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Database: PDB
Entry: 3IHX
LinkDB: 3IHX
Original site: 3IHX 
HEADER    TRANSFERASE                             31-JUL-09   3IHX              
TITLE     METHYLTRANSFERASE DOMAIN OF HUMAN PR DOMAIN-CONTAINING PROTEIN 10     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PR DOMAIN ZINC FINGER PROTEIN 10;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 188 TO 339;                                   
COMPND   5 SYNONYM: PR DOMAIN-CONTAINING PROTEIN 10, TRISTANIN;                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRDM10, KIAA1231, PFM7, TRIS;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PRDM10, METHYLTRANSFERASE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS   
KEYWDS   2 CONSORTIUM, SGC, DNA-BINDING, METAL-BINDING, NUCLEUS,                
KEYWDS   3 PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC-       
KEYWDS   4 FINGER, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.AMAYA,L.DOMBROVSKI,S.NI,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,       
AUTHOR   2 A.M.EDWARDS,A.BOTCHKAREV,J.MIN,A.N.PLOTNIKOV,H.WU,STRUCTURAL         
AUTHOR   3 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   3   01-NOV-17 3IHX    1       REMARK                                   
REVDAT   2   13-JUL-11 3IHX    1       VERSN                                    
REVDAT   1   18-AUG-09 3IHX    0                                                
JRNL        AUTH   M.F.AMAYA,L.DOMBROVSKI,S.NI,C.BOUNTRA,J.WEIGELT,             
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOTCHKAREV,J.MIN,A.N.PLOTNIKOV, 
JRNL        AUTH 3 H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)                    
JRNL        TITL   METHYLTRANSFERASE DOMAIN OF HUMAN PR DOMAIN-CONTAINING       
JRNL        TITL 2 PROTEIN 10                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 94.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 22254                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 976                             
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1478                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 56                           
REMARK   3   BIN FREE R VALUE                    : 0.4630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3782                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 52                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.54000                                             
REMARK   3    B22 (A**2) : -2.54000                                             
REMARK   3    B33 (A**2) : 5.07000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.460         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.316         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.302         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.521        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3893 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5325 ; 1.742 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   484 ; 7.734 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   164 ;35.530 ;22.988       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   517 ;16.331 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;16.892 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   585 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3026 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2472 ; 0.612 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3905 ; 1.121 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1421 ; 1.999 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1420 ; 3.137 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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     6        A    91                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3114 -64.8778  -1.3956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3069 T22:   0.4255                                     
REMARK   3      T33:   0.4415 T12:  -0.0295                                     
REMARK   3      T13:  -0.0167 T23:  -0.2438                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.0764 L22:   4.1975                                     
REMARK   3      L33:   0.8901 L12:  -0.4136                                     
REMARK   3      L13:  -1.9820 L23:  -1.2988                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0475 S12:  -0.6892 S13:  -0.1234                       
REMARK   3      S21:   0.0618 S22:   0.2043 S23:   0.0340                       
REMARK   3      S31:   0.0229 S32:   0.1484 S33:  -0.1568                       
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 :   A    92        A   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6180 -64.5819  -0.1087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1565 T22:   0.3436                                     
REMARK   3      T33:   0.3361 T12:  -0.0254                                     
REMARK   3      T13:   0.0614 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8988 L22:   4.1933                                     
REMARK   3      L33:   3.0343 L12:  -1.0265                                     
REMARK   3      L13:   0.0025 L23:   0.3042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1511 S12:  -0.4809 S13:  -0.4726                       
REMARK   3      S21:   0.1787 S22:   0.4712 S23:   0.3816                       
