HEADER    IMMUNE SYSTEM                           07-MAR-10   2X89              
TITLE     STRUCTURE OF THE BETA2_MICROGLOBULIN INVOLVED IN                      
TITLE    2 AMYLOIDOGENESIS                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTIBODY;                                                  
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   7 CHAIN: D, E, F, G;                                                   
COMPND   8 FRAGMENT: RESIDUES 27-119;                                           
COMPND   9 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;                           
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IMMUNE SYSTEM                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.DOMANSKA,V.SRINIVASAN,S.VANDERHAEGEN,E.PARDON,J.A.MARQUEZ,          
AUTHOR   2 V.BELLOTTI,L.WYNS,J.STEYAERT                                         
REVDAT   1   19-JAN-11 2X89    0                                                
JRNL        AUTH   K.DOMANSKA,S.VANDERHAEGEN,V.SRINIVASAN,E.PARDON,F.DUPEUX,    
JRNL        AUTH 2 J.A.MARQUEZ,S.GIORGETTI,M.STOPPINI,L.WYNS,V.BELLOTTI,        
JRNL        AUTH 3 J.STEYAERT                                                   
JRNL        TITL   ATOMIC STRUCTURE OF A NANOBODY-TRAPPED DOMAIN- SWAPPED       
JRNL        TITL 2 DIMER OF AN AMYLOIDOGENIC {BETA}2- MICROGLOBULIN VARIANT.    
JRNL        REF    PROC.NATL.ACAD.SCI.USA                     2011              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   21220305                                                     
JRNL        DOI    10.1073/PNAS.1008560108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.86                          
REMARK   3   NUMBER OF REFLECTIONS             : 62741                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.23962                         
REMARK   3   R VALUE            (WORKING SET) : 0.23813                         
REMARK   3   FREE R VALUE                     : 0.26691                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.1                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3356                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.160                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.215                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4562                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.269                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 216                          
REMARK   3   BIN FREE R VALUE                    : 0.333                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5935                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 295                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.626                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07                                                
REMARK   3    B22 (A**2) : 0.04                                                 
REMARK   3    B33 (A**2) : 0.01                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.03                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.215         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.186         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.727         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6078 ; 0.028 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8226 ; 2.439 ; 1.933       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   735 ; 9.840 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   309 ;38.271 ;23.625       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   985 ;18.965 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;21.780 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   853 ; 0.187 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4722 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2794 ; 0.282 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3956 ; 0.318 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   414 ; 0.223 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    87 ; 0.290 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.170 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3792 ; 1.482 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5899 ; 2.269 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2702 ; 3.678 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2327 ; 5.596 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   1                                
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    1                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     95       A     220      4                      
REMARK   3           1     B     95       B     220      4                      
REMARK   3           1     C     95       C     220      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    974 ;  0.43 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    974 ;  0.61 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    974 ;  0.41 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    974 ;  2.23 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    974 ;  2.09 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    974 ;  2.27 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   2                                
REMARK   3     CHAIN NAMES                    : D E F G                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    1                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D      1       D      92      4                      
REMARK   3           1     E      1       E      92      4                      
REMARK   3           1     F      1       F      92      4                      
REMARK   3           1     G      1       G      92      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    D    (A):    672 ;  1.32 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    E    (A):    672 ;  1.51 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    F    (A):    672 ;  1.19 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    G    (A):    672 ;  1.37 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    D (A**2):    672 ;  1.97 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    E (A**2):    672 ;  2.08 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    F (A**2):    672 ;  2.21 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    G (A**2):    672 ;  2.23 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   128                          
REMARK   3    ORIGIN FOR THE GROUP (A): -67.8247  18.3046   6.6027              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2350 T22:  -0.2469                                     
REMARK   3      T33:  -0.2336 T12:   0.0091                                     
REMARK   3      T13:   0.0082 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0279 L22:   2.5568                                     
REMARK   3      L33:   1.9727 L12:   1.0529                                     
REMARK   3      L13:  -1.2964 L23:  -0.8182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1351 S12:   0.1223 S13:   0.3975                       
REMARK   3      S21:  -0.1184 S22:  -0.0401 S23:   0.1939                       
REMARK   3      S31:  -0.1895 S32:  -0.2109 S33:  -0.0950                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   128                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.1805  -5.2654  19.2975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3128 T22:  -0.3256                                     
REMARK   3      T33:  -0.3015 T12:   0.0094                                     
REMARK   3      T13:  -0.0055 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1111 L22:   3.3466                                     
REMARK   3      L33:   3.7538 L12:   0.6746                                     
REMARK   3      L13:  -1.4072 L23:  -2.2265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0267 S12:   0.2415 S13:  -0.0600                       
REMARK   3      S21:  -0.0413 S22:   0.0477 S23:   0.0863                       
REMARK   3      S31:   0.2038 S32:  -0.2467 S33:  -0.0743                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   128                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.3367   2.5009 -44.2155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2486 T22:  -0.3275                                     
REMARK   3      T33:  -0.2599 T12:   0.0253                                     
REMARK   3      T13:   0.0349 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5541 L22:   1.5914                                     
REMARK   3      L33:   5.9706 L12:  -0.1196                                     
REMARK   3      L13:   1.0626 L23:   0.2278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0276 S12:  -0.0349 S13:  -0.3027                       
REMARK   3      S21:  -0.0359 S22:   0.0610 S23:   0.0354                       
REMARK   3      S31:   0.5604 S32:  -0.0167 S33:  -0.0886                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     6        D    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.7070  13.4972  -4.8917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2763 T22:  -0.1574                                     
REMARK   3      T33:  -0.1379 T12:  -0.0300                                     
REMARK   3      T13:  -0.0036 T23:   0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2732 L22:   1.2346                                     
REMARK   3      L33:   5.9368 L12:  -0.3190                                     
REMARK   3      L13:  -0.6844 L23:  -1.9559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0951 S12:  -0.2161 S13:   0.0490                       
REMARK   3      S21:  -0.0216 S22:  -0.0187 S23:  -0.2374                       
REMARK   3      S31:  -0.0650 S32:   0.4987 S33:  -0.0763                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     6        E    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.9340  20.8889 -22.2631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1964 T22:  -0.2662                                     
REMARK   3      T33:  -0.2359 T12:   0.0078                                     
REMARK   3      T13:   0.0093 T23:  -0.0440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3420 L22:   1.5650                                     
REMARK   3      L33:   3.7796 L12:   0.0119                                     
REMARK   3      L13:  -0.6062 L23:  -1.1947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1249 S12:  -0.1488 S13:   0.1688                       
REMARK   3      S21:   0.0504 S22:   0.0681 S23:   0.0521                       
REMARK   3      S31:  -0.1192 S32:   0.0901 S33:  -0.1930                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     6        F    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3838   5.4925   2.3181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2208 T22:  -0.2201                                     
REMARK   3      T33:  -0.2161 T12:  -0.0091                                     
REMARK   3      T13:   0.0160 T23:   0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3197 L22:   1.6347                                     
REMARK   3      L33:   4.2338 L12:   1.4266                                     
REMARK   3      L13:  -0.0309 L23:   0.3720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0253 S12:   0.3187 S13:   0.1339                       
REMARK   3      S21:  -0.3254 S22:   0.2494 S23:  -0.1578                       
REMARK   3      S31:  -0.1617 S32:   0.3897 S33:  -0.2241                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     6        G    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0042   3.2311 -16.8882              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1011 T22:  -0.1261                                     
REMARK   3      T33:  -0.0751 T12:   0.0149                                     
REMARK   3      T13:  -0.0122 T23:   0.0518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0058 L22:   0.0615                                     
REMARK   3      L33:   9.9405 L12:  -0.0829                                     
REMARK   3      L13:  -0.0907 L23:   0.7446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1205 S12:   0.3062 S13:   0.2385                       
REMARK   3      S21:  -0.0285 S22:   0.1114 S23:  -0.0256                       
REMARK   3      S31:  -0.6295 S32:  -0.0463 S33:  -0.2319                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.     
REMARK   3   ONE MOLECULE IN THE ASYMMETRIC UNIT IS DISORDERED.                 
REMARK   4                                                                      
REMARK   4 2X89 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAR-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-42956.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97812                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66127                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.16                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.32                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BMG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.7                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6%PEG4000 0.2M AMMONIUM                  
REMARK 280  SULPHATE 0.1MNAACETEATE4.6                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       50.43200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP D    98                                                      
REMARK 465     MET D    99                                                      
REMARK 465     ARG E    97                                                      
REMARK 465     ASP E    98                                                      
REMARK 465     MET E    99                                                      
REMARK 465     ARG F    97                                                      
REMARK 465     ASP F    98                                                      
REMARK 465     MET F    99                                                      
REMARK 465     ALA G    15                                                      
REMARK 465     GLU G    16                                                      
REMARK 465     ASN G    17                                                      
REMARK 465     SER G    57                                                      
REMARK 465     LYS G    58                                                      
REMARK 465     ASP G    59                                                      
REMARK 465     ASP G    98                                                      
REMARK 465     MET G    99                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A 117    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ALA D  15    CB                                                  
REMARK 470     GLU D  16    CB   CG   CD   OE1  OE2                             
REMARK 470     ASN D  17    CB   CG   OD1  ND2                                  
REMARK 470     LYS D  19    CG   CD   CE   NZ                                   
REMARK 470     SER E  57    CB   OG                                             
REMARK 470     LYS E  58    CB   CG   CD   CE   NZ                              
REMARK 470     ASP E  59    CB   CG   OD1  OD2                                  
REMARK 470     TRP E  60    CH2                                                 
REMARK 470     TRP E  60    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3              
REMARK 470     LYS G  19    CG   CD   CE   NZ                                   
REMARK 470     SER G  20    OG                                                  
REMARK 470     LEU G  40    CG   CD1  CD2                                       
REMARK 470     TRP G  60    CH2                                                 
REMARK 470     TRP G  60    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3              
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR C   117     O    HOH C  2039              0.74            
REMARK 500   CD1  TYR C   117     O    HOH C  2041              0.84            
REMARK 500   CE1  TYR C   117     O    HOH C  2041              0.89            
REMARK 500   CE2  TYR C   117     O    HOH C  2040              0.89            
REMARK 500   CD2  TYR C   117     O    HOH C  2040              0.98            
REMARK 500   CZ   TYR C   117     O    HOH C  2039              1.05            
REMARK 500   CG   TYR C   117     O    HOH C  2041              1.53            
REMARK 500   CZ   TYR C   117     O    HOH C  2041              1.56            
REMARK 500   CE2  TYR C   117     O    HOH C  2039              1.83            
REMARK 500   OD1  ASP C    99     NH1  ARG C   103              1.98            
REMARK 500   CD2  TYR C   117     O    HOH C  2041              1.98            
REMARK 500   CE2  TYR C   117     O    HOH C  2041              2.00            
REMARK 500   O    ASP C    73     O    ALA C    75              2.04            
REMARK 500   OG   SER G    11     O    HIS G    13              2.10            
REMARK 500   NH2  ARG C   103     NE2  GLN G     8              2.11            
