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Database: PDB
Entry: 2GSE
LinkDB: 2GSE
Original site: 2GSE 
HEADER    HYDROLASE                               26-APR-06   2GSE              
TITLE     CRYSTAL STRUCTURE OF HUMAN DIHYDROPYRIMIDINEASE-LIKE 2                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPYRIMIDINASE-RELATED PROTEIN 2;                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: DIHYDROPYRIMIDINASE-LIKE 2 (13-490);                       
COMPND   5 SYNONYM: DRP-2, COLLAPSIN RESPONSE MEDIATOR PROTEIN 2, CRMP-2, N2A3; 
COMPND   6 EC: 3.5.2.2;                                                         
COMPND   7 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: DPYSL2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4                                 
KEYWDS    ALPHA/BETA BARREL, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS           
KEYWDS   2 CONSORTIUM, SGC, DIHYDROPYRIMIDINASE-RELATED PROTEIN 2, DRP2,        
KEYWDS   3 COLLAPSIN RESPONSE MEDIATOR PROTEIN 2, CRMP2, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.OGG,P.STENMARK,C.ARROWSMITH,H.BERGLUND,R.COLLINS,A.EDWARDS,M.EHN,   
AUTHOR   2 S.FLODIN,A.FLORES,S.GRASLUND,B.M.HALLBERG,M.HAMMARSTROM,T.KOTENYOVA, 
AUTHOR   3 P.KURSULA,P.NILSSON-EHLE,T.NYMAN,C.PERSSON,J.SAGEMARK,M.SUNDSTROM,   
AUTHOR   4 L.HOLMBERG-SCHIAVONE,A.G.THORSELL,J.UPPENBERG,S.VAN DEN BERG,        
AUTHOR   5 J.WEIGELT,P.NORDLUND,STRUCTURAL GENOMICS CONSORTIUM (SGC)            
REVDAT   6   24-JAN-18 2GSE    1       AUTHOR                                   
REVDAT   5   18-OCT-17 2GSE    1       REMARK                                   
REVDAT   4   28-APR-09 2GSE    1       JRNL                                     
REVDAT   3   24-FEB-09 2GSE    1       VERSN                                    
REVDAT   2   26-SEP-06 2GSE    1       KEYWDS                                   
REVDAT   1   09-MAY-06 2GSE    0                                                
JRNL        AUTH   P.STENMARK,D.OGG,S.FLODIN,A.FLORES,T.KOTENYOVA,T.NYMAN,      
JRNL        AUTH 2 P.NORDLUND,P.KURSULA                                         
JRNL        TITL   THE STRUCTURE OF HUMAN COLLAPSIN RESPONSE MEDIATOR PROTEIN   
JRNL        TITL 2 2, A REGULATOR OF AXONAL GROWTH.                             
JRNL        REF    J.NEUROCHEM.                  V. 101   906 2007              
JRNL        REFN                   ISSN 0022-3042                               
JRNL        PMID   17250651                                                     
JRNL        DOI    10.1111/J.1471-4159.2006.04401.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 75230                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3960                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5519                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 291                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14638                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 849                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.04000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.448         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.272         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.203         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.776         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14938 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  9970 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20270 ; 1.567 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24423 ; 0.980 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1897 ; 6.572 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   657 ;37.662 ;24.764       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2526 ;16.135 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    76 ;18.892 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2289 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16731 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2885 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3178 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 10593 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7148 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7846 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   913 ; 0.195 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.012 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     9 ; 0.167 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.171 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    23 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.139 ; 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):  9790 ; 0.696 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3866 ; 0.128 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15258 ; 1.153 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5966 ; 1.697 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5012 ; 2.586 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     17       A     485      6                      
REMARK   3           1     B     17       B     485      6                      
REMARK   3           1     C     17       C     485      6                      
REMARK   3           1     D     17       D     485      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   6059 ;  0.30 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   6059 ;  0.31 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   6059 ;  0.31 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   6059 ;  0.30 ;  5.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   6059 ;  1.72 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   6059 ;  1.65 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   6059 ;  1.73 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   6059 ;  1.72 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 2GSE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037495.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 173                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PRODC                              