REMARK   3      S31:  -0.0033 S32:  -0.0378 S33:  -0.3201                       
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 :   B     5        B   148                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9182 -37.2324   4.2196              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1642 T22:   0.2658                                     
REMARK   3      T33:   0.2002 T12:  -0.1162                                     
REMARK   3      T13:   0.0146 T23:  -0.0665                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4427 L22:   5.9407                                     
REMARK   3      L33:   1.9154 L12:   1.1867                                     
REMARK   3      L13:   1.2901 L23:   0.3643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4758 S12:   0.5362 S13:  -0.1544                       
REMARK   3      S21:  -0.2736 S22:   0.5679 S23:  -0.6867                       
REMARK   3      S31:   0.0435 S32:   0.1758 S33:  -0.0921                       
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 :   C    11        C   148                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1347 -57.8286   0.6057              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1637 T22:   0.1998                                     
REMARK   3      T33:   0.2978 T12:   0.0147                                     
REMARK   3      T13:   0.0733 T23:   0.0996                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7508 L22:   4.0455                                     
REMARK   3      L33:   2.1291 L12:  -0.0338                                     
REMARK   3      L13:  -1.2406 L23:  -0.9297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1980 S12:  -0.6559 S13:  -0.4238                       
REMARK   3      S21:   0.2340 S22:   0.2313 S23:   0.3218                       
REMARK   3      S31:  -0.3075 S32:  -0.0598 S33:  -0.0333                       
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 :   D     7        D    93                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7900 -31.5770  -4.7128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4482 T22:   0.2106                                     
REMARK   3      T33:   0.4590 T12:  -0.0645                                     
REMARK   3      T13:  -0.2288 T23:   0.1611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.3431 L22:   2.5434                                     
REMARK   3      L33:   3.9854 L12:   0.4408                                     
REMARK   3      L13:   7.1812 L23:   1.2083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0586 S12:  -0.0814 S13:   1.0432                       
REMARK   3      S21:  -0.2965 S22:   0.2526 S23:   0.8390                       
REMARK   3      S31:  -0.6435 S32:   0.0483 S33:   0.8060                       
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 :   D    94        D   147                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5703 -31.7897  -0.1638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2755 T22:   0.2459                                     
REMARK   3      T33:   0.1468 T12:  -0.0845                                     
REMARK   3      T13:  -0.1585 T23:   0.1028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.0463 L22:   5.0968                                     
REMARK   3      L33:   3.0561 L12:   2.0013                                     
REMARK   3      L13:   3.7095 L23:   0.5260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9130 S12:   0.1041 S13:   1.0503                       
REMARK   3      S21:  -0.1538 S22:   0.4666 S23:   0.4454                       
REMARK   3      S31:  -0.3373 S32:   0.2545 S33:   0.4463                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3IHX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054432.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25428                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 3DB5, 3EP0                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2NH4OAC, BIS -6.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, PH 6.5                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.38450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       57.57675            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       19.19225            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     LYS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     SER A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     ASP A    71                                                      
REMARK 465     LYS A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     ASP A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     LYS A    76                                                      
REMARK 465     GLU A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     ASP A    79                                                      
REMARK 465     LEU A    80                                                      
REMARK 465     HIS A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     ASP A    83                                                      
REMARK 465     ASN A   147                                                      
REMARK 465     GLN A   148                                                      
REMARK 465     LYS A   149                                                      
REMARK 465     ILE A   150                                                      