REMARK 500   CZ   TYR C   117     O    HOH C  2040              2.12            
REMARK 500   OE1  GLN C    72     CG2  VAL C    79              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS B  22   CB    CYS B  22   SG     -0.107                       
REMARK 500    ARG B  55   C     ASP B  56   N      -0.169                       
REMARK 500    GLU B  87   CG    GLU B  87   CD      0.091                       
REMARK 500    GLU B  89   CG    GLU B  89   CD      0.101                       
REMARK 500    CYS B  96   CA    CYS B  96   CB      0.135                       
REMARK 500    CYS B 104   CB    CYS B 104   SG     -0.101                       
REMARK 500    GLU C  89   CB    GLU C  89   CG      0.153                       
REMARK 500    GLU C  89   CG    GLU C  89   CD      0.114                       
REMARK 500    GLU C  89   CD    GLU C  89   OE2     0.085                       
REMARK 500    CYS D  25   CB    CYS D  25   SG     -0.104                       
REMARK 500    CYS D  80   CB    CYS D  80   SG     -0.134                       
REMARK 500    GLU E  36   CG    GLU E  36   CD      0.153                       
REMARK 500    GLU E  36   CD    GLU E  36   OE1     0.076                       
REMARK 500    CYS E  80   CB    CYS E  80   SG     -0.105                       
REMARK 500    CYS F  80   CB    CYS F  80   SG     -0.139                       
REMARK 500    PHE G  30   N     PHE G  30   CA      0.137                       
REMARK 500    TRP G  95   CE3   TRP G  95   CZ3    -0.146                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  38   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP A  56   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP B  56   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    GLN B  72   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    CYS B  96   CA  -  CB  -  SG  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ARG C  19   CG  -  CD  -  NE  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    ASP C  29   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG C  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    LYS C  65   CD  -  CE  -  NZ  ANGL. DEV. = -22.1 DEGREES          
REMARK 500    SER C  85   CB  -  CA  -  C   ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ARG C 103   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    MET D   6   CG  -  SD  -  CE  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG E  81   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG E  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP F  59   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG F  81   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG F  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    GLY G  29   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    PHE G  30   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    LEU G  64   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU G  64   CB  -  CG  -  CD2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG G  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP A  29       29.78     43.96                                   
REMARK 500    TYR A  32      139.49   -170.76                                   
REMARK 500    LYS A  76       -1.70   -158.30                                   
REMARK 500    ASN A  77      -12.53     76.79                                   
REMARK 500    ALA A  92      173.36    177.81                                   
REMARK 500    TYR B  32      141.56   -171.98                                   
REMARK 500    GLN B  72      138.17    147.83                                   
REMARK 500    ASN B  77      -43.15     74.68                                   
REMARK 500    ALA B  92      166.88    174.98                                   
REMARK 500    VAL B 108      135.41    -39.34                                   
REMARK 500    ALA C  14      134.30    -35.23                                   
REMARK 500    ASP C  29       44.73     32.08                                   
REMARK 500    GLN C  72     -128.14   -154.49                                   
REMARK 500    ASP C  73      148.68    124.58                                   
REMARK 500    ALA C  75     -150.03    -75.03                                   
REMARK 500    ASN C  77      -35.67    115.02                                   
REMARK 500    ALA C  92      163.08    170.70                                   
REMARK 500    ASN D  17       -1.57    102.69                                   
REMARK 500    LYS D  19      -78.74    -99.22                                   
REMARK 500    SER D  20      124.95    146.12                                   
REMARK 500    LYS E  48      -47.28    -27.52                                   
REMARK 500    SER E  57       98.99    -68.58                                   
REMARK 500    LYS E  58       21.39    130.09                                   
REMARK 500    ASN F  42       38.45     36.86                                   
REMARK 500    SER F  57       22.30     83.55                                   
REMARK 500    ASP F  59     -158.59    145.96                                   
REMARK 500    TRP F  60       -9.64     70.78                                   
REMARK 500    PRO G  32      -13.68    -47.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A   74     ALA A   75                   43.05                    
REMARK 500 ALA A   75     LYS A   76                   93.65                    
REMARK 500 SER B    7     GLY B    8                 -128.33                    
REMARK 500 SER B   71     GLN B   72                 -130.89                    
REMARK 500 ALA B   75     LYS B   76                  139.93                    
REMARK 500 LYS B   76     ASN B   77                 -144.73                    
REMARK 500 LYS C   76     ASN C   77                 -144.85                    
REMARK 500 GLY C  119     GLN C  120                  143.18                    
REMARK 500 SER D   20     ASN D   21                 -149.28                    
REMARK 500 LYS E   48     VAL E   49                 -132.27                    
REMARK 500 LYS F   58     ASP F   59                  149.36                    
REMARK 500 SER F   61     PHE F   62                 -149.13                    
REMARK 500 HIS G   31     PRO G   32                 -146.23                    
REMARK 500 SER G   33     ASP G   34                  149.86                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN B  74        21.0      L          L   OUTSIDE RANGE           
REMARK 500    LYS B  76        23.7      L          L   OUTSIDE RANGE           
REMARK 500    THR B 125        22.4      L          L   OUTSIDE RANGE           
REMARK 500    THR C  28        22.9      L          L   OUTSIDE RANGE           
REMARK 500    ASP C  29        21.3      L          L   OUTSIDE RANGE           
REMARK 500    MET D   6        17.9      L          L   OUTSIDE RANGE           
REMARK 500    MET E   6        20.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL E  49        22.8      L          L   OUTSIDE RANGE           
REMARK 500    MET F   6        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP F  59        17.7      L          L   OUTSIDE RANGE           
REMARK 500    MET G   6        21.3      L          L   OUTSIDE RANGE           
REMARK 500    PHE G  30        18.6      L          L   OUTSIDE RANGE           
REMARK 500    HIS G  31        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UQS   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A                          
REMARK 900   BOUND BACTERIAL GLYCOLIPID                                         
REMARK 900 RELATED ID: 1BD2   RELATED DB: PDB                                   
REMARK 900  COMPLEX BETWEEN HUMAN T-CELL RECEPTOR B7,                           
REMARK 900  VIRAL PEPTIDE (TAX) AND MHC CLASS I                                 
REMARK 900  MOLECULE HLA-A 0201                                                 
REMARK 900 RELATED ID: 2ESV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE HLA-E-VMAPRTLIL/KK50.4                             
REMARK 900  TCR COMPLEX                                                         
REMARK 900 RELATED ID: 2XKS   RELATED DB: PDB                                   
REMARK 900  PRION-LIKE CONVERSION DURING AMYLOID FORMATION                      
REMARK 900   AT ATOMIC RESOLUTION                                               
REMARK 900 RELATED ID: 2AK4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SB27 TCR IN COMPLEX                            
REMARK 900  WITH HLA-B*3508-13MER PEPTIDE                                       
REMARK 900 RELATED ID: 1YPZ   RELATED DB: PDB                                   
REMARK 900  IMMUNE RECEPTOR                                                     
REMARK 900 RELATED ID: 1IM3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CYTOMEGALOVIRUS                      
REMARK 900   PROTEIN US2BOUND TO THE MHC CLASS I                                
REMARK 900  MOLECULE HLA-A2/TAX                                                 
REMARK 900 RELATED ID: 1I7U   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CLASS I MHC A2 IN                              
REMARK 900  COMPLEX WITH PEPTIDEP1049-6V                                        
REMARK 900 RELATED ID: 1UXW   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED                           
REMARK 900  WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE                          
REMARK 900   (LMP2) OF EPSTEIN-BARR VIRUS                                       
REMARK 900 RELATED ID: 1C16   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/                            
REMARK 900  DELTA T CELL LIGAND T22                                             
REMARK 900 RELATED ID: 1HSA   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN HLA-                       
REMARK 900  B(ASTERISK)2705                                                     
REMARK 900 RELATED ID: 2AXF   RELATED DB: PDB                                   
REMARK 900  THE IMMUNOGENICITY OF A VIRAL CYTOTOXIC T                           
REMARK 900  CELL EPITOPE ISCONTROLLED BY ITS MHC-BOUND                          
REMARK 900  CONFORMATION                                                        
REMARK 900 RELATED ID: 1GZP   RELATED DB: PDB                                   
REMARK 900  CD1B IN COMPLEX WITH GM2 GANGLIOSIDE                                
REMARK 900 RELATED ID: 2BNQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL AND KINETIC BASIS FOR HIGHTENED                          
REMARK 900  IMMUNOGENICITY OF T CELL VACCINES                                   
REMARK 900 RELATED ID: 1W72   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A1:MAGE-A1 IN                              
REMARK 900  COMPLEX WITH FAB-HYB3                                               
REMARK 900 RELATED ID: 2JCC   RELATED DB: PDB                                   
REMARK 900  AH3 RECOGNITION OF MUTANT HLA-A2 W167A                              
REMARK 900 RELATED ID: 2BCK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A*2402 COMPLEXED                           
REMARK 900  WITH A TELOMERASEPEPTIDE                                            
REMARK 900 RELATED ID: 1DE4   RELATED DB: PDB                                   
REMARK 900  HEMOCHROMATOSIS PROTEIN HFE COMPLEXED WITH                          
REMARK 900  TRANSFERRINRECEPTOR                                                 
REMARK 900 RELATED ID: 2VLK   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN                        
REMARK 900   IMMUNODOMINANT T-CELL RECEPTOR ARE                                 
REMARK 900  PROGRAMMED BY ITS VBETA DOMAIN                                      
REMARK 900 RELATED ID: 1EXU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN MHC-RELATED                          
REMARK 900  FC RECEPTOR                                                         
REMARK 900 RELATED ID: 1QRN   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED                         
REMARK 900   WITH HLA-A2 BOUND TO ALTERED HTLV-1                                
REMARK 900  TAX PEPTIDE P6A                                                     
REMARK 900 RELATED ID: 2HLA   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN AW                         
REMARK 900  68.1 (HLA-AW 68.1, HUMAN LEUCOCYTE                                  
REMARK 900  ANTIGEN)                                                            
REMARK 900 RELATED ID: 1MHE   RELATED DB: PDB                                   
REMARK 900  THE HUMAN NON-CLASSICAL MAJOR                                       
REMARK 900  HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E                           
REMARK 900 RELATED ID: 1EEZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE DETERMINATION OF HLA-A2.1                         
REMARK 900   COMPLEXED TOGP2 PEPTIDE VARIANT(I2L/V5L)                           
REMARK 900 RELATED ID: 1IM9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN NATURAL                              
REMARK 900  KILLER CELLINHIBITORY RECEPTOR KIR2DL1 BOUND                        
REMARK 900  TO ITS MHC LIGAND HLA-CW4                                           
REMARK 900 RELATED ID: 1JHT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A2*0201 IN                                 
REMARK 900  COMPLEX WITH ANONAMERIC ALTERED PEPTIDE LIGAND                      
REMARK 900   (ALGIGILTV) FROM THE MART-1/MELAN-A.                               
REMARK 900 RELATED ID: 1QQD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR                          
REMARK 900   THE KIR2D NATURAL KILLER CELL INHIBITORY                           
REMARK 900  RECEPTOR                                                            
REMARK 900 RELATED ID: 1QR1   RELATED DB: PDB                                   
REMARK 900  POOR BINDING OF A HER-2/NEU EPITOPE (GP2                            
REMARK 900  ) TO HLA-A2.1 IS DUE TO A LACK OF                                   
REMARK 900  INTERACTIONS IN THE CENTER OF THE PEPTIDE                           
REMARK 900 RELATED ID: 1ZS8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MURINE MHC CLASS                           
REMARK 900  IB MOLECULE M10.5                                                   
REMARK 900 RELATED ID: 1HLA   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN A2 (                       
REMARK 900  HLA-A2, HUMAN LEUCOCYTE ANTIGEN)                                    
REMARK 900 RELATED ID: 1JGD   RELATED DB: PDB                                   
REMARK 900  HLA-B*2709 BOUND TO DECA-PEPTIDE S10R                               
REMARK 900 RELATED ID: 1I1Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (                            
REMARK 900  HLA-A2.1) COMPLEXED WITH BETA 2-                                    
REMARK 900  MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y                        
REMARK 900 RELATED ID: 1VGK   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF CLASS I MAJOR                              
REMARK 900  HISTOCOMPATIBILITYCOMPLEX, H-2KD AT 2.0 A                           
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1AGE   RELATED DB: PDB                                   
REMARK 900  ANTAGONIST HIV-1 GAG PEPTIDES INDUCE                                
REMARK 900  STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG                            
REMARK 900  PEPTIDE (GGKKKYRL - 7R MUTATION)                                    
REMARK 900 RELATED ID: 1UR7   RELATED DB: PDB                                   
REMARK 900  MOLECULAR REFINEMENT OF ANTI-HLA-A2 USING                           
REMARK 900  LIGHT CHAIN SHUFFLING: A STRUCTURAL MODEL                           
REMARK 900  FOR HLA ANTIBODY BINDING                                            
REMARK 900 RELATED ID: 1S9X   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF NY-ESO-1                              
REMARK 900  EPITOPE ANALOGUE,SLLMWITQA, IN COMPLEX WITH                         
REMARK 900  HLA-A2                                                              
REMARK 900 RELATED ID: 1HHG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2X4U   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO HIV-1 PEPTIDE RT468-476                                  
REMARK 900 RELATED ID: 1DUZ   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA                       
REMARK 900  -A 0201) INCOMPLEX WITH A NONAMERIC PEPTIDE                         
REMARK 900   FROM HTLV-1 TAX PROTEIN                                            
REMARK 900 RELATED ID: 1A9E   RELATED DB: PDB                                   
REMARK 900  DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE                         
REMARK 900   BOUND TO HLA-B 3501 DUE TO NONSTANDARD                             
REMARK 900  POSITIONING OF THE C-TERMINUS                                       
REMARK 900 RELATED ID: 2CLR   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA                       
REMARK 900  -A 0201) COMPLEXED WITH A DECAMERIC PEPTIDE                         
REMARK 900   FROM CALRETICULIN                                                  
REMARK 900 RELATED ID: 3HLA   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN A2.                        
