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Database: PDB
Entry: 6DEE
LinkDB: 6DEE
Original site: 6DEE 
HEADER    ENDOCYTOSIS                             11-MAY-18   6DEE              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINUS OF HOMO SAPIENS SPIN90 (SH3-      
TITLE    2 PROTEIN INTERACTING WITH NCK), RESIDUES 306-722                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NCK-INTERACTING PROTEIN WITH SH3 DOMAIN;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 306-722;                                      
COMPND   5 SYNONYM: 54 KDA VACA-INTERACTING PROTEIN, 54 KDA VIMENTIN-INTERACTING
COMPND   6 PROTEIN, VIP54, 90 KDA SH3 PROTEIN INTERACTING WITH NCK, AF3P21, DIA-
COMPND   7 INTERACTING PROTEIN 1, DIP-1, DIAPHANOUS PROTEIN-INTERACTING PROTEIN,
COMPND   8 SH3 ADAPTER PROTEIN SPIN90, WASP-INTERACTING SH3-DOMAIN PROTEIN,     
COMPND   9 WISH, WISKOTT-ALDRICH SYNDROME PROTEIN-INTERACTING PROTEIN;          
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NCKIPSD, AF3P21, SPIN90;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGV67                                     
KEYWDS    PARTIALLY ACTIVE FORM, N-TERMINALLY TRUNCATED SPIN90, 6 AND HALF      
KEYWDS   2 ARMADILLO REPEATS, PART OF MIDDLE SEGMENT, ACTIVATES ARP2-3 COMPLEX, 
KEYWDS   3 NOT FULL ACTIVITY, ENDOCYTOSIS                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.NOLEN,Q.LUAN                                                      
REVDAT   4   01-JAN-20 6DEE    1       REMARK                                   
REVDAT   3   28-NOV-18 6DEE    1       JRNL                                     
REVDAT   2   31-OCT-18 6DEE    1       JRNL                                     
REVDAT   1   24-OCT-18 6DEE    0                                                
JRNL        AUTH   Q.LUAN,S.L.LIU,L.A.HELGESON,B.J.NOLEN                        
JRNL        TITL   STRUCTURE OF THE NUCLEATION-PROMOTING FACTOR SPIN90 BOUND TO 
JRNL        TITL 2 THE ACTIN FILAMENT NUCLEATOR ARP2/3 COMPLEX.                 
JRNL        REF    EMBO J.                       V.  37       2018              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   30322896                                                     
JRNL        DOI    10.15252/EMBJ.2018100005                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 8212                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.264                           
REMARK   3   R VALUE            (WORKING SET) : 0.259                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.010                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 822                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.1998 -  5.4968    0.98     1302   145  0.2300 0.2611        
REMARK   3     2  5.4968 -  4.3644    1.00     1250   139  0.2706 0.2839        
REMARK   3     3  4.3644 -  3.8132    1.00     1234   137  0.2535 0.3287        
REMARK   3     4  3.8132 -  3.4647    1.00     1212   135  0.2787 0.3460        
REMARK   3     5  3.4647 -  3.2165    1.00     1217   135  0.3100 0.4257        
REMARK   3     6  3.2165 -  3.0269    0.98     1175   131  0.3349 0.4238        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.520            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           2603                                  
REMARK   3   ANGLE     :  0.513           3555                                  
REMARK   3   CHIRALITY :  0.018            455                                  
REMARK   3   PLANARITY :  0.002            460                                  
REMARK   3   DIHEDRAL  : 10.469            829                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6DEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234281.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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) : 0.9791829                          
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : SAGITTAL FOCUSING 2ND CRYSTAL      
REMARK 200                                   HORIZONTAL FOCUSING                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000 2.3.6                     
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000 2.3.6                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8213                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: PDB ENTRY 6DED                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES, PH 6, 100 MM MAGNESIUM        
REMARK 280  SULFATE, 1.5% PEG6000, PH 6.0, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       40.90600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       49.25200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       49.25200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.45300            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       49.25200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       49.25200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.35900            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       49.25200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.25200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       20.45300            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       49.25200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.25200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.35900            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       40.90600            
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 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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     GLU A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     LYS A   364                                                      
REMARK 465     ASP A   365                                                      
REMARK 465     LEU A   366                                                      