REMARK 465     HIS A   151                                                      
REMARK 465     ASP A   152                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     LYS B    37                                                      
REMARK 465     LEU B    70                                                      
REMARK 465     ASP B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     ASP B    74                                                      
REMARK 465     ARG B    75                                                      
REMARK 465     LYS B    76                                                      
REMARK 465     GLU B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     ASP B    79                                                      
REMARK 465     LEU B    80                                                      
REMARK 465     HIS B    81                                                      
REMARK 465     GLU B    82                                                      
REMARK 465     LYS B   131                                                      
REMARK 465     LYS B   149                                                      
REMARK 465     ILE B   150                                                      
REMARK 465     HIS B   151                                                      
REMARK 465     ASP B   152                                                      
REMARK 465     LYS C     1                                                      
REMARK 465     HIS C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     PRO C     7                                                      
REMARK 465     ILE C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     ASN C    10                                                      
REMARK 465     SER C    69                                                      
REMARK 465     LEU C    70                                                      
REMARK 465     ASP C    71                                                      
REMARK 465     LYS C    72                                                      
REMARK 465     GLY C    73                                                      
REMARK 465     ASP C    74                                                      
REMARK 465     ARG C    75                                                      
REMARK 465     LYS C    76                                                      
REMARK 465     GLU C    77                                                      
REMARK 465     ARG C    78                                                      
REMARK 465     ASP C    79                                                      
REMARK 465     LEU C    80                                                      
REMARK 465     HIS C    81                                                      
REMARK 465     GLU C    82                                                      
REMARK 465     LYS C   149                                                      
REMARK 465     ILE C   150                                                      
REMARK 465     HIS C   151                                                      
REMARK 465     ASP C   152                                                      
REMARK 465     LYS D     1                                                      
REMARK 465     HIS D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     LEU D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     PRO D    52                                                      
REMARK 465     LEU D    53                                                      
REMARK 465     VAL D    54                                                      
REMARK 465     ARG D    55                                                      
REMARK 465     GLY D    56                                                      
REMARK 465     SER D    57                                                      
REMARK 465     GLU D    58                                                      
REMARK 465     LEU D    59                                                      
REMARK 465     LYS D    60                                                      
REMARK 465     SER D    69                                                      
REMARK 465     LEU D    70                                                      
REMARK 465     ASP D    71                                                      
REMARK 465     LYS D    72                                                      
REMARK 465     GLY D    73                                                      
REMARK 465     ASP D    74                                                      
REMARK 465     ARG D    75                                                      
REMARK 465     LYS D    76                                                      
REMARK 465     GLU D    77                                                      
REMARK 465     ARG D    78                                                      
REMARK 465     ASP D    79                                                      
REMARK 465     LEU D    80                                                      
REMARK 465     HIS D    81                                                      
REMARK 465     GLU D    82                                                      
REMARK 465     ASP D    83                                                      
REMARK 465     LEU D    84                                                      
