A  142  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI GLY A  143  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI PRO A  144  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI SER A  145  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI SER A  146  UNP  Q9WV55              CLONING ARTIFACT               
SEQADV 2CRI GLY A  147  UNP  Q9WV55              CLONING ARTIFACT               
SEQRES   1 A  147  GLY SER SER GLY SER SER GLY MET ALA LYS HIS GLU GLN          
SEQRES   2 A  147  ILE LEU VAL LEU ASP PRO PRO SER ASP LEU LYS PHE LYS          
SEQRES   3 A  147  GLY PRO PHE THR ASP VAL VAL THR THR ASN LEU LYS LEU          
SEQRES   4 A  147  GLN ASN PRO SER ASP ARG LYS VAL CYS PHE LYS VAL LYS          
SEQRES   5 A  147  THR THR ALA PRO ARG ARG TYR CYS VAL ARG PRO ASN SER          
SEQRES   6 A  147  GLY ILE ILE ASP PRO GLY SER ILE VAL THR VAL SER VAL          
SEQRES   7 A  147  MET LEU GLN PRO PHE ASP TYR ASP PRO ASN GLU LYS SER          
SEQRES   8 A  147  LYS HIS LYS PHE MET VAL GLN THR ILE PHE ALA PRO PRO          
SEQRES   9 A  147  ASN ILE SER ASP MET GLU ALA VAL TRP LYS GLU ALA LYS          
SEQRES  10 A  147  PRO ASP GLU LEU MET ASP SER LYS LEU ARG CYS VAL PHE          
SEQRES  11 A  147  GLU MET PRO ASN GLU ASN ASP LYS LEU ASN ASP SER GLY          
SEQRES  12 A  147  PRO SER SER GLY                                              
HELIX    1   1 ASP A  108  ALA A  116  1                                   9    
SHEET    1   A 4 VAL A  16  ASP A  18  0                                        
SHEET    2   A 4 THR A  35  GLN A  40 -1  O  LYS A  38   N  ASP A  18           
SHEET    3   A 4 ILE A  73  LEU A  80 -1  O  VAL A  78   N  THR A  35           
SHEET    4   A 4 TYR A  59  ARG A  62 -1  N  CYS A  60   O  MET A  79           
SHEET    1   B 5 ASP A  22  LYS A  26  0                                        
SHEET    2   B 5 MET A 122  GLU A 131  1  O  GLU A 131   N  PHE A  25           
SHEET    3   B 5 PHE A  95  PHE A 101 -1  N  PHE A  95   O  LEU A 126           
SHEET    4   B 5 VAL A  47  THR A  53 -1  N  CYS A  48   O  ILE A 100           
SHEET    5   B 5 SER A  65  ILE A  67 -1  O  GLY A  66   N  PHE A  49           
CISPEP   1 ASP A   18    PRO A   19          1         0.00                     
CISPEP   2 GLY A   27    PRO A   28          1         0.07                     
CISPEP   3 ARG A   62    PRO A   63          1         0.01                     
CISPEP   4 ASP A   18    PRO A   19          2         0.04                     
CISPEP   5 GLY A   27    PRO A   28          2         0.04                     
CISPEP   6 ARG A   62    PRO A   63          2         0.02                     
CISPEP   7 ASP A   18    PRO A   19          3         0.07                     
CISPEP   8 GLY A   27    PRO A   28          3         0.03                     
CISPEP   9 ARG A   62    PRO A   63          3        -0.02                     
CISPEP  10 ASP A   18    PRO A   19          4         0.07                     
CISPEP  11 GLY A   27    PRO A   28          4         0.03                     
CISPEP  12 ARG A   62    PRO A   63          4        -0.01                     
CISPEP  13 ASP A   18    PRO A   19          5        -0.01                     
CISPEP  14 GLY A   27    PRO A   28          5         0.11                     
CISPEP  15 ARG A   62    PRO A   63          5        -0.02                     
CISPEP  16 ASP A   18    PRO A   19          6         0.10                     
CISPEP  17 GLY A   27    PRO A   28          6         0.01                     
CISPEP  18 ARG A   62    PRO A   63          6        -0.03                     
CISPEP  19 ASP A   18    PRO A   19          7         0.06                     
CISPEP  20 GLY A   27    PRO A   28          7         0.13                     
CISPEP  21 ARG A   62    PRO A   63          7        -0.02                     
CISPEP  22 ASP A   18    PRO A   19          8        -0.02                     
CISPEP  23 GLY A   27    PRO A   28          8         0.02                     
CISPEP  24 ARG A   62    PRO A   63          8        -0.07                     
CISPEP  25 ASP A   18    PRO A   19          9         0.00                     
CISPEP  26 GLY A   27    PRO A   28          9         0.06                     
CISPEP  27 ARG A   62    PRO A   63          9         0.03                     
CISPEP  28 ASP A   18    PRO A   19         10         0.03                     
CISPEP  29 GLY A   27    PRO A   28         10         0.05                     
CISPEP  30 ARG A   62    PRO A   63         10        -0.02                     
CISPEP  31 ASP A   18    PRO A   19         11         0.03                     
CISPEP  32 GLY A   27    PRO A   28         11         0.08                     
CISPEP  33 ARG A   62    PRO A   63         11        -0.02                     
CISPEP  34 ASP A   18    PRO A   19         12        -0.03                     
CISPEP  35 GLY A   27    PRO A   28         12         0.09                     
CISPEP  36 ARG A   62    PRO A   63         12        -0.08                     
CISPEP  37 ASP A   18    PRO A   19         13        -0.02                     
CISPEP  38 GLY A   27    PRO A   28         13         0.05                     
CISPEP  39 ARG A   62    PRO A   63         13        -0.02                     
CISPEP  40 ASP A   18    PRO A   19         14         0.02                     
CISPEP  41 GLY A   27    PRO A   28         14         0.08                     
CISPEP  42 ARG A   62    PRO A   63         14         0.03                     
CISPEP  43 ASP A   18    PRO A   19         15        -0.04                     
CISPEP  44 GLY A   27    PRO A   28         15         0.05                     
CISPEP  45 ARG A   62    PRO A   63         15         0.06                     
CISPEP  46 ASP A   18    PRO A   19         16        -0.02                     
CISPEP  47 GLY A   27    PRO A   28         16         0.07                     
CISPEP  48 ARG A   62    PRO A   63         16         0.04                     
CISPEP  49 ASP A   18    PRO A   19         17         0.08                     
CISPEP  50 GLY A   27    PRO A   28         17         0.04                     
CISPEP  51 ARG A   62    PRO A   63         17        -0.05                     
CISPEP  52 ASP A   18    PRO A   19         18         0.09                     
CISPEP  53 GLY A   27    PRO A   28         18         0.09                     
CISPEP  54 ARG A   62    PRO A   63         18         0.05                     
CISPEP  55 ASP A   18    PRO A   19         19         0.00                     
CISPEP  56 GLY A   27    PRO A   28         19         0.02                     
CISPEP  57 ARG A   62    PRO A   63         19         0.06                     
CISPEP  58 ASP A   18    PRO A   19         20        -0.03                     
CISPEP  59 GLY A   27    PRO A   28         20         0.02                     
CISPEP  60 ARG A   62    PRO A   63         20        -0.06                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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