REMARK 465     SER A   367                                                      
REMARK 465     MET A   368                                                      
REMARK 465     ALA A   369                                                      
REMARK 465     LEU A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     SER A   372                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     GLN A   374                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     ASP A   394                                                      
REMARK 465     ASP A   395                                                      
REMARK 465     ALA A   396                                                      
REMARK 465     GLN A   397                                                      
REMARK 465     GLN A   398                                                      
REMARK 465     ARG A   399                                                      
REMARK 465     LEU A   544                                                      
REMARK 465     ASP A   545                                                      
REMARK 465     THR A   546                                                      
REMARK 465     PHE A   714                                                      
REMARK 465     LEU A   715                                                      
REMARK 465     VAL A   716                                                      
REMARK 465     LEU A   717                                                      
REMARK 465     GLY A   718                                                      
REMARK 465     GLU A   719                                                      
REMARK 465     ALA A   720                                                      
REMARK 465     PRO A   721                                                      
REMARK 465     SER A   722                                                      
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     VAL A 308    CG1  CG2                                            
REMARK 470     PRO A 309    CG   CD                                             
REMARK 470     ARG A 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 311    OG1  CG2                                            
REMARK 470     ILE A 312    CG1  CG2  CD1                                       
REMARK 470     GLU A 315    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 322    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 324    OG1  CG2                                            
REMARK 470     GLU A 329    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 330    CG   CD1  CD2                                       
REMARK 470     SER A 345    OG                                                  
REMARK 470     VAL A 346    CG1  CG2                                            
REMARK 470     PRO A 347    CG   CD                                             
REMARK 470     SER A 349    OG                                                  
REMARK 470     VAL A 352    CG1  CG2                                            
REMARK 470     GLU A 354    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 356    CG1  CG2                                            
REMARK 470     LEU A 358    CG   CD1  CD2                                       
REMARK 470     SER A 359    OG                                                  
REMARK 470     VAL A 361    CG1  CG2                                            
REMARK 470     VAL A 375    CG1  CG2                                            
REMARK 470     ASP A 388    CG   OD1  OD2                                       
REMARK 470     ARG A 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 400    OG                                                  
REMARK 470     TRP A 401    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 401    CZ3  CH2                                            
REMARK 470     TYR A 404    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 406    CG   OD1  OD2                                       
REMARK 470     GLU A 407    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 431    CG   CD   CE   NZ                                   
REMARK 470     ASN A 436    CG   OD1  ND2                                       
REMARK 470     GLU A 437    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 439    CG   CD   OE1  OE2                                  
REMARK 470     SER A 469    OG                                                  
REMARK 470     SER A 476    OG                                                  
REMARK 470     HIS A 498    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 513    OG                                                  
REMARK 470     MET A 514    CG   SD   CE                                        
REMARK 470     GLU A 516    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 519    CG   CD                                             
REMARK 470     HIS A 522    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A 523    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 524    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 525    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 526    CG   CD1  CD2                                       
REMARK 470     THR A 528    OG1  CG2                                            
REMARK 470     PRO A 529    CG   CD                                             
REMARK 470     GLN A 532    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 535    CG   CD1  CD2                                       
REMARK 470     ASN A 536    CG   OD1  ND2                                       
REMARK 470     GLU A 539    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 540    CG   OD1  OD2                                       
REMARK 470     THR A 547    OG1  CG2                                            
REMARK 470     GLU A 548    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 550    CG   CD1  CD2                                       