REMARK 465     GLN D   148                                                      
REMARK 465     LYS D   149                                                      
REMARK 465     ILE D   150                                                      
REMARK 465     HIS D   151                                                      
REMARK 465     ASP D   152                                                      
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     HIS A   6    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A  16    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  36    OG                                                  
REMARK 470     LYS A  37    CG   CD   CE   NZ                                   
REMARK 470     ARG A  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A  40    CG1  CG2  CD1                                       
REMARK 470     VAL A  54    CG1  CG2                                            
REMARK 470     ARG A  55    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  58    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  59    CG   CD1  CD2                                       
REMARK 470     LYS A  67    CG   CD   CE   NZ                                   
REMARK 470     VAL A  68    CG1  CG2                                            
REMARK 470     LEU A  84    CG   CD1  CD2                                       
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     SER A  89    OG                                                  
REMARK 470     LEU A  93    CG   CD1  CD2                                       
REMARK 470     ASN A  95    CG   OD1  ND2                                       
REMARK 470     VAL A 112    CG1  CG2                                            
REMARK 470     GLN A 115    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     GLN A 132    CG   CD   OE1  NE2                                  
REMARK 470     SER A 141    OG                                                  
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 145    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 146    CG1  CG2                                            
REMARK 470     LEU B   5    CG   CD1  CD2                                       
REMARK 470     HIS B   6    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE B   8    CG1  CG2  CD1                                       
REMARK 470     ARG B  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B  30    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B  36    OG                                                  
REMARK 470     ARG B  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     ARG B  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  54    CG1  CG2                                            
REMARK 470     ARG B  55    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  58    CG   CD   OE1  OE2                                  
REMARK 470     SER B  69    OG                                                  
REMARK 470     GLU B  87    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 106    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU B 107    CG   CD1  CD2                                       
REMARK 470     VAL B 112    CG1  CG2                                            
REMARK 470     HIS B 118    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL B 128    CG1  CG2                                            
REMARK 470     GLU B 129    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 132    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 134    CG   CD1  CD2                                       
REMARK 470     SER B 141    OG                                                  
REMARK 470     GLU B 144    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 148    CG   CD   OE1  NE2                                  
REMARK 470     VAL C  24    CG1  CG2                                            
REMARK 470     ARG C  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE C  30    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER C  36    OG                                                  
REMARK 470     ARG C  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  50    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  55    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  58    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  67    CG   CD   CE   NZ                                   
REMARK 470     VAL C  68    CG1  CG2                                            
REMARK 470     THR C  92    OG1  CG2                                            
REMARK 470     LEU C  93    CG   CD1  CD2                                       
REMARK 470     LEU C 107    CG   CD1  CD2                                       
REMARK 470     HIS C 118    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     LYS C 131    CG   CD   CE   NZ                                   
REMARK 470     SER C 141    OG                                                  
REMARK 470     ILE D   8    CD1                                                 
REMARK 470     ARG D  16    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D  23    CG   CD1  CD2                                       
REMARK 470     ARG D  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D  31    CG   CD1  CD2                                       
REMARK 470     SER D  36    OG                                                  