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79142                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.14300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.360                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 10K, 0.1M TRIS, 0.2M CACL, PH    
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                
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       63.05000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 300 REMARK: THE BIOLOGICAL ASSEMBY IS A TETRAMER                         
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 60220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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     MET A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     VAL A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     GLU A   490                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     VAL B     0                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     TYR B     8                                                      
REMARK 465     PHE B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     GLU B   490                                                      
REMARK 465     MET C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     SER C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     VAL C     0                                                      
REMARK 465     ASP C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     ASN C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     TYR C     8                                                      
REMARK 465     PHE C     9                                                      
REMARK 465     GLN C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     MET C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     GLU C   490                                                      
REMARK 465     MET D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     SER D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     VAL D     0                                                      
REMARK 465     ASP D     1                                                      
REMARK 465     LEU D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     ASN D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     TYR D     8                                                      
REMARK 465     PHE D     9                                                      
REMARK 465     GLN D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     MET D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     SER D    14                                                      
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   OD1  ASN A   347     OG1  THR A   349              1.97            
REMARK 500   OE1  GLN A   122     O    HOH A  1171              2.04            
REMARK 500   O    HOH B  1054     O    HOH D  1221              2.04            
REMARK 500   OG1  THR B   419     OE2  GLU B   438              2.06            
REMARK 500   ND2  ASN C   347     OG1  THR C   349              2.13            
REMARK 500   OD1  ASP A   128     OH   TYR A   135              2.13            
REMARK 500   O    GLY C   464     O    HOH C  1171              2.14            
REMARK 500   O    HOH C  1056     O    HOH C  1180              2.14            
REMARK 500   NZ   LYS A   398     OD2  ASP A   408              2.14            
REMARK 500   O    SER B   416     O    HOH B  1188              2.15            
REMARK 500   O    SER C    30     O    HOH C  1137              2.15            
REMARK 500   OE1  GLN C   245     O    HOH C  1042              2.19            
REMARK 500   OE1  GLN D   245     O    HOH D  1026              2.19            
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 A 179   CB    CYS A 179   SG     -0.116                       
REMARK 500    CYS C 179   CB    CYS C 179   SG     -0.147                       
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 268   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 173   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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    GLU A  38      146.04   -172.54                                   
REMARK 500    SER A  62       -3.88     71.07                                   
REMARK 500    ARG A  75       55.20   -145.66                                   
REMARK 500    PHE A 170       71.34     67.72                                   
REMARK 500    ARG A 173      -67.84   -132.45                                   
REMARK 500    CYS A 334       83.81   -151.40                                   
REMARK 500    ALA A 342       -8.25    -55.48                                   
REMARK 500    ASN A 347       98.90   -162.70                                   
REMARK 500    SER A 385      -51.55   -149.34                                   
REMARK 500    ASN A 426       40.32   -103.13                                   
REMARK 500    ASP A 456       24.95     49.43                                   
REMARK 500    ASN B  48       96.03     45.35                                   
REMARK 500    PRO B  52      158.62    -48.25                                   
REMARK 500    GLN B  77       44.90     37.69                                   
REMARK 500    PHE B 170       62.21     65.11                                   
REMARK 500    ARG B 173      -71.05   -150.04                                   
REMARK 500    LEU B 215        6.56    -60.49                                   