REMARK 470     PRO A 551    CG   CD                                             
REMARK 470     ASP A 552    CG   OD1  OD2                                       
REMARK 470     CYS A 554    SG                                                  
REMARK 470     LEU A 563    CG   CD1  CD2                                       
REMARK 470     PRO A 566    CG   CD                                             
REMARK 470     ASP A 569    CG   OD1  OD2                                       
REMARK 470     GLN A 570    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 572    CG1  CG2                                            
REMARK 470     SER A 578    OG                                                  
REMARK 470     LYS A 579    CG   CD   CE   NZ                                   
REMARK 470     ASN A 582    CG   OD1  ND2                                       
REMARK 470     VAL A 583    CG1  CG2                                            
REMARK 470     ILE A 585    CG1  CG2  CD1                                       
REMARK 470     SER A 587    OG                                                  
REMARK 470     LYS A 589    CG   CD   CE   NZ                                   
REMARK 470     LEU A 591    CG   CD1  CD2                                       
REMARK 470     LEU A 592    CG   CD1  CD2                                       
REMARK 470     LEU A 593    CG   CD1  CD2                                       
REMARK 470     ARG A 596    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 598    CG   OD1  OD2                                       
REMARK 470     PRO A 600    CG   CD                                             
REMARK 470     VAL A 601    CG1  CG2                                            
REMARK 470     ARG A 602    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 603    CG1  CG2  CD1                                       
REMARK 470     PHE A 604    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 605    CG   CD   CE   NZ                                   
REMARK 470     HIS A 606    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 607    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 608    CG   CD                                             
REMARK 470     GLN A 609    CG   CD   OE1  NE2                                  
REMARK 470     PRO A 610    CG   CD                                             
REMARK 470     PRO A 611    CG   CD                                             
REMARK 470     ASP A 649    CG   OD1  OD2                                       
REMARK 470     LEU A 650    CG   CD1  CD2                                       
REMARK 470     SER A 651    OG                                                  
REMARK 470     PRO A 652    CG   CD                                             
REMARK 470     ASP A 654    CG   OD1  OD2                                       
REMARK 470     LYS A 655    CG   CD   CE   NZ                                   
REMARK 470     LEU A 656    CG   CD1  CD2                                       
REMARK 470     ARG A 657    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 659    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 661    CG   CD1  CD2                                       
REMARK 470     SER A 662    OG                                                  
REMARK 470     MET A 664    CG   SD   CE                                        
REMARK 470     HIS A 665    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A 667    CG1  CG2  CD1                                       
REMARK 470     ARG A 669    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 670    OG1  CG2                                            
REMARK 470     THR A 671    OG1  CG2                                            
REMARK 470     TYR A 673    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 674    CG   CD1  CD2                                       
REMARK 470     HIS A 676    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 677    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 678    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 679    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 682    CG   OD1  OD2                                       
REMARK 470     LEU A 683    CG   CD1  CD2                                       
REMARK 470     ILE A 686    CG1  CG2  CD1                                       
REMARK 470     ARG A 688    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 689    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 690    CG1  CG2  CD1                                       
REMARK 470     LEU A 691    CG   CD1  CD2                                       
REMARK 470     ASN A 692    CG   OD1  ND2                                       
REMARK 470     GLU A 693    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 694    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 695    CG   CD   OE1  OE2                                  
REMARK 470     THR A 696    OG1  CG2                                            
REMARK 470     SER A 697    OG                                                  
REMARK 470     PRO A 698    CG   CD                                             
REMARK 470     GLN A 699    CG   CD   OE1  NE2                                  
REMARK 470     CYS A 700    SG                                                  
REMARK 470     MET A 702    CG   SD   CE                                        
REMARK 470     ASP A 703    CG   OD1  OD2                                       
REMARK 470     ARG A 704    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 706    CG1  CG2  CD1                                       
REMARK 470     VAL A 707    CG1  CG2                                            
REMARK 470     GLU A 709    CG   CD   OE1  OE2                                  
REMARK 470     MET A 710    CG   SD   CE                                        
REMARK 470     CYS A 711    SG                                                  