REMARK 470     LYS D  37    CG   CD   CE   NZ                                   
REMARK 470     ARG D  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D  61    CG   OD1  OD2                                       
REMARK 470     CYS D  62    SG                                                  
REMARK 470     ILE D  64    CG1  CG2  CD1                                       
REMARK 470     LYS D  67    CG   CD   CE   NZ                                   
REMARK 470     VAL D  68    CG1  CG2                                            
REMARK 470     GLU D  87    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 104    CG   CD   OE1  NE2                                  
REMARK 470     HIS D 118    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     VAL D 128    CG1  CG2                                            
REMARK 470     LYS D 131    CG   CD   CE   NZ                                   
REMARK 470     GLN D 132    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 144    CG   CD   OE1  OE2                                  
REMARK 470     ASN D 147    CG   OD1  ND2                                       
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  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    PRO D   9   C   -  N   -  CA  ANGL. DEV. =  -9.8 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    VAL A  54     -152.16   -141.17                                   
REMARK 500    GLU A  58       67.66     34.52                                   
REMARK 500    LEU A  88       49.33    -96.62                                   
REMARK 500    TYR A 116      -58.94   -128.11                                   
REMARK 500    LEU B  88       48.03    -90.16                                   
REMARK 500    HIS B 118       26.49     48.85                                   
REMARK 500    ARG C  38     -154.62   -139.31                                   
REMARK 500    LYS D  42      138.93    -39.43                                   
REMARK 500    CYS D  62       59.78   -143.58                                   
REMARK 500    LEU D  88       31.43    -77.00                                   
REMARK 500    HIS D 118       41.41   -105.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3IHX A    1   152  UNP    Q9NQV6   PRD10_HUMAN    188    339             
DBREF  3IHX B    1   152  UNP    Q9NQV6   PRD10_HUMAN    188    339             
DBREF  3IHX C    1   152  UNP    Q9NQV6   PRD10_HUMAN    188    339             
DBREF  3IHX D    1   152  UNP    Q9NQV6   PRD10_HUMAN    188    339             
SEQRES   1 A  152  LYS HIS GLY PRO LEU HIS PRO ILE PRO ASN ARG PRO VAL          
SEQRES   2 A  152  LEU THR ARG ALA ARG ALA SER LEU PRO LEU VAL LEU TYR          
SEQRES   3 A  152  ILE ASP ARG PHE LEU GLY GLY VAL PHE SER LYS ARG ARG          
SEQRES   4 A  152  ILE PRO LYS ARG THR GLN PHE GLY PRO VAL GLU GLY PRO          
SEQRES   5 A  152  LEU VAL ARG GLY SER GLU LEU LYS ASP CYS TYR ILE HIS          
SEQRES   6 A  152  LEU LYS VAL SER LEU ASP LYS GLY ASP ARG LYS GLU ARG          
SEQRES   7 A  152  ASP LEU HIS GLU ASP LEU TRP PHE GLU LEU SER ASP GLU          
SEQRES   8 A  152  THR LEU CYS ASN TRP MET MET PHE VAL ARG PRO ALA GLN          
SEQRES   9 A  152  ASN HIS LEU GLU GLN ASN LEU VAL ALA TYR GLN TYR GLY          
SEQRES  10 A  152  HIS HIS VAL TYR TYR THR THR ILE LYS ASN VAL GLU PRO          
SEQRES  11 A  152  LYS GLN GLU LEU LYS VAL TRP TYR ALA ALA SER TYR ALA          
SEQRES  12 A  152  GLU PHE VAL ASN GLN LYS ILE HIS ASP                          
SEQRES   1 B  152  LYS HIS GLY PRO LEU HIS PRO ILE PRO ASN ARG PRO VAL          
SEQRES   2 B  152  LEU THR ARG ALA ARG ALA SER LEU PRO LEU VAL LEU TYR          
SEQRES   3 B  152  ILE ASP ARG PHE LEU GLY GLY VAL PHE SER LYS ARG ARG          
SEQRES   4 B  152  ILE PRO LYS ARG THR GLN PHE GLY PRO VAL GLU GLY PRO          
SEQRES   5 B  152  LEU VAL ARG GLY SER GLU LEU LYS ASP CYS TYR ILE HIS          
SEQRES   6 B  152  LEU LYS VAL SER LEU ASP LYS GLY ASP ARG LYS GLU ARG          
SEQRES   7 B  152  ASP LEU HIS GLU ASP LEU TRP PHE GLU LEU SER ASP GLU          
SEQRES   8 B  152  THR LEU CYS ASN TRP MET MET PHE VAL ARG PRO ALA GLN          
SEQRES   9 B  152  ASN HIS LEU GLU GLN ASN LEU VAL ALA TYR GLN TYR GLY          
SEQRES  10 B  152  HIS HIS VAL TYR TYR THR THR ILE LYS ASN VAL GLU PRO          
SEQRES  11 B  152  LYS GLN GLU LEU LYS VAL TRP TYR ALA ALA SER TYR ALA          
SEQRES  12 B  152  GLU PHE VAL ASN GLN LYS ILE HIS ASP                          
SEQRES   1 C  152  LYS HIS GLY PRO LEU HIS PRO ILE PRO ASN ARG PRO VAL          
SEQRES   2 C  152  LEU THR ARG ALA ARG ALA SER LEU PRO LEU VAL LEU TYR          
SEQRES   3 C  152  ILE ASP ARG PHE LEU GLY GLY VAL PHE SER LYS ARG ARG          
SEQRES   4 C  152  ILE PRO LYS ARG THR GLN PHE GLY PRO VAL GLU GLY PRO          
SEQRES   5 C  152  LEU VAL ARG GLY SER GLU LEU LYS ASP CYS TYR ILE HIS          
SEQRES   6 C  152  LEU LYS VAL SER LEU ASP LYS GLY ASP ARG LYS GLU ARG          
SEQRES   7 C  152  ASP LEU HIS GLU ASP LEU TRP PHE GLU LEU SER ASP GLU          
SEQRES   8 C  152  THR LEU CYS ASN TRP MET MET PHE VAL ARG PRO ALA GLN          
SEQRES   9 C  152  ASN HIS LEU GLU GLN ASN LEU VAL ALA TYR GLN TYR GLY          
SEQRES  10 C  152  HIS HIS VAL TYR TYR THR THR ILE LYS ASN VAL GLU PRO          
SEQRES  11 C  152  LYS GLN GLU LEU LYS VAL TRP TYR ALA ALA SER TYR ALA          
SEQRES  12 C  152  GLU PHE VAL ASN GLN LYS ILE HIS ASP                          