REMARK 900  1 (HLA-A2.1 HUMAN LEUCOCYTE ANTIGEN)                                
REMARK 900 RELATED ID: 1M05   RELATED DB: PDB                                   
REMARK 900  HLA B8 IN COMPLEX WITH AN EPSTEIN BARR                              
REMARK 900  VIRUS DETERMINANT                                                   
REMARK 900 RELATED ID: 2X4O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO HIV-1 ENVELOPE PEPTIDE ENV120-                           
REMARK 900  128                                                                 
REMARK 900 RELATED ID: 1TVB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MELANOMA ANTIGEN GP100(                        
REMARK 900  209-217) BOUNDTO HUMAN CLASS I MHC HLA-                             
REMARK 900  A2                                                                  
REMARK 900 RELATED ID: 2V2W   RELATED DB: PDB                                   
REMARK 900  T CELL CROSS-REACTIVITY AND CONFORMATIONAL                          
REMARK 900  CHANGES DURING TCR ENGAGEMENT                                       
REMARK 900 RELATED ID: 1ONQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CD1A IN COMPLEX WITH                           
REMARK 900  A SULFATIDE                                                         
REMARK 900 RELATED ID: 2X4P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO A PHOTOCLEAVABLE PEPTIDE                                 
REMARK 900 RELATED ID: 2VLR   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN                        
REMARK 900   IMMUNODOMINANT T-CELL RECEPTOR ARE                                 
REMARK 900  PROGRAMMED BY ITS VBETA DOMAIN                                      
REMARK 900 RELATED ID: 2BVO   RELATED DB: PDB                                   
REMARK 900  STRUCTURES OF THREE HIV-1 HLA-B5703-                                
REMARK 900  PEPTIDE COMPLEXES AND IDENTIFICATION OF                             
REMARK 900  RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG                       
REMARK 900  -TERM NON-PROGRESSION                                               
REMARK 900 RELATED ID: 1A1N   RELATED DB: PDB                                   
REMARK 900  MHC CLASS I MOLECULE B*3501 COMPLEXED WITH                          
REMARK 900   PEPTIDE VPLRPMTYFROM THE NEF PROTEIN (75-                          
REMARK 900  82) OF HIV1                                                         
REMARK 900 RELATED ID: 1LP9   RELATED DB: PDB                                   
REMARK 900  XENOREACTIVE COMPLEX AHIII 12.2 TCR BOUND                           
REMARK 900  TO P1049/HLA-A2.1                                                   
REMARK 900 RELATED ID: 1ZSD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*3501 PRESENTING                          
REMARK 900  AN 11-MER EBVANTIGEN EPLPQGQLTAY                                    
REMARK 900 RELATED ID: 1M6O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA B*4402 IN COMPLEX                          
REMARK 900   WITH HLADPA*0201 PEPTIDE                                           
REMARK 900 RELATED ID: 1HHK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ZT4   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF HUMAN CD1D WITH                            
REMARK 900  AND WITHOUT ALPHA-GALACTOSYLCERAMIDE                                
REMARK 900 RELATED ID: 1HSB   RELATED DB: PDB                                   
REMARK 900  CLASS I HISTOCOMPATIBILITY ANTIGEN AW68.1 (                         
REMARK 900  LEUCOCYTE ANTIGEN)                                                  
REMARK 900 RELATED ID: 1CE6   RELATED DB: PDB                                   
REMARK 900  MHC CLASS I H-2DB COMPLEXED WITH A                                  
REMARK 900  SENDAI VIRUSNUCLEOPROTEIN PEPTIDE                                   
REMARK 900 RELATED ID: 2XKU   RELATED DB: PDB                                   
REMARK 900  PRION-LIKE CONVERSION DURING AMYLOID FORMATION                      
REMARK 900   AT ATOMIC RESOLUTION                                               
REMARK 900 RELATED ID: 1X7Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A*1101 WITH SARS                           
REMARK 900   NUCLEOCAPSIDPEPTIDE                                                
REMARK 900 RELATED ID: 1PY4   RELATED DB: PDB                                   
REMARK 900  BETA2 MICROGLOBULIN MUTANT H31Y DISPLAYS HINTS                      
REMARK 900   FOR AMYLOIDFORMATIONS                                              
REMARK 900 RELATED ID: 1SYV   RELATED DB: PDB                                   
REMARK 900  HLA-B*4405 COMPLEXED TO THE DOMINANT SELF                           
REMARK 900   LIGAND EEFGRAYGF                                                   
REMARK 900 RELATED ID: 2J8U   RELATED DB: PDB                                   
REMARK 900  LARGE CDR3A LOOP ALTERATION AS A FUNCTION                           
REMARK 900  OF MHC MUTATION.                                                    
REMARK 900 RELATED ID: 2XPG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A MHC CLASS I-PEPTIDE                          
REMARK 900   COMPLEX                                                            
REMARK 900 RELATED ID: 1SYS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA, B*4403, AND                               
REMARK 900  PEPTIDE EEPTVIKKY                                                   
REMARK 900 RELATED ID: 1OGT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED                           
REMARK 900  WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE                         
REMARK 900  1 RECEPTOR (VPAC1) PEPTIDE (RESIDUES 400-408                        
REMARK 900  )                                                                   
REMARK 900 RELATED ID: 2X4T   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO A PEIODATE-CLEAVABLE PEPTIDE                             
REMARK 900 RELATED ID: 1CG9   RELATED DB: PDB                                   
REMARK 900  COMPLEX RECOGNITION OF THE SUPERTYPIC BW6-                          
REMARK 900  DETERMINANT ONHLA-B AND-C MOLECULES BY THE                          
REMARK 900   MONOCLONAL ANTIBODY SFR8-B6                                        
REMARK 900 RELATED ID: 1P7Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A2 BOUND TO LIR-                           
REMARK 900  1, A HOST ANDVIRAL MHC RECEPTOR                                     
REMARK 900 RELATED ID: 1Q94   RELATED DB: PDB                                   
REMARK 900  STRUCTURES OF HLA-A*1101 IN COMPLEX WITH                            
REMARK 900  IMMUNODOMINANTNONAMER AND DECAMER HIV-1                             
REMARK 900  EPITOPES CLEARLY REVEAL THEPRESENCE OF A                            
REMARK 900  MIDDLE ANCHOR RESIDUE                                               
REMARK 900 RELATED ID: 1JNJ   RELATED DB: PDB                                   
REMARK 900  NMR SOLUTION STRUCTURE OF THE HUMAN BETA2-                          
REMARK 900  MICROGLOBULIN                                                       
REMARK 900 RELATED ID: 1AGB   RELATED DB: PDB                                   
REMARK 900  ANTAGONIST HIV-1 GAG PEPTIDES INDUCE                                
REMARK 900  STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG                            
REMARK 900  PEPTIDE (GGRKKYKL - 3R MUTATION)                                    
REMARK 900 RELATED ID: 2D31   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DISULFIDE-LINKED HLA-G                         
REMARK 900   DIMER                                                              
REMARK 900 RELATED ID: 1XZ0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CD1A IN COMPLEX WITH                           
REMARK 900  A SYNTHETICMYCOBACTIN LIPOPEPTIDE                                   
REMARK 900 RELATED ID: 1LDS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MONOMERIC HUMAN BETA-2                         
REMARK 900  -MICROGLOBULIN                                                      
REMARK 900 RELATED ID: 1HHH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TVH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MODIFIED MELANOMA ANTIGEN                      
REMARK 900   GP100(209-T2M) BOUND TO HUMAN CLASS I                              
REMARK 900  MHC HLA-A2                                                          
REMARK 900 RELATED ID: 1XR8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURES OF HLA-B*1501 IN                                 
REMARK 900  COMPLEX WITH PEPTIDESFROM HUMAN UBCH6 AND                           
REMARK 900  EPSTEIN-BARR VIRUS EBNA-3                                           
REMARK 900 RELATED ID: 2BSS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF                       
REMARK 900   THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED                      
REMARK 900   TO HLA-B2705                                                       
REMARK 900 RELATED ID: 1A1M   RELATED DB: PDB                                   
REMARK 900  MHC CLASS I MOLECULE B*5301 COMPLEXED WITH                          
REMARK 900   PEPTIDETYPDINQML FROM GAG PROTEIN OF HIV2                          
REMARK 900 RELATED ID: 1E28   RELATED DB: PDB                                   
REMARK 900  NONSTANDARD PEPTIDE BINDING OF HLA-B*5101                           
REMARK 900  COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2                       
REMARK 900  (TAFTIPSI)                                                          
REMARK 900 RELATED ID: 2BVP   RELATED DB: PDB                                   
REMARK 900  STRUCTURES OF THREE HIV-1 HLA-B5703-                                
REMARK 900  PEPTIDE COMPLEXES AND IDENTIFICATION OF                             
REMARK 900  RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG                       
REMARK 900  -TERM NON-PROGRESSION                                               
REMARK 900 RELATED ID: 2V2X   RELATED DB: PDB                                   
REMARK 900  T CELL CROSS-REACTIVITY AND CONFORMATIONAL                          
REMARK 900  CHANGES DURING TCR ENGAGEMENT.                                      