REMARK 500    CYS B 334       81.50   -153.04                                   
REMARK 500    SER B 385      -62.68   -143.69                                   
REMARK 500    ASN B 393       34.35     80.39                                   
REMARK 500    ASN B 426       66.25   -103.48                                   
REMARK 500    HIS B 460       69.66   -118.07                                   
REMARK 500    LEU C  17      139.00   -170.97                                   
REMARK 500    PRO C  52      179.02    -46.75                                   
REMARK 500    SER C  62       -4.45     66.16                                   
REMARK 500    ASP C  80      110.04   -168.30                                   
REMARK 500    ARG C 173      -65.04   -126.78                                   
REMARK 500    ARG C 227       63.15   -118.65                                   
REMARK 500    CYS C 334       77.38   -153.21                                   
REMARK 500    SER C 385      -56.02   -133.53                                   
REMARK 500    ASN C 393       44.20     73.01                                   
REMARK 500    ALA C 407       44.78    -85.40                                   
REMARK 500    GLN C 449       29.49     44.00                                   
REMARK 500    PRO D  52      172.31    -40.64                                   
REMARK 500    SER D  62       -3.48     64.54                                   
REMARK 500    ARG D  75       55.63   -140.26                                   
REMARK 500    GLN D  77       47.04     28.24                                   
REMARK 500    PHE D 170       67.03     70.90                                   
REMARK 500    ARG D 173      -72.70   -112.82                                   
REMARK 500    SER D 292      136.62    -39.50                                   
REMARK 500    CYS D 334       76.88   -154.57                                   
REMARK 500    ASN D 347      110.86   -163.43                                   
REMARK 500    SER D 385      -59.27   -148.02                                   
REMARK 500    ASN D 393       38.18     78.42                                   
REMARK 500    ASN D 426       59.16   -101.79                                   
REMARK 500    GLU D 463      128.59    -39.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1000  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1089   O                                                      
REMARK 620 2 HOH A1215   O    76.2                                              
REMARK 620 3 THR A 349   O   159.9  85.9                                        
REMARK 620 4 HOH A1202   O   100.7 148.3  99.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 349   O                                                      
REMARK 620 2 HOH B1061   O    91.9                                              
REMARK 620 3 HOH B1099   O   163.0  78.4                                        
REMARK 620 4 HOH B1141   O    77.8  99.7  90.1                                  
REMARK 620 5 HOH B1175   O    82.0  79.2 109.3 159.7                            
REMARK 620 6 HOH B1178   O    96.7 171.2  92.9  80.4 103.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 349   O                                                      
REMARK 620 2 HOH C1122   O   154.0                                              
REMARK 620 3 HOH C1206   O    83.6  72.9                                        
REMARK 620 4 HOH C1222   O   108.4  97.6 156.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D1089   O                                                      
REMARK 620 2 HOH D1158   O   163.0                                              
REMARK 620 3 HOH D1215   O    98.5  81.4                                        
REMARK 620 4 THR D 349   O    71.5  91.5  90.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 1003                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1808   RELATED DB: TARGETDB                              
DBREF  2GSE A   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
DBREF  2GSE B   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
DBREF  2GSE C   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
DBREF  2GSE D   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
SEQADV 2GSE MET A  -10  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS A   -9  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS A   -8  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS A   -7  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS A   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS A   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS A   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE SER A   -3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER A   -2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY A   -1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE VAL A    0  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASP A    1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU A    2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY A    3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE THR A    4  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLU A    5  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASN A    6  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU A    7  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE TYR A    8  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE PHE A    9  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLN A   10  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER A   11  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE MET A   12  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE MET B  -10  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS B   -9  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS B   -8  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS B   -7  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS B   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS B   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS B   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE SER B   -3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER B   -2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY B   -1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE VAL B    0  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASP B    1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU B    2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY B    3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE THR B    4  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLU B    5  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASN B    6  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU B    7  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE TYR B    8  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE PHE B    9  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLN B   10  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER B   11  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE MET B   12  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE MET C  -10  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS C   -9  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS C   -8  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS C   -7  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS C   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS C   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS C   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE SER C   -3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER C   -2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY C   -1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE VAL C    0  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASP C    1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU C    2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY C    3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE THR C    4  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLU C    5  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASN C    6  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU C    7  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE TYR C    8  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE PHE C    9  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLN C   10  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER C   11  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE MET C   12  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE MET D  -10  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS D   -9  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS D   -8  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS D   -7  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS D   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS D   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE HIS D   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 2GSE SER D   -3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER D   -2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY D   -1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE VAL D    0  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASP D    1  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU D    2  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLY D    3  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE THR D    4  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLU D    5  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE ASN D    6  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE LEU D    7  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE TYR D    8  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE PHE D    9  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE GLN D   10  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE SER D   11  UNP  Q16555              CLONING ARTIFACT               
SEQADV 2GSE MET D   12  UNP  Q16555              CLONING ARTIFACT               
SEQRES   1 A  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 A  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 A  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 A  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 A  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 A  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 A  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 A  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 A  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 A  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 A  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 A  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 A  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 A  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 A  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 A  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 A  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 A  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 A  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 A  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 A  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 A  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 A  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 A  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 A  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 A  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 A  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 A  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 A  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 A  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 A  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 A  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 A  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 A  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 A  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 A  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 A  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 A  501  ALA ARG SER ARG LEU ALA GLU                                  