SEQRES   1 D  152  LYS HIS GLY PRO LEU HIS PRO ILE PRO ASN ARG PRO VAL          
SEQRES   2 D  152  LEU THR ARG ALA ARG ALA SER LEU PRO LEU VAL LEU TYR          
SEQRES   3 D  152  ILE ASP ARG PHE LEU GLY GLY VAL PHE SER LYS ARG ARG          
SEQRES   4 D  152  ILE PRO LYS ARG THR GLN PHE GLY PRO VAL GLU GLY PRO          
SEQRES   5 D  152  LEU VAL ARG GLY SER GLU LEU LYS ASP CYS TYR ILE HIS          
SEQRES   6 D  152  LEU LYS VAL SER LEU ASP LYS GLY ASP ARG LYS GLU ARG          
SEQRES   7 D  152  ASP LEU HIS GLU ASP LEU TRP PHE GLU LEU SER ASP GLU          
SEQRES   8 D  152  THR LEU CYS ASN TRP MET MET PHE VAL ARG PRO ALA GLN          
SEQRES   9 D  152  ASN HIS LEU GLU GLN ASN LEU VAL ALA TYR GLN TYR GLY          
SEQRES  10 D  152  HIS HIS VAL TYR TYR THR THR ILE LYS ASN VAL GLU PRO          
SEQRES  11 D  152  LYS GLN GLU LEU LYS VAL TRP TYR ALA ALA SER TYR ALA          
SEQRES  12 D  152  GLU PHE VAL ASN GLN LYS ILE HIS ASP                          
FORMUL   5  HOH   *52(H2 O)                                                     
HELIX    1   1 THR A   15  SER A   20  1                                   6    
HELIX    2   2 ASN A   95  VAL A  100  5                                   6    
HELIX    3   3 ALA A  139  VAL A  146  1                                   8    
HELIX    4   4 THR B   15  SER B   20  1                                   6    
HELIX    5   5 ASN B   95  VAL B  100  5                                   6    
HELIX    6   6 ALA B  139  GLN B  148  1                                  10    
HELIX    7   7 THR C   15  SER C   20  1                                   6    
HELIX    8   8 ASN C   95  VAL C  100  5                                   6    
HELIX    9   9 ALA C  139  ASN C  147  1                                   9    
HELIX   10  10 THR D   15  SER D   20  1                                   6    
HELIX   11  11 ASN D   95  VAL D  100  5                                   6    
HELIX   12  12 ALA D  139  ASN D  147  1                                   9    
SHEET    1   A 2 LEU A  25  ILE A  27  0                                        
SHEET    2   A 2 VAL A  34  SER A  36 -1  O  PHE A  35   N  TYR A  26           
SHEET    1   B 4 GLN A  45  PHE A  46  0                                        
SHEET    2   B 4 VAL A 120  THR A 124 -1  O  TYR A 122   N  PHE A  46           
SHEET    3   B 4 LEU A 111  GLN A 115 -1  N  VAL A 112   O  THR A 123           
SHEET    4   B 4 VAL A 136  TYR A 138  1  O  TRP A 137   N  ALA A 113           
SHEET    1   C 2 LEU A  53  VAL A  54  0                                        
SHEET    2   C 2 TRP A  85  PHE A  86 -1  O  TRP A  85   N  VAL A  54           
SHEET    1   D 2 TYR B  26  ILE B  27  0                                        
SHEET    2   D 2 VAL B  34  PHE B  35 -1  O  PHE B  35   N  TYR B  26           
SHEET    1   E 5 GLN B  45  PHE B  46  0                                        
SHEET    2   E 5 HIS B 119  THR B 124 -1  O  TYR B 122   N  PHE B  46           
SHEET    3   E 5 LEU B 111  TYR B 116 -1  N  VAL B 112   O  THR B 123           
SHEET    4   E 5 LYS B 135  TYR B 138  1  O  TRP B 137   N  ALA B 113           
SHEET    5   E 5 ARG B 101  PRO B 102  1  N  ARG B 101   O  VAL B 136           
SHEET    1   F 3 LEU B  53  VAL B  54  0                                        
SHEET    2   F 3 LEU B  84  PHE B  86 -1  O  TRP B  85   N  VAL B  54           
SHEET    3   F 3 LYS B  67  VAL B  68 -1  N  VAL B  68   O  LEU B  84           
SHEET    1   G 2 LEU C  25  ILE C  27  0                                        
SHEET    2   G 2 VAL C  34  SER C  36 -1  O  PHE C  35   N  TYR C  26           
SHEET    1   H 5 GLN C  45  PHE C  46  0                                        
SHEET    2   H 5 VAL C 120  THR C 124 -1  O  TYR C 122   N  PHE C  46           
SHEET    3   H 5 LEU C 111  GLN C 115 -1  N  TYR C 114   O  TYR C 121           
SHEET    4   H 5 LYS C 135  TYR C 138  1  O  TRP C 137   N  ALA C 113           
SHEET    5   H 5 ARG C 101  PRO C 102  1  N  ARG C 101   O  VAL C 136           
SHEET    1   I 2 LEU C  53  VAL C  54  0                                        
SHEET    2   I 2 TRP C  85  PHE C  86 -1  O  TRP C  85   N  VAL C  54           
SHEET    1   J 3 LEU D  25  ILE D  27  0                                        
SHEET    2   J 3 VAL D  34  SER D  36 -1  O  PHE D  35   N  TYR D  26           
SHEET    3   J 3 GLU D 133  LEU D 134 -1  O  LEU D 134   N  VAL D  34           
SHEET    1   K 4 GLN D  45  PHE D  46  0                                        
SHEET    2   K 4 VAL D 120  THR D 124 -1  O  TYR D 122   N  PHE D  46           
SHEET    3   K 4 LEU D 111  GLN D 115 -1  N  VAL D 112   O  THR D 123           
SHEET    4   K 4 VAL D 136  TYR D 138  1  O  TRP D 137   N  ALA D 113           
CISPEP   1 GLY A   47    PRO A   48          0         6.03                     
CISPEP   2 GLY B   47    PRO B   48          0        11.37                     
CISPEP   3 GLY C   47    PRO C   48          0        15.44                     
CISPEP   4 GLY D   47    PRO D   48          0        15.94                     
CRYST1   94.864   94.864   76.769  90.00  90.00  90.00 P 43         16          
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      0.010541  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010541  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013026        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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