REMARK 900 RELATED ID: 1XR9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURES OF HLA-B*1501 IN                                 
REMARK 900  COMPLEX WITH PEPTIDESFROM HUMAN UBCH6 AND                           
REMARK 900  EPSTEIN-BARR VIRUS EBNA-3                                           
REMARK 900 RELATED ID: 2GJ6   RELATED DB: PDB                                   
REMARK 900  THE COMPLEX BETWEEN TCR A6 AND HUMAN CLASS                          
REMARK 900   I MHC HLA-A2WITH THE MODIFIED HTLV-1                               
REMARK 900  TAX (Y5K-4-[3-INDOLYL]-BUTYRICACID) PEPTIDE                         
REMARK 900 RELATED ID: 2X4R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO CYTOMEGALOVIRUS (CMV) PP65                               
REMARK 900  EPITOPE                                                             
REMARK 900 RELATED ID: 1QLF   RELATED DB: PDB                                   
REMARK 900  MHC CLASS I H-2DB COMPLEXED WITH                                    
REMARK 900  GLYCOPEPTIDE K3G                                                    
REMARK 900 RELATED ID: 1EFX   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A COMPLEX BETWEEN THE HUMAN                            
REMARK 900  NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A                          
REMARK 900  CLASS I MHC LIGAND HLA-CW3                                          
REMARK 900 RELATED ID: 1TMC   RELATED DB: PDB                                   
REMARK 900  TRUNCATED HUMAN CLASS I HISTOCOMPATIBILITY                          
REMARK 900  ANTIGEN HLA-AW68 COMPLEXED WITH A DECAMERIC                         
REMARK 900   PEPTIDE (EVAPPEYHRK)                                               
REMARK 900 RELATED ID: 2AV1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HTLV-1 TAX PEPTIDE                             
REMARK 900  BOUND TO HUMANCLASS I MHC HLA-A2 WITH                               
REMARK 900  THE E63Q AND K66A MUTATIONS IN THEHEAVY                             
REMARK 900  CHAIN.                                                              
REMARK 900 RELATED ID: 1QSF   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A6-TCR BOUND TO HLA-A2                                 
REMARK 900  COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE                           
REMARK 900  Y8A                                                                 
REMARK 900 RELATED ID: 1KPR   RELATED DB: PDB                                   
REMARK 900  THE HUMAN NON-CLASSICAL MAJOR                                       
REMARK 900  HISTOCOMPATIBILITY COMPLEXMOLECULE HLA-E                            
REMARK 900 RELATED ID: 1DUY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A0201/OCTAMERIC TAX                        
REMARK 900   PEPTIDE COMPLEX                                                    
REMARK 900 RELATED ID: 1JGE   RELATED DB: PDB                                   
REMARK 900  HLA-B*2705 BOUND TO NONA-PEPTIDE M9                                 
REMARK 900 RELATED ID: 2HJL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B5703 AND HIV-1                            
REMARK 900  PEPTIDE                                                             
REMARK 900 RELATED ID: 1QEW   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA                       
REMARK 900  -A 0201)COMPLEX WITH A NONAMERIC PEPTIDE                            
REMARK 900  FROM MELANOMA-ASSOCIATEDANTIGEN 3 (RESIDUES                         
REMARK 900  271-279)                                                            
REMARK 900 RELATED ID: 1W0V   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED                           
REMARK 900  WITH THE SELF-PEPTIDE TIS FROM EGF-                                 
REMARK 900  RESPONSE FACTOR 1                                                   
REMARK 900 RELATED ID: 1K5N   RELATED DB: PDB                                   
REMARK 900  HLA-B*2709 BOUND TO NONA-PEPTIDE M9                                 
REMARK 900 RELATED ID: 1AO7   RELATED DB: PDB                                   
REMARK 900  COMPLEX BETWEEN HUMAN T-CELL RECEPTOR, VIRAL                        
REMARK 900   PEPTIDE (TAX), AND HLA-A 0201                                      
REMARK 900 RELATED ID: 2BNR   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL AND KINETIC BASIS FOR HIGHTENED                          
REMARK 900  IMMUNOGENICITY OF T CELL VACCINES                                   
REMARK 900 RELATED ID: 1XH3   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL RESTRAINTS AND FLEXIBILITY OF                        
REMARK 900  14-MERICPEPTIDES IN COMPLEX WITH HLA-B*                             
REMARK 900  3501                                                                
REMARK 900 RELATED ID: 2BST   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF                       
REMARK 900   THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED                      
REMARK 900   TO HLA-B2705                                                       
REMARK 900 RELATED ID: 1MI5   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF LC13 TCR IN                                
REMARK 900  COMPLEX WITH HLAB8-EBVPEPTIDE COMPLEX                               
REMARK 900 RELATED ID: 2H26   RELATED DB: PDB                                   
REMARK 900  HUMAN CD1B IN COMPLEX WITH ENDOGENOUS                               
REMARK 900  PHOSPHATIDYLCHOLINEAND SPACER                                       
REMARK 900 RELATED ID: 1S9Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF NY-ESO-1                              
REMARK 900  EPITOPE ANALOGUE,SLLMWITQS, IN COMPLEX WITH                         
REMARK 900  HLA-A2                                                              
REMARK 900 RELATED ID: 1A1O   RELATED DB: PDB                                   
REMARK 900  MHC CLASS I MOLECULE B5301 COMPLEXED WITH                           
REMARK 900  PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA                            
REMARK 900  PARASITE P. FALCIPARUM                                              
REMARK 900 RELATED ID: 2A83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED                           
REMARK 900  WITH THE GLUCAGONRECEPTOR (GR) PEPTIDE (                            
REMARK 900  RESIDUES 412-420)                                                   
REMARK 900 RELATED ID: 1AGF   RELATED DB: PDB                                   
REMARK 900  ANTAGONIST HIV-1 GAG PEPTIDES INDUCE                                
REMARK 900  STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG                            
REMARK 900  PEPTIDE (GGKKRYKL - 5R MUTATION)                                    
REMARK 900 RELATED ID: 1OGA   RELATED DB: PDB                                   
REMARK 900  A STRUCTURAL BASIS FOR IMMUNODOMINANT HUMAN                         
REMARK 900  T-CELL RECEPTOR RECOGNITION.                                        
REMARK 900 RELATED ID: 2F8O   RELATED DB: PDB                                   
REMARK 900  A NATIVE TO AMYLOIDOGENIC TRANSITION REGULATED                      
REMARK 900   BY ABACKBONE TRIGGER                                               
REMARK 900 RELATED ID: 2X70   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO A PHOTOCLEAVABLE PEPTIDE                                 
REMARK 900 RELATED ID: 2CII   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-2DB COMPLEXED                            
REMARK 900  WITH A PARTIAL PEPTIDE EPITOPE SUGGESTS AN                          
REMARK 900  MHC CLASS I ASSEMBLY-INTERMEDIATE                                   
REMARK 900 RELATED ID: 1I7R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CLASS I MHC A2 IN                              
REMARK 900  COMPLEX WITH PEPTIDEP1058                                           
REMARK 900 RELATED ID: 1JF1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A2*0201 IN                                 
REMARK 900  COMPLEX WITH ADECAMERIC ALTERED PEPTIDE LIGAND                      
REMARK 900   FROM THE MART-1/MELAN-A                                            
REMARK 900 RELATED ID: 2C7U   RELATED DB: PDB                                   
REMARK 900  CONFLICTING SELECTIVE FORCES AFFECT CD8 T-                          
REMARK 900  CELL RECEPTOR CONTACT SITES IN AN HLA-A2                            
REMARK 900  IMMUNODOMINANT HIV EPITOPE.                                         
REMARK 900 RELATED ID: 1E27   RELATED DB: PDB                                   
REMARK 900  NONSTANDARD PEPTIDE BINDING OF HLA-B*5101                           
REMARK 900  COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM1                       
REMARK 900  (LPPVVAKEI)                                                         
REMARK 900 RELATED ID: 2F74   RELATED DB: PDB                                   
REMARK 900  MURINE MHC CLASS I H-2DB IN COMPLEX WITH                            
REMARK 900   HUMAN B2-MICROGLOBULIN AND LCMV-DERIVED                            
REMARK 900  IMMUNODMINANT PEPTIDE GP33                                          
REMARK 900 RELATED ID: 1W0W   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED                           
REMARK 900  WITH THE SELF-PEPTIDE TIS FROM EGF-                                 
REMARK 900  RESPONSE FACTOR 1                                                   
REMARK 900 RELATED ID: 1GZQ   RELATED DB: PDB                                   
REMARK 900  CD1B IN COMPLEX WITH PHOPHATIDYLINOSITOL                            
REMARK 900 RELATED ID: 1UXS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED                           
REMARK 900  WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE                          
REMARK 900   (LMP2)OF EPSTEIN-BARR VIRUS                                        
REMARK 900 RELATED ID: 1AKJ   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE HUMAN MHC CLASS I                                    
REMARK 900  GLYCOPROTEIN HLA-A2 ANDTHE T CELL CORECEPTOR                        
REMARK 900   CD8                                                                
REMARK 900 RELATED ID: 2HJK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B5703 AND HIV-1                            
REMARK 900  PEPTIDE                                                             
REMARK 900 RELATED ID: 2VB5   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF W60G MUTANT OF HUMAN                          
REMARK 900  BETA2-MICROGLOBULIN                                                 
REMARK 900 RELATED ID: 1AGD   RELATED DB: PDB                                   
REMARK 900  ANTAGONIST HIV-1 GAG PEPTIDES INDUCE                                
REMARK 900  STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG                            
REMARK 900  PEPTIDE (GGKKKYKL - INDEX PEPTIDE)                                  
REMARK 900 RELATED ID: 2X4N   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO RESIDUAL FRAGMENTS OF A                                  
REMARK 900  PHOTOCLEAVABLE PEPTIDE THAT IS CLEAVED UPON                         
REMARK 900  UV-LIGHT TREATMENT                                                  
REMARK 900 RELATED ID: 1R3H   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF T10                                            
REMARK 900 RELATED ID: 1EEY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE DETERMINATION OF HLA A2                           
REMARK 900  COMPLEXED TOPEPTIDE GP2 WITH THE SUBSTITUTION                       
REMARK 900   (I2L/V5L/L9V)                                                      
REMARK 900 RELATED ID: 1I7T   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CLASS I MHC A2 IN                              
REMARK 900  COMPLEX WITH PEPTIDEP1049-5V                                        
REMARK 900 RELATED ID: 1YDP   RELATED DB: PDB                                   
REMARK 900  1.9A CRYSTAL STRUCTURE OF HLA-G                                     
REMARK 900 RELATED ID: 1I4F   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A*0201/MAGE-A4-                            
REMARK 900  PEPTIDE COMPLEX                                                     
REMARK 900 RELATED ID: 2VLL   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN                        
REMARK 900   IMMUNODOMINANT T-CELL RECEPTOR ARE                                 
REMARK 900  PROGRAMMED BY ITS VBETA DOMAIN                                      
REMARK 900 RELATED ID: 2BSR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF                       
REMARK 900   THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED                      
REMARK 900   TO HLA-B2705                                                       
REMARK 900 RELATED ID: 2VLJ   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURAL DYNAMICS AND ENERGETICS OF AN                        
REMARK 900   IMMUNODOMINANT T-CELL RECEPTOR ARE                                 
REMARK 900  PROGRAMMED BY ITS VBETA DOMAIN                                      
REMARK 900 RELATED ID: 1B0G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (                            
REMARK 900  HLA-A2.1) COMPLEXED WITH BETA 2-                                    
REMARK 900  MICROGLOBULIN AND HUMAN PEPTIDE P1049                               
REMARK 900 RELATED ID: 2X4S   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.                            
REMARK 900  1 BOUND TO A PEPTIDE REPRESENTING THE                               
REMARK 900  EPITOPE OF THE H5N1 (AVIAN FLU)                                     
REMARK 900  NUCLEOPROTEIN                                                       
REMARK 900 RELATED ID: 1B0R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-A0201 COMPLEXED                            
REMARK 900  WITH A PEPTIDE WITH THE CARBOXYL-TERMINAL                           
REMARK 900  GROUP SUBSTITUTED BY A METHYL GROUP                                 
REMARK 900 RELATED ID: 1OF2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED                           
REMARK 900  WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE                         
REMARK 900  1 RECEPTOR (VPAC1) PEPTIDE (RESIDUES 400-408                        
REMARK 900  )                                                                   
REMARK 900 RELATED ID: 1HHI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1QSE   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN A6-TCR BOUND TO HLA-                             
REMARK 900  A2 COMPLEXED WITH ALTERED HTLV-1 TAX                                
REMARK 900  PEPTIDE V7R                                                         
REMARK 900 RELATED ID: 1A9B   RELATED DB: PDB                                   
REMARK 900  DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE                         
REMARK 900   BOUND TO HLA-B 3501 DUE TO NONSTANDARD                             
REMARK 900  POSITIONING OF THE C-TERMINUS                                       
REMARK 900 RELATED ID: 2AXG   RELATED DB: PDB                                   
REMARK 900  THE IMMUNOGENICITY OF A VIRAL CYTOTOXIC T                           
REMARK 900  CELL EPITOPE ISCONTROLLED BY ITS MHC-BOUND                          
REMARK 900  CONFORMATION                                                        
REMARK 900 RELATED ID: 2BVQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURES OF THREE HIV-1 HLA-B5703-                                
REMARK 900  PEPTIDE COMPLEXES AND IDENTIFICATION OF                             
REMARK 900  RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG                       
REMARK 900  -TERM NON-PROGRESSION                                               
REMARK 900 RELATED ID: 1AGC   RELATED DB: PDB                                   
REMARK 900  ANTAGONIST HIV-1 GAG PEPTIDES INDUCE                                
REMARK 900  STRUCTURAL CHANGES IN HLA B8 - HIV-1 GAG                            
REMARK 900  PEPTIDE (GGKKKYQL - 7Q MUTATION)                                    
REMARK 900 RELATED ID: 1QVO   RELATED DB: PDB                                   
REMARK 900  STRUCTURES OF HLA-A*1101 IN COMPLEX WITH                            
REMARK 900  IMMUNODOMINANTNONAMER AND DECAMER HIV-1                             
REMARK 900  EPITOPES CLEARLY REVEAL THEPRESENCE OF A                            
REMARK 900  MIDDLE ANCHOR RESIDUE                                               
REMARK 900 RELATED ID: 1HHJ   RELATED DB: PDB                                   
REMARK 900  HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA                       
REMARK 900  -A 0201) COMPLEX WITH A NONAMERIC PEPTIDE                           
REMARK 900  FROM HIV-1 REVERSE TRANSCRIPTASE (RESIDUES                          
REMARK 900  309-317)                                                            
REMARK 900 RELATED ID: 1S9W   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF NY-ESO-1                              
REMARK 900  EPITOPE, SLLMWITQC,IN COMPLEX WITH HLA-A2                           
REMARK 900 RELATED ID: 1KTL   RELATED DB: PDB                                   
REMARK 900  THE HUMAN NON-CLASSICAL MAJOR                                       
REMARK 900  HISTOCOMPATIBILITY COMPLEXMOLECULE HLA-E                            
REMARK 900 RELATED ID: 1A6Z   RELATED DB: PDB                                   
REMARK 900  HFE (HUMAN) HEMOCHROMATOSIS PROTEIN                                 
REMARK 900 RELATED ID: 2CIK   RELATED DB: PDB                                   
REMARK 900  INSIGHTS INTO CROSSREACTIVITY IN HUMAN                              
REMARK 900  ALLORECOGNITION: THE STRUCTURE OF HLA-B35011                        
REMARK 900  PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME                       
REMARK 900   P450.                                                              
REMARK 900 RELATED ID: 1I1F   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (                            
REMARK 900  HLA-A2.1) COMPLEXED WITH BETA 2-                                    
REMARK 900  MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y                        
REMARK 900 RELATED ID: 2UWE   RELATED DB: PDB                                   
REMARK 900  LARGE CDR3A LOOP ALTERATION AS A FUNCTION                           
REMARK 900  OF MHC MUTATION                                                     
REMARK 900 RELATED ID: 2AV7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HTLV-1 TAX PEPTIDE                             
REMARK 900  BOUND TO HUMANCLASS I MHC HLA-A2 WITH                               
REMARK 900  THE K66A MUTATION IN THE HEAVYCHAIN.                                