SEQRES   1 B  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 B  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 B  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 B  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 B  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 B  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 B  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 B  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 B  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 B  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 B  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 B  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 B  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 B  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 B  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 B  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 B  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 B  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 B  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 B  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 B  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 B  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 B  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 B  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 B  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 B  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 B  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 B  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 B  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 B  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 B  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 B  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 B  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 B  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 B  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 B  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 B  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 B  501  ALA ARG SER ARG LEU ALA GLU                                  
SEQRES   1 C  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 C  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 C  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 C  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 C  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 C  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 C  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 C  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 C  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 C  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 C  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 C  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 C  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 C  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 C  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 C  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 C  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 C  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 C  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 C  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 C  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 C  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 C  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 C  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 C  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 C  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 C  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 C  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 C  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 C  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 C  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 C  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 C  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 C  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 C  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 C  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 C  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 C  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 C  501  ALA ARG SER ARG LEU ALA GLU                                  
SEQRES   1 D  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 D  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 D  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 D  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 D  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 D  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 D  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 D  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 D  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 D  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 D  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 D  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 D  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 D  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 D  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 D  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 D  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 D  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 D  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 D  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 D  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 D  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 D  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 D  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 D  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 D  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 D  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 D  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 D  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 D  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 D  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 D  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 D  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 D  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 D  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 D  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 D  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 D  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 D  501  ALA ARG SER ARG LEU ALA GLU                                  
HET     CA  A1000       1                                                       
HET     CA  B1001       1                                                       
HET     CA  C1002       1                                                       
HET     CA  D1003       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   9  HOH   *849(H2 O)                                                    
HELIX    1   1 ASP A   88  GLY A   99  1                                  12    
HELIX    2   2 SER A  115  SER A  131  1                                  17    
HELIX    3   3 GLY A  147  HIS A  159  1                                  13    
HELIX    4   4 THR A  177  GLY A  192  1                                  16    
HELIX    5   5 ASN A  201  ASP A  214  1                                  14    
HELIX    6   6 PRO A  220  ARG A  227  1                                   8    
HELIX    7   7 PRO A  228  ASN A  247  1                                  20    
HELIX    8   8 SER A  257  LYS A  269  1                                  13    
HELIX    9   9 ILE A  279  THR A  285  1                                   7    
HELIX   10  10 ASP A  286  SER A  292  5                                   7    
HELIX   11  11 ASN A  294  PHE A  301  1                                   8    
HELIX   12  12 THR A  312  CYS A  323  1                                  12    
HELIX   13  13 ASN A  337  ALA A  342  1                                   6    
HELIX   14  14 VAL A  343  LYS A  345  5                                   3    
HELIX   15  15 ASN A  347  ILE A  351  5                                   5    
HELIX   16  16 GLU A  360  VAL A  370  1                                  11    
HELIX   17  17 ASP A  376  SER A  385  1                                  10    
HELIX   18  18 SER A  385  PHE A  392  1                                   8    
HELIX   19  19 PRO A  475  ARG A  487  1                                  13    
HELIX   20  20 ASP B   88  ALA B   98  1                                  11    
HELIX   21  21 SER B  115  SER B  131  1                                  17    
HELIX   22  22 GLY B  147  HIS B  159  1                                  13    
HELIX   23  23 THR B  177  GLY B  192  1                                  16    
HELIX   24  24 ASN B  201  LEU B  215  1                                  15    
HELIX   25  25 PRO B  220  ARG B  227  1                                   8    
HELIX   26  26 PRO B  228  THR B  246  1                                  19    
HELIX   27  27 SER B  257  LYS B  270  1                                  14    
HELIX   28  28 ILE B  279  THR B  285  1                                   7    
HELIX   29  29 ASP B  286  SER B  292  5                                   7    
HELIX   30  30 ASN B  294  ALA B  300  1                                   7    
HELIX   31  31 THR B  312  CYS B  323  1                                  12    
HELIX   32  32 ASN B  337  ALA B  342  1                                   6    
HELIX   33  33 VAL B  343  LYS B  345  5                                   3    
HELIX   34  34 ASN B  347  ILE B  351  5                                   5    
HELIX   35  35 GLU B  360  VAL B  370  1                                  11    
HELIX   36  36 ASP B  376  SER B  385  1                                  10    
HELIX   37  37 SER B  385  PHE B  392  1                                   8    
HELIX   38  38 PRO B  475  ARG B  487  1                                  13    
HELIX   39  39 ASP C   88  GLY C   99  1                                  12    
HELIX   40  40 SER C  115  SER C  131  1                                  17    
HELIX   41  41 GLY C  147  HIS C  159  1                                  13    
HELIX   42  42 THR C  177  ILE C  191  1                                  15    
HELIX   43  43 ASN C  201  LEU C  215  1                                  15    
HELIX   44  44 PRO C  220  ARG C  227  1                                   8    
HELIX   45  45 PRO C  228  ASN C  247  1                                  20    
HELIX   46  46 SER C  257  LYS C  270  1                                  14    
HELIX   47  47 ILE C  279  THR C  285  1                                   7    
HELIX   48  48 ASP C  286  SER C  292  5                                   7    
HELIX   49  49 ASN C  294  PHE C  301  1                                   8    
HELIX   50  50 THR C  312  CYS C  323  1                                  12    
HELIX   51  51 ASN C  337  ALA C  342  1                                   6    