REMARK 470     LYS A 712    CG   CD   CE   NZ                                   
REMARK 470     GLU A 713    CG   CD   OE1  OE2                                  
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    PRO A 347   N   -  CA  -  CB  ANGL. DEV. =   7.3 DEGREES          
REMARK 500    PRO A 519   N   -  CA  -  CB  ANGL. DEV. =   7.3 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    SER A 481     -169.41    -76.08                                   
REMARK 500    PRO A 566     -179.28    -67.42                                   
REMARK 500    ALA A 568      -51.59   -128.59                                   
REMARK 500    LYS A 712       73.37   -112.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6DEE A  306   722  UNP    Q9NZQ3   SPN90_HUMAN    306    722             
SEQADV 6DEE SER A  305  UNP  Q9NZQ3              EXPRESSION TAG                 
SEQRES   1 A  418  SER ALA ALA VAL PRO ARG THR ILE GLY ALA GLU LEU MET          
SEQRES   2 A  418  GLU LEU VAL ARG ARG ASN THR GLY LEU SER HIS GLU LEU          
SEQRES   3 A  418  CYS ARG VAL ALA ILE GLY ILE ILE VAL GLY HIS ILE GLN          
SEQRES   4 A  418  ALA SER VAL PRO ALA SER SER PRO VAL MET GLU GLN VAL          
SEQRES   5 A  418  LEU LEU SER LEU VAL GLU GLY LYS ASP LEU SER MET ALA          
SEQRES   6 A  418  LEU PRO SER GLY GLN VAL CYS HIS ASP GLN GLN ARG LEU          
SEQRES   7 A  418  GLU VAL ILE PHE ALA ASP LEU ALA ARG ARG LYS ASP ASP          
SEQRES   8 A  418  ALA GLN GLN ARG SER TRP ALA LEU TYR GLU ASP GLU GLY          
SEQRES   9 A  418  VAL ILE ARG CYS TYR LEU GLU GLU LEU LEU HIS ILE LEU          
SEQRES  10 A  418  THR ASP ALA ASP PRO GLU VAL CYS LYS LYS MET CYS LYS          
SEQRES  11 A  418  ARG ASN GLU PHE GLU SER VAL LEU ALA LEU VAL ALA TYR          
SEQRES  12 A  418  TYR GLN MET GLU HIS ARG ALA SER LEU ARG LEU LEU LEU          
SEQRES  13 A  418  LEU LYS CYS PHE GLY ALA MET CYS SER LEU ASP ALA ALA          
SEQRES  14 A  418  ILE ILE SER THR LEU VAL SER SER VAL LEU PRO VAL GLU          
SEQRES  15 A  418  LEU ALA ARG ASP MET GLN THR ASP THR GLN ASP HIS GLN          
SEQRES  16 A  418  LYS LEU CYS TYR SER ALA LEU ILE LEU ALA MET VAL PHE          
SEQRES  17 A  418  SER MET GLY GLU ALA VAL PRO TYR ALA HIS TYR GLU HIS          
SEQRES  18 A  418  LEU GLY THR PRO PHE ALA GLN PHE LEU LEU ASN ILE VAL          
SEQRES  19 A  418  GLU ASP GLY LEU PRO LEU ASP THR THR GLU GLN LEU PRO          
SEQRES  20 A  418  ASP LEU CYS VAL ASN LEU LEU LEU ALA LEU ASN LEU HIS          
SEQRES  21 A  418  LEU PRO ALA ALA ASP GLN ASN VAL ILE MET ALA ALA LEU          
SEQRES  22 A  418  SER LYS HIS ALA ASN VAL LYS ILE PHE SER GLU LYS LEU          
SEQRES  23 A  418  LEU LEU LEU LEU ASN ARG GLY ASP ASP PRO VAL ARG ILE          
SEQRES  24 A  418  PHE LYS HIS GLU PRO GLN PRO PRO HIS SER VAL LEU LYS          
SEQRES  25 A  418  PHE LEU GLN ASP VAL PHE GLY SER PRO ALA THR ALA ALA          
SEQRES  26 A  418  ILE PHE TYR HIS THR ASP MET MET ALA LEU ILE ASP ILE          
SEQRES  27 A  418  THR VAL ARG HIS ILE ALA ASP LEU SER PRO GLY ASP LYS          
SEQRES  28 A  418  LEU ARG MET GLU TYR LEU SER LEU MET HIS ALA ILE VAL          
SEQRES  29 A  418  ARG THR THR PRO TYR LEU GLN HIS ARG HIS ARG LEU PRO          
SEQRES  30 A  418  ASP LEU GLN ALA ILE LEU ARG ARG ILE LEU ASN GLU GLU          
SEQRES  31 A  418  GLU THR SER PRO GLN CYS GLN MET ASP ARG MET ILE VAL          
SEQRES  32 A  418  ARG GLU MET CYS LYS GLU PHE LEU VAL LEU GLY GLU ALA          
SEQRES  33 A  418  PRO SER                                                      
HELIX    1 AA1 THR A  311  GLY A  325  1                                  15    
HELIX    2 AA2 SER A  327  VAL A  346  1                                  20    
HELIX    3 AA3 SER A  349  LEU A  360  1                                  12    
HELIX    4 AA4 CYS A  376  ALA A  390  1                                  15    
HELIX    5 AA5 ARG A  391  ARG A  391  5                                   1    
HELIX    6 AA6 SER A  400  GLU A  405  5                                   6    
HELIX    7 AA7 ASP A  406  ALA A  424  1                                  19    
HELIX    8 AA8 ASP A  425  LYS A  434  1                                  10    
HELIX    9 AA9 PHE A  438  GLU A  451  1                                  14    
HELIX   10 AB1 ARG A  453  SER A  469  1                                  17    
HELIX   11 AB2 ASP A  471  SER A  481  1                                  11    
HELIX   12 AB3 VAL A  482  ASP A  494  1                                  13    
HELIX   13 AB4 ASP A  497  PHE A  512  1                                  16    
HELIX   14 AB5 PRO A  519  GLU A  524  1                                   6    
HELIX   15 AB6 GLY A  527  ASP A  540  1                                  14    
HELIX   16 AB7 LEU A  550  ASN A  562  1                                  13    
HELIX   17 AB8 ASN A  571  HIS A  580  1                                  10    
HELIX   18 AB9 VAL A  583  GLY A  597  1                                  15    
HELIX   19 AC1 HIS A  612  PHE A  622  1                                  11    
HELIX   20 AC2 SER A  624  ALA A  629  1                                   6    
HELIX   21 AC3 TYR A  632  LEU A  650  1                                  19    
HELIX   22 AC4 LEU A  656  THR A  671  1                                  16    
HELIX   23 AC5 PRO A  672  ARG A  677  1                                   6    
HELIX   24 AC6 LEU A  680  ASN A  692  1                                  13    
HELIX   25 AC7 SER A  697  CYS A  711  1                                  15    
CRYST1   98.504   98.504   81.812  90.00  90.00  90.00 P 41 21 2     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      0.010152  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010152  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012223        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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