DBREF  2X89 A    1   128  PDB    2X89     2X89             1    128             
DBREF  2X89 B    1   128  PDB    2X89     2X89             1    128             
DBREF  2X89 C    1   128  PDB    2X89     2X89             1    128             
DBREF  2X89 D    7    99  UNP    P61769   B2MG_HUMAN      27    119             
DBREF  2X89 E    7    99  UNP    P61769   B2MG_HUMAN      27    119             
DBREF  2X89 F    7    99  UNP    P61769   B2MG_HUMAN      27    119             
DBREF  2X89 G    7    99  UNP    P61769   B2MG_HUMAN      27    119             
SEQADV 2X89 MET D    6  UNP  P61769              EXPRESSION TAG                 
SEQADV 2X89 MET E    6  UNP  P61769              EXPRESSION TAG                 
SEQADV 2X89 MET F    6  UNP  P61769              EXPRESSION TAG                 
SEQADV 2X89 MET G    6  UNP  P61769              EXPRESSION TAG                 
SEQRES   1 A  128  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 A  128  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 A  128  TYR THR ASP SER ARG TYR CYS MET ALA TRP PHE ARG GLN          
SEQRES   4 A  128  ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ARG ILE ASN          
SEQRES   5 A  128  SER GLY ARG ASP ILE THR TYR TYR ALA ASP SER VAL LYS          
SEQRES   6 A  128  GLY ARG PHE THR PHE SER GLN ASP ASN ALA LYS ASN THR          
SEQRES   7 A  128  VAL TYR LEU GLN MET ASP SER LEU GLU PRO GLU ASP THR          
SEQRES   8 A  128  ALA THR TYR TYR CYS ALA THR ASP ILE PRO LEU ARG CYS          
SEQRES   9 A  128  ARG ASP ILE VAL ALA LYS GLY GLY ASP GLY PHE ARG TYR          
SEQRES  10 A  128  TRP GLY GLN GLY THR GLN VAL THR VAL SER SER                  
SEQRES   1 B  128  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 B  128  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 B  128  TYR THR ASP SER ARG TYR CYS MET ALA TRP PHE ARG GLN          
SEQRES   4 B  128  ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ARG ILE ASN          
SEQRES   5 B  128  SER GLY ARG ASP ILE THR TYR TYR ALA ASP SER VAL LYS          
SEQRES   6 B  128  GLY ARG PHE THR PHE SER GLN ASP ASN ALA LYS ASN THR          
SEQRES   7 B  128  VAL TYR LEU GLN MET ASP SER LEU GLU PRO GLU ASP THR          
SEQRES   8 B  128  ALA THR TYR TYR CYS ALA THR ASP ILE PRO LEU ARG CYS          
SEQRES   9 B  128  ARG ASP ILE VAL ALA LYS GLY GLY ASP GLY PHE ARG TYR          
SEQRES  10 B  128  TRP GLY GLN GLY THR GLN VAL THR VAL SER SER                  
SEQRES   1 C  128  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY SER VAL GLN          
SEQRES   2 C  128  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 C  128  TYR THR ASP SER ARG TYR CYS MET ALA TRP PHE ARG GLN          
SEQRES   4 C  128  ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ARG ILE ASN          
SEQRES   5 C  128  SER GLY ARG ASP ILE THR TYR TYR ALA ASP SER VAL LYS          
SEQRES   6 C  128  GLY ARG PHE THR PHE SER GLN ASP ASN ALA LYS ASN THR          
SEQRES   7 C  128  VAL TYR LEU GLN MET ASP SER LEU GLU PRO GLU ASP THR          
SEQRES   8 C  128  ALA THR TYR TYR CYS ALA THR ASP ILE PRO LEU ARG CYS          
SEQRES   9 C  128  ARG ASP ILE VAL ALA LYS GLY GLY ASP GLY PHE ARG TYR          
SEQRES  10 C  128  TRP GLY GLN GLY THR GLN VAL THR VAL SER SER                  
SEQRES   1 D   94  MET ILE GLN VAL TYR SER ARG HIS PRO ALA GLU ASN GLY          
SEQRES   2 D   94  LYS SER ASN PHE LEU ASN CYS TYR VAL SER GLY PHE HIS          
SEQRES   3 D   94  PRO SER ASP ILE GLU VAL ASP LEU LEU LYS ASN GLY GLU          
SEQRES   4 D   94  ARG ILE GLU LYS VAL GLU HIS SER ASP LEU SER PHE SER          
SEQRES   5 D   94  LYS ASP TRP SER PHE TYR LEU LEU TYR TYR THR GLU PHE          
SEQRES   6 D   94  THR PRO THR GLU LYS ASP GLU TYR ALA CYS ARG VAL ASN          
SEQRES   7 D   94  HIS VAL THR LEU SER GLN PRO LYS ILE VAL LYS TRP ASP          
SEQRES   8 D   94  ARG ASP MET                                                  
SEQRES   1 E   94  MET ILE GLN VAL TYR SER ARG HIS PRO ALA GLU ASN GLY          
SEQRES   2 E   94  LYS SER ASN PHE LEU ASN CYS TYR VAL SER GLY PHE HIS          
SEQRES   3 E   94  PRO SER ASP ILE GLU VAL ASP LEU LEU LYS ASN GLY GLU          
SEQRES   4 E   94  ARG ILE GLU LYS VAL GLU HIS SER ASP LEU SER PHE SER          
SEQRES   5 E   94  LYS ASP TRP SER PHE TYR LEU LEU TYR TYR THR GLU PHE          
SEQRES   6 E   94  THR PRO THR GLU LYS ASP GLU TYR ALA CYS ARG VAL ASN          
SEQRES   7 E   94  HIS VAL THR LEU SER GLN PRO LYS ILE VAL LYS TRP ASP          
SEQRES   8 E   94  ARG ASP MET                                                  
SEQRES   1 F   94  MET ILE GLN VAL TYR SER ARG HIS PRO ALA GLU ASN GLY          
SEQRES   2 F   94  LYS SER ASN PHE LEU ASN CYS TYR VAL SER GLY PHE HIS          
SEQRES   3 F   94  PRO SER ASP ILE GLU VAL ASP LEU LEU LYS ASN GLY GLU          
SEQRES   4 F   94  ARG ILE GLU LYS VAL GLU HIS SER ASP LEU SER PHE SER          
SEQRES   5 F   94  LYS ASP TRP SER PHE TYR LEU LEU TYR TYR THR GLU PHE          
SEQRES   6 F   94  THR PRO THR GLU LYS ASP GLU TYR ALA CYS ARG VAL ASN          
SEQRES   7 F   94  HIS VAL THR LEU SER GLN PRO LYS ILE VAL LYS TRP ASP          
SEQRES   8 F   94  ARG ASP MET                                                  
SEQRES   1 G   94  MET ILE GLN VAL TYR SER ARG HIS PRO ALA GLU ASN GLY          
SEQRES   2 G   94  LYS SER ASN PHE LEU ASN CYS TYR VAL SER GLY PHE HIS          
SEQRES   3 G   94  PRO SER ASP ILE GLU VAL ASP LEU LEU LYS ASN GLY GLU          
SEQRES   4 G   94  ARG ILE GLU LYS VAL GLU HIS SER ASP LEU SER PHE SER          
SEQRES   5 G   94  LYS ASP TRP SER PHE TYR LEU LEU TYR TYR THR GLU PHE          
SEQRES   6 G   94  THR PRO THR GLU LYS ASP GLU TYR ALA CYS ARG VAL ASN          
SEQRES   7 G   94  HIS VAL THR LEU SER GLN PRO LYS ILE VAL LYS TRP ASP          
SEQRES   8 G   94  ARG ASP MET                                                  
FORMUL   8  HOH   *295(H2 O)                                                    
HELIX    1   1 TYR A   27  ARG A   31  5                                   5    
HELIX    2   2 GLU A   87  THR A   91  5                                   5    
HELIX    3   3 ILE A  100  ARG A  105  1                                   6    
HELIX    4   4 TYR B   27  ARG B   31  5                                   5    
HELIX    5   5 GLU B   87  THR B   91  5                                   5    
HELIX    6   6 ILE B  100  ARG B  105  1                                   6    
HELIX    7   7 TYR C   27  ARG C   31  5                                   5    
HELIX    8   8 GLU C   87  THR C   91  5                                   5    
HELIX    9   9 ILE C  100  ARG C  105  1                                   6    
HELIX   10  10 HIS D   31  SER D   33  5                                   3    
HELIX   11  11 HIS E   31  SER E   33  5                                   3    
HELIX   12  12 HIS F   31  SER F   33  5                                   3    
SHEET    1  AA 4 GLN A   3  SER A   7  0                                        
SHEET    2  AA 4 LEU A  18  SER A  25 -1  O  SER A  21   N  SER A   7           
SHEET    3  AA 4 VAL A  79  MET A  83 -1  O  VAL A  79   N  CYS A  22           
SHEET    4  AA 4 PHE A  68  SER A  71 -1  O  THR A  69   N  GLN A  82           
SHEET    1  AB 4 SER A  11  GLN A  13  0                                        
SHEET    2  AB 4 THR A 122  SER A 127  1  O  THR A 125   N  VAL A  12           
SHEET    3  AB 4 ALA A  92  ASP A  99 -1  O  ALA A  92   N  VAL A 124           
SHEET    4  AB 4 TYR A 117  TRP A 118 -1  O  TYR A 117   N  THR A  98           
SHEET    1  AC 6 SER A  11  GLN A  13  0                                        
SHEET    2  AC 6 THR A 122  SER A 127  1  O  THR A 125   N  VAL A  12           
SHEET    3  AC 6 ALA A  92  ASP A  99 -1  O  ALA A  92   N  VAL A 124           
SHEET    4  AC 6 CYS A  33  GLN A  39 -1  O  CYS A  33   N  ASP A  99           
SHEET    5  AC 6 GLU A  46  ILE A  51 -1  O  GLU A  46   N  ARG A  38           
SHEET    6  AC 6 THR A  58  TYR A  60 -1  O  TYR A  59   N  ARG A  50           
SHEET    1  AD 2 TYR A 117  TRP A 118  0                                        
SHEET    2  AD 2 ALA A  92  ASP A  99 -1  O  THR A  98   N  TYR A 117           
SHEET    1  BA 4 GLN B   3  SER B   7  0                                        
SHEET    2  BA 4 LEU B  18  SER B  25 -1  O  SER B  21   N  SER B   7           
SHEET    3  BA 4 VAL B  79  MET B  83 -1  O  VAL B  79   N  CYS B  22           
SHEET    4  BA 4 PHE B  68  GLN B  72 -1  O  THR B  69   N  GLN B  82           
SHEET    1  BB 4 SER B  11  GLN B  13  0                                        
SHEET    2  BB 4 THR B 122  SER B 127  1  O  THR B 125   N  VAL B  12           
SHEET    3  BB 4 ALA B  92  ASP B  99 -1  O  ALA B  92   N  VAL B 124           
SHEET    4  BB 4 TYR B 117  TRP B 118 -1  O  TYR B 117   N  THR B  98           
SHEET    1  BC 6 SER B  11  GLN B  13  0                                        
SHEET    2  BC 6 THR B 122  SER B 127  1  O  THR B 125   N  VAL B  12           
SHEET    3  BC 6 ALA B  92  ASP B  99 -1  O  ALA B  92   N  VAL B 124           
SHEET    4  BC 6 CYS B  33  GLN B  39 -1  O  CYS B  33   N  ASP B  99           
SHEET    5  BC 6 GLU B  46  ILE B  51 -1  O  GLU B  46   N  ARG B  38           
SHEET    6  BC 6 THR B  58  TYR B  60 -1  O  TYR B  59   N  ARG B  50           
SHEET    1  BD 2 TYR B 117  TRP B 118  0                                        
SHEET    2  BD 2 ALA B  92  ASP B  99 -1  O  THR B  98   N  TYR B 117           
SHEET    1  CA 4 GLN C   3  SER C   7  0                                        
SHEET    2  CA 4 LEU C  18  SER C  25 -1  O  SER C  21   N  SER C   7           
SHEET    3  CA 4 VAL C  79  MET C  83 -1  O  VAL C  79   N  CYS C  22           
SHEET    4  CA 4 PHE C  68  SER C  71 -1  O  THR C  69   N  GLN C  82           
SHEET    1  CB 4 GLY C  10  GLN C  13  0                                        
SHEET    2  CB 4 THR C 122  SER C 127  1  O  GLN C 123   N  GLY C  10           