HELIX   52  52 VAL C  343  LYS C  345  5                                   3    
HELIX   53  53 ASN C  347  ILE C  351  5                                   5    
HELIX   54  54 GLU C  360  VAL C  370  1                                  11    
HELIX   55  55 ASP C  376  SER C  385  1                                  10    
HELIX   56  56 SER C  385  ASN C  393  1                                   9    
HELIX   57  57 PRO C  475  ARG C  487  1                                  13    
HELIX   58  58 ASP D   88  GLY D   99  1                                  12    
HELIX   59  59 SER D  115  SER D  131  1                                  17    
HELIX   60  60 GLY D  147  HIS D  159  1                                  13    
HELIX   61  61 THR D  177  GLY D  192  1                                  16    
HELIX   62  62 ASN D  201  ASP D  214  1                                  14    
HELIX   63  63 PRO D  220  SER D  226  1                                   7    
HELIX   64  64 PRO D  228  ASN D  247  1                                  20    
HELIX   65  65 SER D  257  LYS D  270  1                                  14    
HELIX   66  66 ILE D  279  THR D  285  1                                   7    
HELIX   67  67 ASP D  286  SER D  292  5                                   7    
HELIX   68  68 ASN D  294  PHE D  301  1                                   8    
HELIX   69  69 THR D  312  CYS D  323  1                                  12    
HELIX   70  70 ASN D  337  ALA D  342  1                                   6    
HELIX   71  71 VAL D  343  LYS D  345  5                                   3    
HELIX   72  72 ASN D  347  ILE D  351  5                                   5    
HELIX   73  73 GLU D  360  VAL D  370  1                                  11    
HELIX   74  74 ASP D  376  SER D  385  1                                  10    
HELIX   75  75 SER D  385  PHE D  392  1                                   8    
HELIX   76  76 PRO D  475  LEU D  488  1                                  14    
SHEET    1   A 4 LEU A  41  GLY A  46  0                                        
SHEET    2   A 4 SER A  30  GLU A  38 -1  N  TYR A  36   O  LYS A  43           
SHEET    3   A 4 LEU A  17  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4   A 4 LYS A  56  GLU A  59  1  O  ILE A  58   N  LYS A  20           
SHEET    1   B 8 LEU A  41  GLY A  46  0                                        
SHEET    2   B 8 SER A  30  GLU A  38 -1  N  TYR A  36   O  LYS A  43           
SHEET    3   B 8 LEU A  17  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4   B 8 MET A  64  PRO A  67  1  O  VAL A  65   N  VAL A  25           
SHEET    5   B 8 LEU A 409  THR A 419 -1  O  VAL A 410   N  ILE A  66           
SHEET    6   B 8 GLU A 438  SER A 448 -1  O  LEU A 444   N  ILE A 411           
SHEET    7   B 8 LYS A 451  GLU A 455 -1  O  VAL A 453   N  VAL A 446           
SHEET    8   B 8 THR A 458  LEU A 459 -1  O  THR A 458   N  GLU A 455           
SHEET    1   C 7 GLY A  69  THR A  74  0                                        
SHEET    2   C 7 THR A 101  VAL A 108  1  O  MET A 103   N  ASP A  71           
SHEET    3   C 7 ASP A 134  ILE A 141  1  O  HIS A 138   N  VAL A 108           
SHEET    4   C 7 SER A 163  TYR A 167  1  O  LEU A 165   N  ILE A 141           
SHEET    5   C 7 ILE A 194  HIS A 198  1  O  GLN A 196   N  PHE A 164           
SHEET    6   C 7 LEU A 250  VAL A 255  1  O  TYR A 251   N  ALA A 195           
SHEET    7   C 7 VAL A 274  PRO A 278  1  O  TYR A 275   N  ILE A 252           
SHEET    1   D 2 PRO A  79  ASP A  80  0                                        
SHEET    2   D 2 MET A  83  THR A  84 -1  O  MET A  83   N  ASP A  80           
SHEET    1   E 4 LEU B  41  GLY B  46  0                                        
SHEET    2   E 4 SER B  30  GLU B  38 -1  N  TYR B  36   O  LYS B  43           
SHEET    3   E 4 LEU B  17  VAL B  25 -1  N  LEU B  17   O  MET B  37           
SHEET    4   E 4 LYS B  56  GLU B  59  1  O  ILE B  58   N  LEU B  18           
SHEET    1   F 8 LEU B  41  GLY B  46  0                                        
SHEET    2   F 8 SER B  30  GLU B  38 -1  N  TYR B  36   O  LYS B  43           
SHEET    3   F 8 LEU B  17  VAL B  25 -1  N  LEU B  17   O  MET B  37           
SHEET    4   F 8 MET B  64  PRO B  67  1  O  VAL B  65   N  VAL B  25           
SHEET    5   F 8 LEU B 409  THR B 419 -1  O  VAL B 410   N  ILE B  66           
SHEET    6   F 8 GLU B 438  SER B 448 -1  O  LEU B 444   N  ILE B 411           
SHEET    7   F 8 LYS B 451  GLU B 455 -1  O  LYS B 451   N  SER B 448           
SHEET    8   F 8 THR B 458  LEU B 459 -1  O  THR B 458   N  GLU B 455           
SHEET    1   G 7 GLY B  69  THR B  74  0                                        
SHEET    2   G 7 THR B 101  VAL B 108  1  O  MET B 103   N  ASP B  71           
SHEET    3   G 7 ASP B 134  ILE B 141  1  O  HIS B 138   N  ASP B 106           
SHEET    4   G 7 SER B 163  TYR B 167  1  O  LEU B 165   N  ILE B 141           
SHEET    5   G 7 ILE B 194  HIS B 198  1  O  GLN B 196   N  PHE B 164           
SHEET    6   G 7 LEU B 250  VAL B 255  1  O  TYR B 251   N  ALA B 195           
SHEET    7   G 7 VAL B 274  PRO B 278  1  O  TYR B 275   N  ILE B 252           
SHEET    1   H 2 PRO B  79  ASP B  80  0                                        
SHEET    2   H 2 MET B  83  THR B  84 -1  O  MET B  83   N  ASP B  80           
SHEET    1   I 4 LEU C  41  GLY C  46  0                                        
SHEET    2   I 4 SER C  30  GLU C  38 -1  N  TYR C  36   O  GLN C  44           
SHEET    3   I 4 LEU C  17  VAL C  25 -1  N  ILE C  24   O  PHE C  31           
SHEET    4   I 4 THR C  57  GLU C  59  1  O  ILE C  58   N  LYS C  20           
SHEET    1   J 8 LEU C  41  GLY C  46  0                                        
SHEET    2   J 8 SER C  30  GLU C  38 -1  N  TYR C  36   O  GLN C  44           