SHEET    3  CB 4 ALA C  92  ASP C  99 -1  O  ALA C  92   N  VAL C 124           
SHEET    4  CB 4 TYR C 117  TRP C 118 -1  O  TYR C 117   N  THR C  98           
SHEET    1  CC 6 GLY C  10  GLN C  13  0                                        
SHEET    2  CC 6 THR C 122  SER C 127  1  O  GLN C 123   N  GLY C  10           
SHEET    3  CC 6 ALA C  92  ASP C  99 -1  O  ALA C  92   N  VAL C 124           
SHEET    4  CC 6 CYS C  33  GLN C  39 -1  O  CYS C  33   N  ASP C  99           
SHEET    5  CC 6 ARG C  45  ILE C  51 -1  O  GLU C  46   N  ARG C  38           
SHEET    6  CC 6 THR C  58  TYR C  60 -1  O  TYR C  59   N  ARG C  50           
SHEET    1  CD 2 TYR C 117  TRP C 118  0                                        
SHEET    2  CD 2 ALA C  92  ASP C  99 -1  O  THR C  98   N  TYR C 117           
SHEET    1  DA 4 ILE D   7  SER D  11  0                                        
SHEET    2  DA 4 ASN D  21  SER D  28 -1  O  ASN D  24   N  TYR D  10           
SHEET    3  DA 4 PHE D  62  PHE D  70 -1  O  LEU D  64   N  VAL D  27           
SHEET    4  DA 4 SER D  55  PHE D  56  1  O  SER D  55   N  TYR D  63           
SHEET    1  DB 4 ILE D   7  SER D  11  0                                        
SHEET    2  DB 4 ASN D  21  SER D  28 -1  O  ASN D  24   N  TYR D  10           
SHEET    3  DB 4 PHE D  62  PHE D  70 -1  O  LEU D  64   N  VAL D  27           
SHEET    4  DB 4 GLU D  50  HIS D  51 -1  O  GLU D  50   N  TYR D  67           
SHEET    1  DC 2 SER D  55  PHE D  56  0                                        
SHEET    2  DC 2 PHE D  62  PHE D  70  1  O  TYR D  63   N  SER D  55           
SHEET    1  DD 6 GLU D  44  ARG D  45  0                                        
SHEET    2  DD 6 ILE D  35  LYS D  41 -1  O  LYS D  41   N  GLU D  44           
SHEET    3  DD 6 TYR D  78  LYS D  94 -1  O  ALA D  79   N  LEU D  40           
SHEET    4  DD 6 TYR E  78  LYS E  94 -1  O  CYS E  80   N  VAL D  93           
SHEET    5  DD 6 ILE E  35  LYS E  41 -1  O  GLU E  36   N  ASN E  83           
SHEET    6  DD 6 GLU E  44  ARG E  45 -1  O  GLU E  44   N  LYS E  41           
SHEET    1  EA 4 ILE E   7  SER E  11  0                                        
SHEET    2  EA 4 ASN E  21  SER E  28 -1  O  ASN E  24   N  TYR E  10           
SHEET    3  EA 4 TYR E  63  PHE E  70 -1  O  LEU E  64   N  VAL E  27           
SHEET    4  EA 4 GLU E  50  ASP E  53 -1  O  GLU E  50   N  TYR E  67           
SHEET    1  FA 4 ILE F   7  SER F  11  0                                        
SHEET    2  FA 4 ASN F  21  SER F  28 -1  O  ASN F  24   N  TYR F  10           
SHEET    3  FA 4 TYR F  63  PHE F  70 -1  O  LEU F  64   N  VAL F  27           
SHEET    4  FA 4 GLU F  50  ASP F  53 -1  O  GLU F  50   N  TYR F  67           
SHEET    1  FB 6 GLU F  44  ARG F  45  0                                        
SHEET    2  FB 6 ILE F  35  LYS F  41 -1  O  LYS F  41   N  GLU F  44           
SHEET    3  FB 6 TYR F  78  LYS F  94 -1  O  ALA F  79   N  LEU F  40           
SHEET    4  FB 6 TYR G  78  LYS G  94 -1  O  CYS G  80   N  VAL F  93           
SHEET    5  FB 6 ILE G  35  LYS G  41 -1  O  GLU G  36   N  ASN G  83           
SHEET    6  FB 6 GLU G  44  ARG G  45 -1  O  GLU G  44   N  LYS G  41           
SHEET    1  GA 4 ILE G   7  SER G  11  0                                        
SHEET    2  GA 4 ASN G  21  SER G  28 -1  O  ASN G  24   N  TYR G  10           
SHEET    3  GA 4 TYR G  63  PHE G  70 -1  O  LEU G  64   N  VAL G  27           
SHEET    4  GA 4 GLU G  50  HIS G  51 -1  O  GLU G  50   N  TYR G  67           
SSBOND   1 CYS A   22    CYS A   96                          1555   1555  2.00  
SSBOND   2 CYS A   33    CYS A  104                          1555   1555  2.03  
SSBOND   3 CYS B   22    CYS B   96                          1555   1555  2.02  
SSBOND   4 CYS B   33    CYS B  104                          1555   1555  2.10  
SSBOND   5 CYS C   22    CYS C   96                          1555   1555  1.99  
SSBOND   6 CYS C   33    CYS C  104                          1555   1555  2.03  
SSBOND   7 CYS D   25    CYS D   80                          1555   1555  2.00  
SSBOND   8 CYS E   25    CYS E   80                          1555   1555  1.95  
SSBOND   9 CYS F   25    CYS F   80                          1555   1555  1.96  
SSBOND  10 CYS G   25    CYS G   80                          1555   1555  1.99  
LINK         O   HIS G  31                 CB  ASP G  34     1555   1555  1.57  
CISPEP   1 GLY B    8    GLY B    9          0        15.34                     
CISPEP   2 ASN B   74    ALA B   75          0         3.82                     
CISPEP   3 ASN C   74    ALA C   75          0         5.34                     
CISPEP   4 ALA C   75    LYS C   76          0        16.84                     
CISPEP   5 TRP F   60    SER F   61          0       -14.41                     
CRYST1   77.490  100.864   83.743  90.00 106.43  90.00 P 1 21 1      8          
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      0.012905  0.000000  0.003805        0.00000                         
SCALE2      0.000000  0.009914  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012450        0.00000                         
ATOM    197  N   SER A  30     -65.287  22.567 -10.693  1.00 65.54           N  
ATOM    198  CA  SER A  30     -65.759  21.922  -9.459  1.00 64.56           C  
ATOM    199  C   SER A  30     -64.668  21.413  -8.481  1.00 63.62           C  
ATOM    200  O   SER A  30     -64.789  20.314  -7.950  1.00 63.56           O  
ATOM    201  CB  SER A  30     -66.773  20.810  -9.774  1.00 64.16           C  
ATOM    202  OG  SER A  30     -67.796  21.353 -10.607  1.00 65.28           O  
ATOM    203  N   ARG A  31     -63.654  22.235  -8.206  1.00 61.73           N  
ATOM    204  CA  ARG A  31     -62.533  21.828  -7.336  1.00 58.93           C  
ATOM    205  C   ARG A  31     -62.493  22.613  -6.050  1.00 56.98           C  
ATOM    206  O   ARG A  31     -62.350  23.832  -6.054  1.00 54.55           O  
ATOM    207  CB  ARG A  31     -61.185  22.048  -8.051  1.00 60.97           C  
ATOM    208  CG  ARG A  31     -60.302  20.813  -8.035  1.00 65.51           C  
ATOM    209  CD  ARG A  31     -60.821  19.844  -9.071  1.00 74.98           C  
ATOM    210  NE  ARG A  31     -60.472  18.489  -8.714  1.00 84.87           N  
ATOM    211  CZ  ARG A  31     -59.589  17.743  -9.368  1.00 87.78           C  
ATOM    212  NH1 ARG A  31     -58.977  18.211 -10.449  1.00 89.93           N  
ATOM    213  NH2 ARG A  31     -59.333  16.515  -8.940  1.00 91.11           N  
ATOM    214  N   TYR A  32     -62.571  21.903  -4.933  1.00 54.34           N  
ATOM    215  CA  TYR A  32     -62.664  22.525  -3.661  1.00 53.65           C  
ATOM    216  C   TYR A  32     -62.511  21.494  -2.591  1.00 54.88           C  
ATOM    217  O   TYR A  32     -63.039  20.352  -2.710  1.00 54.37           O  
ATOM    218  CB  TYR A  32     -64.006  23.265  -3.486  1.00 54.10           C  
ATOM    219  CG  TYR A  32     -65.285  22.453  -3.708  1.00 52.76           C  
ATOM    220  CD1 TYR A  32     -65.936  21.841  -2.637  1.00 52.05           C  
ATOM    221  CD2 TYR A  32     -65.791  22.249  -4.981  1.00 50.24           C  
ATOM    222  CE1 TYR A  32     -67.131  21.087  -2.813  1.00 52.77           C  
ATOM    223  CE2 TYR A  32     -67.020  21.471  -5.182  1.00 50.15           C  
ATOM    224  CZ  TYR A  32     -67.671  20.942  -4.087  1.00 50.44           C  
ATOM    225  OH  TYR A  32     -68.815  20.193  -4.215  1.00 54.73           O  
ATOM    226  N   CYS A  33     -61.774  21.874  -1.548  1.00 54.65           N  
ATOM    227  CA  CYS A  33     -61.739  21.071  -0.394  1.00 55.51           C  
ATOM    228  C   CYS A  33     -63.064  21.202   0.433  1.00 56.15           C  
ATOM    229  O   CYS A  33     -63.878  22.105   0.211  1.00 54.02           O  
ATOM    230  CB  CYS A  33     -60.486  21.328   0.477  1.00 55.89           C  
ATOM    231  SG  CYS A  33     -60.420  22.892   1.437  1.00 60.20           S  
ATOM    232  N   MET A  34     -63.240  20.309   1.414  1.00 57.30           N  
ATOM    233  CA  MET A  34     -64.500  20.302   2.186  1.00 60.54           C  
ATOM    234  C   MET A  34     -64.178  19.905   3.609  1.00 59.44           C  
ATOM    235  O   MET A  34     -63.337  19.097   3.841  1.00 60.34           O  
ATOM    236  CB  MET A  34     -65.498  19.313   1.571  1.00 58.34           C  
ATOM    237  CG  MET A  34     -66.789  19.128   2.387  1.00 62.35           C  
ATOM    238  SD  MET A  34     -67.876  18.056   1.492  1.00 66.93           S  
ATOM    239  CE  MET A  34     -67.029  16.588   1.494  1.00 74.05           C  
ATOM    240  N   ALA A  35     -64.872  20.512   4.561  1.00 60.73           N  
ATOM    241  CA  ALA A  35     -64.620  20.279   5.987  1.00 59.46           C  
ATOM    242  C   ALA A  35     -65.990  20.327   6.644  1.00 59.27           C  
ATOM    243  O   ALA A  35     -66.885  21.096   6.203  1.00 57.81           O  
ATOM    244  CB  ALA A  35     -63.731  21.337   6.574  1.00 57.73           C  
ATOM    245  N   TRP A  36     -66.120  19.504   7.697  1.00 57.61           N  
ATOM    246  CA  TRP A  36     -67.260  19.512   8.607  1.00 58.19           C  
ATOM    247  C   TRP A  36     -66.791  19.915   9.957  1.00 57.77           C  
ATOM    248  O   TRP A  36     -65.699  19.515  10.383  1.00 57.81           O  
ATOM    249  CB  TRP A  36     -67.913  18.121   8.734  1.00 59.07           C  
ATOM    250  CG  TRP A  36     -68.710  17.733   7.522  1.00 60.08           C  
ATOM    251  CD1 TRP A  36     -68.296  16.972   6.438  1.00 58.02           C  
ATOM    252  CD2 TRP A  36     -70.076  18.047   7.298  1.00 56.06           C  
ATOM    253  NE1 TRP A  36     -69.328  16.825   5.555  1.00 54.87           N  
ATOM    254  CE2 TRP A  36     -70.451  17.421   6.088  1.00 58.97           C  
ATOM    255  CE3 TRP A  36     -71.035  18.784   8.026  1.00 56.43           C  
ATOM    256  CZ2 TRP A  36     -71.730  17.554   5.554  1.00 56.98           C  
ATOM    257  CZ3 TRP A  36     -72.272  18.894   7.521  1.00 57.87           C  
ATOM    258  CH2 TRP A  36     -72.624  18.291   6.275  1.00 57.35           C  
ATOM    259  N   PHE A  37     -67.672  20.693  10.602  1.00 57.79           N  
ATOM    260  CA  PHE A  37     -67.569  21.305  11.921  1.00 57.06           C  
ATOM    261  C   PHE A  37     -68.926  21.016  12.590  1.00 57.19           C  
ATOM    262  O   PHE A  37     -69.931  20.745  11.918  1.00 56.83           O  
ATOM    263  CB  PHE A  37     -67.373  22.826  11.820  1.00 56.84           C  
ATOM    264  CG  PHE A  37     -66.019  23.223  11.310  1.00 58.29           C  
ATOM    265  CD1 PHE A  37     -64.993  23.542  12.207  1.00 58.66           C  
ATOM    266  CD2 PHE A  37     -65.744  23.247   9.914  1.00 58.11           C  
ATOM    267  CE1 PHE A  37     -63.697  23.820  11.746  1.00 59.95           C  
ATOM    268  CE2 PHE A  37     -64.447  23.583   9.448  1.00 59.55           C  
ATOM    269  CZ  PHE A  37     -63.435  23.827  10.355  1.00 58.90           C  
ATOM    270  N   ARG A  38     -68.949  21.081  13.899  1.00 55.67           N  
ATOM    271  CA  ARG A  38     -70.180  21.050  14.593  1.00 57.01           C  
ATOM    272  C   ARG A  38     -70.087  21.889  15.830  1.00 56.66           C  
ATOM    273  O   ARG A  38     -69.006  22.144  16.364  1.00 58.17           O  
ATOM    274  CB  ARG A  38     -70.555  19.612  15.009  1.00 55.20           C  
ATOM    275  CG  ARG A  38     -69.645  19.067  16.064  1.00 55.86           C  
ATOM    276  CD  ARG A  38     -69.783  17.541  16.201  1.00 52.24           C  
ATOM    277  NE  ARG A  38     -68.749  16.999  17.091  1.00 58.02           N  
ATOM    278  CZ  ARG A  38     -68.664  15.692  17.426  1.00 57.51           C  
ATOM    279  NH1 ARG A  38     -69.527  14.877  16.944  1.00 50.03           N  
ATOM    280  NH2 ARG A  38     -67.734  15.199  18.273  1.00 57.26           N  
ATOM    281  N   GLN A  39     -71.252  22.242  16.313  1.00 55.94           N  
ATOM    282  CA  GLN A  39     -71.364  23.065  17.440  1.00 58.47           C  
ATOM    283  C   GLN A  39     -72.617  22.769  18.228  1.00 58.34           C  
ATOM    284  O   GLN A  39     -73.730  22.864  17.707  1.00 59.29           O  
ATOM    285  CB  GLN A  39     -71.384  24.518  16.985  1.00 57.06           C  
ATOM    286  CG  GLN A  39     -71.700  25.423  18.125  1.00 60.41           C  
ATOM    287  CD  GLN A  39     -71.304  26.812  17.806  1.00 61.86           C  
ATOM    288  OE1 GLN A  39     -71.551  27.286  16.704  1.00 62.98           O  
ATOM    289  NE2 GLN A  39     -70.620  27.463  18.733  1.00 61.67           N  
ATOM    290  N   ALA A  40     -72.413  22.436  19.493  1.00 60.30           N  
ATOM    291  CA  ALA A  40     -73.471  22.204  20.444  1.00 60.96           C  
ATOM    292  C   ALA A  40     -73.916  23.517  21.081  1.00 61.82           C  
ATOM    293  O   ALA A  40     -73.120  24.390  21.271  1.00 62.59           O  
ATOM    294  CB  ALA A  40     -72.942  21.260  21.488  1.00 62.32           C  
ATOM    295  N   PRO A  41     -75.214  23.669  21.416  1.00 63.16           N  
ATOM    296  CA  PRO A  41     -75.689  24.876  22.112  1.00 63.32           C  
ATOM    297  C   PRO A  41     -74.798  25.304  23.299  1.00 63.79           C  
ATOM    298  O   PRO A  41     -74.329  24.445  24.092  1.00 64.10           O  
ATOM    299  CB  PRO A  41     -77.100  24.498  22.554  1.00 63.85           C  
ATOM    300  CG  PRO A  41     -77.519  23.441  21.437  1.00 64.39           C  
ATOM    301  CD  PRO A  41     -76.290  22.703  21.120  1.00 63.31           C  
ATOM    302  N   GLY A  42     -74.562  26.621  23.371  1.00 62.87           N  
ATOM    303  CA  GLY A  42     -73.602  27.246  24.261  1.00 62.30           C  
ATOM    304  C   GLY A  42     -72.161  26.752  24.214  1.00 62.53           C  
ATOM    305  O   GLY A  42     -71.392  27.037  25.134  1.00 64.01           O  
ATOM    306  N   LYS A  43     -71.780  26.052  23.159  1.00 61.20           N  
ATOM    307  CA  LYS A  43     -70.429  25.510  23.035  1.00 62.09           C  
ATOM    308  C   LYS A  43     -69.679  26.089  21.837  1.00 61.66           C  
ATOM    309  O   LYS A  43     -70.283  26.607  20.906  1.00 60.02           O  
ATOM    310  CB  LYS A  43     -70.477  23.975  22.896  1.00 61.99           C  
ATOM    311  CG  LYS A  43     -70.052  23.197  24.139  1.00 64.61           C  
ATOM    312  CD  LYS A  43     -71.069  23.314  25.240  1.00 70.70           C  
ATOM    313  CE  LYS A  43     -70.400  23.352  26.602  1.00 76.51           C  
ATOM    314  NZ  LYS A  43     -71.321  23.821  27.730  1.00 78.09           N  
ATOM    315  N   GLU A  44     -68.359  25.969  21.865  1.00 61.93           N  
ATOM    316  CA  GLU A  44     -67.539  26.457  20.792  1.00 63.00           C  
ATOM    317  C   GLU A  44     -67.597  25.424  19.668  1.00 62.16           C  
ATOM    318  O   GLU A  44     -67.633  24.236  19.923  1.00 61.44           O  
ATOM    319  CB  GLU A  44     -66.108  26.694  21.255  1.00 62.96           C  
ATOM    320  CG  GLU A  44     -65.937  28.078  21.880  1.00 73.87           C  
ATOM    321  CD  GLU A  44     -64.785  28.163  22.871  1.00 84.96           C  
ATOM    322  OE1 GLU A  44     -63.770  27.427  22.688  1.00 89.61           O  
ATOM    323  OE2 GLU A  44     -64.895  28.985  23.829  1.00 87.80           O  
ATOM    324  N   ARG A  45     -67.634  25.913  18.438  1.00 61.31           N  
ATOM    325  CA  ARG A  45     -67.571  25.103  17.252  1.00 62.94           C  
ATOM    326  C   ARG A  45     -66.371  24.184  17.340  1.00 62.83           C  
ATOM    327  O   ARG A  45     -65.348  24.585  17.821  1.00 65.14           O  
ATOM    328  CB  ARG A  45     -67.434  26.028  16.046  1.00 62.53           C  
ATOM    329  CG  ARG A  45     -67.381  25.292  14.736  1.00 65.59           C  
ATOM    330  CD  ARG A  45     -67.546  26.257  13.580  1.00 67.77           C  
ATOM    331  NE  ARG A  45     -66.344  27.027  13.259  1.00 67.41           N  
ATOM    332  CZ  ARG A  45     -66.404  28.206  12.619  1.00 70.42           C  
ATOM    333  NH1 ARG A  45     -67.593  28.707  12.290  1.00 70.52           N  
ATOM    334  NH2 ARG A  45     -65.315  28.915  12.336  1.00 66.28           N  
ATOM    335  N   GLU A  46     -66.494  22.972  16.851  1.00 62.40           N  
ATOM    336  CA  GLU A  46     -65.469  21.953  16.962  1.00 62.62           C  
ATOM    337  C   GLU A  46     -65.252  21.366  15.540  1.00 60.01           C  
ATOM    338  O   GLU A  46     -66.212  21.072  14.871  1.00 59.73           O  
ATOM    339  CB  GLU A  46     -65.980  20.879  17.949  1.00 62.17           C  
ATOM    340  CG  GLU A  46     -65.123  19.640  18.007  1.00 66.60           C  
ATOM    341  CD  GLU A  46     -65.649  18.535  18.965  1.00 67.68           C  
ATOM    342  OE1 GLU A  46     -66.833  18.200  18.984  1.00 69.92           O  
ATOM    343  OE2 GLU A  46     -64.826  17.950  19.682  1.00 75.78           O  
ATOM    344  N   TRP A  47     -64.008  21.208  15.095  1.00 57.57           N  
ATOM    345  CA  TRP A  47     -63.713  20.600  13.807  1.00 57.25           C  
ATOM    346  C   TRP A  47     -63.994  19.083  13.854  1.00 56.57           C  
ATOM    347  O   TRP A  47     -63.705  18.420  14.826  1.00 57.80           O  
ATOM    348  CB  TRP A  47     -62.253  20.863  13.417  1.00 56.80           C  
ATOM    349  CG  TRP A  47     -61.858  20.042  12.260  1.00 56.46           C  
ATOM    350  CD1 TRP A  47     -62.152  20.316  10.973  1.00 54.76           C  
ATOM    351  CD2 TRP A  47     -61.065  18.865  12.252  1.00 52.47           C  
ATOM    352  NE1 TRP A  47     -61.635  19.403  10.174  1.00 58.96           N  
ATOM    353  CE2 TRP A  47     -60.953  18.471  10.920  1.00 57.67           C  
ATOM    354  CE3 TRP A  47     -60.449  18.074  13.247  1.00 55.32           C  
ATOM    355  CZ2 TRP A  47     -60.260  17.294  10.530  1.00 54.05           C  
ATOM    356  CZ3 TRP A  47     -59.758  16.948  12.868  1.00 51.16           C  
ATOM    357  CH2 TRP A  47     -59.675  16.559  11.518  1.00 53.88           C  
ATOM    358  N   VAL A  48     -64.584  18.560  12.803  1.00 55.90           N  
ATOM    359  CA  VAL A  48     -64.932  17.153  12.730  1.00 57.16           C  
ATOM    360  C   VAL A  48     -64.102  16.275  11.702  1.00 57.40           C  
ATOM    361  O   VAL A  48     -63.695  15.121  11.957  1.00 59.40           O  
ATOM    362  CB  VAL A  48     -66.488  17.024  12.471  1.00 55.58           C  
ATOM    363  CG1 VAL A  48     -66.870  15.636  12.122  1.00 57.71           C  
ATOM    364  CG2 VAL A  48     -67.283  17.551  13.666  1.00 52.64           C  
ATOM    365  N   ALA A  49     -63.943  16.803  10.511  1.00 58.19           N  
ATOM    366  CA  ALA A  49     -63.480  16.044   9.388  1.00 57.27           C  
ATOM    367  C   ALA A  49     -63.152  17.015   8.232  1.00 58.40           C  
ATOM    368  O   ALA A  49     -63.724  18.103   8.113  1.00 58.10           O  
ATOM    369  CB  ALA A  49     -64.493  14.986   8.988  1.00 58.70           C  
ATOM    370  N   ARG A  50     -62.133  16.606   7.462  1.00 57.50           N  
ATOM    371  CA  ARG A  50     -61.617  17.305   6.309  1.00 57.51           C  
ATOM    372  C   ARG A  50     -61.284  16.287   5.191  1.00 56.81           C  
ATOM    373  O   ARG A  50     -60.782  15.166   5.443  1.00 57.50           O  
ATOM    374  CB  ARG A  50     -60.376  18.124   6.727  1.00 58.04           C  
ATOM    375  CG  ARG A  50     -59.530  18.735   5.644  1.00 56.54           C  
ATOM    376  CD  ARG A  50     -60.113  20.097   5.209  1.00 60.05           C  
ATOM    377  NE  ARG A  50     -59.092  20.758   4.440  1.00 59.36           N  
ATOM    378  CZ  ARG A  50     -58.247  21.656   4.897  1.00 59.23           C  