SHEET    3   J 8 LEU C  17  VAL C  25 -1  N  ILE C  24   O  PHE C  31           
SHEET    4   J 8 MET C  64  PRO C  67  1  O  VAL C  65   N  VAL C  25           
SHEET    5   J 8 LEU C 409  THR C 419 -1  O  TRP C 412   N  MET C  64           
SHEET    6   J 8 GLU C 438  SER C 448 -1  O  ILE C 447   N  LEU C 409           
SHEET    7   J 8 LYS C 451  GLU C 455 -1  O  LYS C 451   N  SER C 448           
SHEET    8   J 8 THR C 458  LEU C 459 -1  O  THR C 458   N  GLU C 455           
SHEET    1   K 7 GLY C  69  THR C  74  0                                        
SHEET    2   K 7 THR C 101  VAL C 108  1  O  MET C 103   N  ASP C  71           
SHEET    3   K 7 TYR C 135  ASP C 140  1  O  HIS C 138   N  ASP C 106           
SHEET    4   K 7 SER C 163  TYR C 167  1  O  SER C 163   N  VAL C 139           
SHEET    5   K 7 ILE C 194  HIS C 198  1  O  GLN C 196   N  PHE C 164           
SHEET    6   K 7 LEU C 250  VAL C 255  1  O  THR C 253   N  VAL C 197           
SHEET    7   K 7 VAL C 274  PRO C 278  1  O  TYR C 275   N  ILE C 252           
SHEET    1   L 2 PRO C  79  ASP C  80  0                                        
SHEET    2   L 2 MET C  83  THR C  84 -1  O  MET C  83   N  ASP C  80           
SHEET    1   M 4 LEU D  41  GLY D  46  0                                        
SHEET    2   M 4 SER D  30  GLU D  38 -1  N  ASP D  34   O  GLY D  46           
SHEET    3   M 4 LEU D  17  VAL D  25 -1  N  LEU D  17   O  MET D  37           
SHEET    4   M 4 THR D  57  GLU D  59  1  O  ILE D  58   N  LYS D  20           
SHEET    1   N 8 LEU D  41  GLY D  46  0                                        
SHEET    2   N 8 SER D  30  GLU D  38 -1  N  ASP D  34   O  GLY D  46           
SHEET    3   N 8 LEU D  17  VAL D  25 -1  N  LEU D  17   O  MET D  37           
SHEET    4   N 8 MET D  64  PRO D  67  1  O  VAL D  65   N  VAL D  25           
SHEET    5   N 8 LEU D 409  THR D 419 -1  O  VAL D 410   N  ILE D  66           
SHEET    6   N 8 GLU D 438  SER D 448 -1  O  SER D 442   N  ASP D 413           
SHEET    7   N 8 LYS D 451  GLU D 455 -1  O  VAL D 453   N  VAL D 446           
SHEET    8   N 8 THR D 458  LEU D 459 -1  O  THR D 458   N  GLU D 455           
SHEET    1   O 7 GLY D  69  THR D  74  0                                        
SHEET    2   O 7 THR D 101  VAL D 108  1  O  MET D 103   N  ASP D  71           
SHEET    3   O 7 ASP D 134  ILE D 141  1  O  HIS D 138   N  ASP D 106           
SHEET    4   O 7 SER D 163  TYR D 167  1  O  LEU D 165   N  ILE D 141           
SHEET    5   O 7 ILE D 194  HIS D 198  1  O  GLN D 196   N  PHE D 164           
SHEET    6   O 7 LEU D 250  VAL D 255  1  O  TYR D 251   N  ALA D 195           
SHEET    7   O 7 VAL D 274  PRO D 278  1  O  TYR D 275   N  ILE D 252           
SHEET    1   P 2 PRO D  79  ASP D  80  0                                        
SHEET    2   P 2 MET D  83  THR D  84 -1  O  MET D  83   N  ASP D  80           
LINK        CA    CA A1000                 O   HOH A1089     1555   1555  3.07  
LINK        CA    CA A1000                 O   HOH A1215     1555   1555  2.37  
LINK        CA    CA A1000                 O   THR A 349     1555   1555  2.21  
LINK        CA    CA A1000                 O   HOH A1202     1555   1555  2.60  
LINK        CA    CA B1001                 O   THR B 349     1555   1555  2.36  
LINK        CA    CA B1001                 O   HOH B1061     1555   1555  2.47  
LINK        CA    CA B1001                 O   HOH B1099     1555   1555  3.01  
LINK        CA    CA B1001                 O   HOH B1141     1555   1555  2.81  
LINK        CA    CA B1001                 O   HOH B1175     1555   1555  2.42  
LINK        CA    CA B1001                 O   HOH B1178     1555   1555  2.38  
LINK        CA    CA C1002                 O   THR C 349     1555   1555  2.28  
LINK        CA    CA C1002                 O   HOH C1122     1555   1555  2.48  
LINK        CA    CA C1002                 O   HOH C1206     1555   1555  2.20  
LINK        CA    CA C1002                 O   HOH C1222     1555   1555  2.45  
LINK        CA    CA D1003                 O   HOH D1089     1555   1555  3.32  
LINK        CA    CA D1003                 O   HOH D1158     1555   1555  2.63  
LINK        CA    CA D1003                 O   HOH D1215     1555   1555  2.21  
LINK        CA    CA D1003                 O   THR D 349     1555   1555  2.12  
CISPEP   1 SER A  304    PRO A  305          0        -4.01                     
CISPEP   2 TYR A  395    PRO A  396          0        -4.08                     
CISPEP   3 SER B  304    PRO B  305          0         3.30                     
CISPEP   4 TYR B  395    PRO B  396          0         3.13                     
CISPEP   5 SER C  304    PRO C  305          0        -5.73                     
CISPEP   6 TYR C  395    PRO C  396          0         5.77                     
CISPEP   7 SER D  304    PRO D  305          0        -4.31                     
CISPEP   8 TYR D  395    PRO D  396          0         1.76                     
SITE     1 AC1  5 GLN A  81  THR A 349  HOH A1089  HOH A1202                    
SITE     2 AC1  5 HOH A1215                                                     
SITE     1 AC2  6 THR B 349  HOH B1061  HOH B1099  HOH B1141                    
SITE     2 AC2  6 HOH B1175  HOH B1178                                          
SITE     1 AC3  4 THR C 349  HOH C1122  HOH C1206  HOH C1222                    
SITE     1 AC4  3 THR D 349  HOH D1158  HOH D1215                               
CRYST1   86.400  126.100  102.900  90.00 113.00  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      0.011574  0.000000  0.004913        0.00000                         
SCALE2      0.000000  0.007930  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010557        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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