ATOM    379  NH1 ARG A  50     -58.347  22.072   6.126  1.00 60.11           N  
ATOM    380  NH2 ARG A  50     -57.295  22.156   4.093  1.00 57.42           N  
ATOM    381  N   ILE A  51     -61.672  16.660   3.989  1.00 57.82           N  
ATOM    382  CA  ILE A  51     -61.319  15.953   2.743  1.00 57.03           C  
ATOM    383  C   ILE A  51     -60.638  16.940   1.738  1.00 57.36           C  
ATOM    384  O   ILE A  51     -61.030  18.055   1.571  1.00 60.10           O  
ATOM    385  CB  ILE A  51     -62.544  15.146   2.143  1.00 57.20           C  
ATOM    386  CG1 ILE A  51     -62.099  14.222   0.939  1.00 55.96           C  
ATOM    387  CG2 ILE A  51     -63.650  16.139   1.754  1.00 58.21           C  
ATOM    388  CD1 ILE A  51     -63.004  13.128   0.544  1.00 57.20           C  
ATOM    389  N   ASN A  52     -59.558  16.538   1.096  1.00 57.17           N  
ATOM    390  CA  ASN A  52     -58.885  17.407   0.157  1.00 54.68           C  
ATOM    391  C   ASN A  52     -59.692  17.577  -1.204  1.00 55.07           C  
ATOM    392  O   ASN A  52     -60.656  16.860  -1.486  1.00 56.24           O  
ATOM    393  CB  ASN A  52     -57.389  16.943  -0.030  1.00 53.77           C  
ATOM    394  CG  ASN A  52     -57.278  15.649  -0.735  1.00 49.71           C  
ATOM    395  OD1 ASN A  52     -58.261  14.987  -0.883  1.00 54.97           O  
ATOM    396  ND2 ASN A  52     -56.104  15.329  -1.297  1.00 47.65           N  
ATOM    397  N   SER A  53     -59.258  18.501  -2.026  1.00 53.48           N  
ATOM    398  CA  SER A  53     -59.916  18.776  -3.272  1.00 53.19           C  
ATOM    399  C   SER A  53     -59.708  17.604  -4.242  1.00 53.07           C  
ATOM    400  O   SER A  53     -60.592  17.269  -5.001  1.00 54.57           O  
ATOM    401  CB  SER A  53     -59.413  20.104  -3.867  1.00 51.37           C  
ATOM    402  OG  SER A  53     -58.091  19.955  -4.372  1.00 50.71           O  
ATOM    403  N   GLY A  54     -58.584  16.919  -4.153  1.00 53.52           N  
ATOM    404  CA  GLY A  54     -58.414  15.724  -4.991  1.00 53.41           C  
ATOM    405  C   GLY A  54     -59.288  14.580  -4.497  1.00 53.01           C  
ATOM    406  O   GLY A  54     -59.327  13.562  -5.097  1.00 53.45           O  
ATOM    407  N   ARG A  55     -59.897  14.735  -3.342  1.00 53.51           N  
ATOM    408  CA  ARG A  55     -60.840  13.747  -2.783  1.00 54.57           C  
ATOM    409  C   ARG A  55     -60.164  12.433  -2.409  1.00 55.94           C  
ATOM    410  O   ARG A  55     -60.820  11.407  -2.307  1.00 54.76           O  
ATOM    411  CB  ARG A  55     -61.987  13.507  -3.779  1.00 54.30           C  
ATOM    412  CG  ARG A  55     -62.817  14.764  -4.059  1.00 52.70           C  
ATOM    413  CD  ARG A  55     -63.704  15.103  -2.768  1.00 52.20           C  
ATOM    414  NE  ARG A  55     -64.628  16.173  -3.103  1.00 57.17           N  
ATOM    415  CZ  ARG A  55     -64.450  17.428  -2.769  1.00 55.03           C  
ATOM    416  NH1 ARG A  55     -63.434  17.777  -2.036  1.00 53.34           N  
ATOM    417  NH2 ARG A  55     -65.326  18.318  -3.124  1.00 58.47           N  
ATOM    418  N   ASP A  56     -58.843  12.452  -2.209  1.00 56.37           N  
ATOM    419  CA  ASP A  56     -58.162  11.185  -1.898  1.00 54.92           C  
ATOM    420  C   ASP A  56     -57.440  11.131  -0.519  1.00 55.60           C  
ATOM    421  O   ASP A  56     -56.787  10.168  -0.179  1.00 58.03           O  
ATOM    422  CB  ASP A  56     -57.214  10.850  -3.020  1.00 52.81           C  
ATOM    423  CG  ASP A  56     -56.161  11.904  -3.233  1.00 52.68           C  
ATOM    424  OD1 ASP A  56     -56.182  13.090  -2.798  1.00 56.00           O  
ATOM    425  OD2 ASP A  56     -55.285  11.545  -3.927  1.00 51.13           O  
ATOM    426  N   ILE A  57     -57.530  12.191   0.235  1.00 57.57           N  
ATOM    427  CA  ILE A  57     -56.971  12.233   1.524  1.00 57.86           C  
ATOM    428  C   ILE A  57     -57.974  12.807   2.501  1.00 58.13           C  
ATOM    429  O   ILE A  57     -58.603  13.839   2.252  1.00 58.53           O  
ATOM    430  CB  ILE A  57     -55.684  13.121   1.468  1.00 58.34           C  
ATOM    431  CG1 ILE A  57     -54.711  12.504   0.497  1.00 53.70           C  
ATOM    432  CG2 ILE A  57     -55.161  13.357   2.836  1.00 60.46           C  
ATOM    433  CD1 ILE A  57     -53.634  13.355   0.137  1.00 64.71           C  
ATOM    434  N   THR A  58     -58.121  12.119   3.627  1.00 58.96           N  
ATOM    435  CA  THR A  58     -59.109  12.478   4.627  1.00 58.21           C  
ATOM    436  C   THR A  58     -58.464  12.628   6.038  1.00 58.57           C  
ATOM    437  O   THR A  58     -57.412  12.056   6.316  1.00 57.04           O  
ATOM    438  CB  THR A  58     -60.336  11.496   4.643  1.00 58.38           C  
ATOM    439  OG1 THR A  58     -59.903  10.150   4.826  1.00 62.63           O  
ATOM    440  CG2 THR A  58     -61.125  11.554   3.346  1.00 54.83           C  
ATOM    441  N   TYR A  59     -59.008  13.540   6.838  1.00 56.89           N  
ATOM    442  CA  TYR A  59     -58.586  13.661   8.223  1.00 57.15           C  
ATOM    443  C   TYR A  59     -59.810  13.693   9.113  1.00 57.87           C  
ATOM    444  O   TYR A  59     -60.793  14.343   8.732  1.00 59.13           O  
ATOM    445  CB  TYR A  59     -57.769  14.917   8.450  1.00 57.10           C  
ATOM    446  CG  TYR A  59     -56.466  14.962   7.667  1.00 57.48           C  
ATOM    447  CD1 TYR A  59     -55.344  14.274   8.128  1.00 59.45           C  
ATOM    448  CD2 TYR A  59     -56.358  15.712   6.487  1.00 56.89           C  
ATOM    449  CE1 TYR A  59     -54.127  14.338   7.419  1.00 59.17           C  
ATOM    450  CE2 TYR A  59     -55.164  15.752   5.740  1.00 57.24           C  
ATOM    451  CZ  TYR A  59     -54.049  15.058   6.218  1.00 58.38           C  
ATOM    452  OH  TYR A  59     -52.866  15.067   5.525  1.00 57.87           O  
ATOM    453  N   TYR A  60     -59.751  12.973  10.255  1.00 57.39           N  
ATOM    454  CA  TYR A  60     -60.856  12.876  11.211  1.00 57.05           C  
ATOM    455  C   TYR A  60     -60.486  13.234  12.617  1.00 56.40           C  
ATOM    456  O   TYR A  60     -59.344  12.937  13.035  1.00 57.23           O  
ATOM    457  CB  TYR A  60     -61.415  11.462  11.183  1.00 58.81           C  
ATOM    458  CG  TYR A  60     -61.894  11.033   9.833  1.00 58.77           C  
ATOM    459  CD1 TYR A  60     -63.174  11.353   9.409  1.00 57.42           C  
ATOM    460  CD2 TYR A  60     -61.048  10.320   8.958  1.00 58.69           C  
ATOM    461  CE1 TYR A  60     -63.658  10.964   8.143  1.00 53.60           C  
ATOM    462  CE2 TYR A  60     -61.527   9.932   7.676  1.00 55.73           C  
ATOM    463  CZ  TYR A  60     -62.846  10.290   7.305  1.00 55.60           C  
ATOM    464  OH  TYR A  60     -63.386   9.901   6.099  1.00 58.53           O  
ATOM    465  N   ALA A  61     -61.377  13.942  13.330  1.00 56.27           N  
ATOM    466  CA  ALA A  61     -61.119  14.215  14.751  1.00 56.88           C  
ATOM    467  C   ALA A  61     -61.001  12.898  15.506  1.00 55.31           C  
ATOM    468  O   ALA A  61     -61.610  11.869  15.101  1.00 57.15           O  
ATOM    469  CB  ALA A  61     -62.155  15.239  15.410  1.00 57.37           C  
ATOM    470  N   ASP A  62     -60.185  12.892  16.560  1.00 55.83           N  
ATOM    471  CA  ASP A  62     -59.966  11.743  17.414  1.00 54.83           C  
ATOM    472  C   ASP A  62     -61.285  10.979  17.784  1.00 56.01           C  
ATOM    473  O   ASP A  62     -61.368   9.736  17.785  1.00 55.75           O  
ATOM    474  CB  ASP A  62     -59.245  12.177  18.715  1.00 56.05           C  
ATOM    475  CG  ASP A  62     -57.752  12.294  18.559  1.00 58.65           C  
ATOM    476  OD1 ASP A  62     -57.291  11.963  17.460  1.00 55.91           O  
ATOM    477  OD2 ASP A  62     -57.048  12.741  19.529  1.00 59.18           O  
CONECT  149  751                                                                
CONECT  231  811                                                                
CONECT  751  149                                                                
CONECT  811  231                                                                
CONECT 1136 1738                                                                
CONECT 1218 1798                                                                
CONECT 1738 1136                                                                
CONECT 1798 1218                                                                
CONECT 2130 2732                                                                
CONECT 2212 2792                                                                
CONECT 2732 2130                                                                
CONECT 2792 2212                                                                
CONECT 3121 3584                                                                
CONECT 3584 3121                                                                
CONECT 3891 4334                                                                
CONECT 4334 3891                                                                
CONECT 4630 5093                                                                
CONECT 5093 4630                                                                
CONECT 5362 5790                                                                
CONECT 5406 5430                                                                
CONECT 5430 5406                                                                
CONECT 5790 5362                                                                
MASTER     1198    0    0   12   82    0    0    6 6225    7   22   62          
END                                                                             
