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Database: PDB
Entry: 1UX6
LinkDB: 1UX6
Original site: 1UX6 
HEADER    CELL ADHESION                           19-FEB-04   1UX6              
TITLE     STRUCTURE OF A THROMBOSPONDIN C-TERMINAL FRAGMENT REVEALS A NOVEL     
TITLE    2 CALCIUM CORE IN THE TYPE 3 REPEATS                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBOSPONDIN-1;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 831-1170;                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: 293-EBNA;                               
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PCEP-PU                                    
KEYWDS    EXTRACELLULAR MATRIX, CALCIUM BINDING, L-TYPE LECTIN, GLYCOPROTEIN,   
KEYWDS   2 CELL ADHESION, CALCIUM-BINDING, HEPARIN-BINDING, EGF-LIKE DOMAIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KVANSAKUL,J.C.ADAMS,E.HOHENESTER                                    
REVDAT   4   12-JUL-17 1UX6    1                                                
REVDAT   3   24-FEB-09 1UX6    1       VERSN                                    
REVDAT   2   15-JUN-05 1UX6    1       JRNL                                     
REVDAT   1   18-MAR-04 1UX6    0                                                
JRNL        AUTH   M.KVANSAKUL,J.C.ADAMS,E.HOHENESTER                           
JRNL        TITL   STRUCTURE OF A THROMBOSPONDIN C-TERMINAL FRAGMENT REVEALS A  
JRNL        TITL 2 NOVEL CALCIUM CORE IN THE TYPE 3 REPEATS                     
JRNL        REF    EMBO J.                       V.  23  1223 2004              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   15014436                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600166                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28902                          
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 SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3197                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 50                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 569                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 60                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2667                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 262                                     
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) : -2.18000                                             
REMARK   3    B22 (A**2) : -2.18000                                             
REMARK   3    B33 (A**2) : 4.36000                                              
REMARK   3    B12 (A**2) : -2.14000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.160 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.870 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.760 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.720 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 58.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-FEB-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290014608.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32099                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       81.17000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.86352            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       28.38000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       81.17000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       46.86352            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       28.38000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       81.17000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       46.86352            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       28.38000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       81.17000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       46.86352            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       28.38000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       81.17000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       46.86352            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       28.38000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       81.17000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       46.86352            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       28.38000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       93.72704            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       56.76000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       93.72704            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       56.76000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       93.72704            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       56.76000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       93.72704            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       56.76000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       93.72704            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       56.76000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       93.72704            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       56.76000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2341  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2359  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED MUTATION A  992 CYS TO SER                                
REMARK 400  ENGINEERED MUTATION A 1067 ASN TO LYS                               
REMARK 400                                                                      
REMARK 400  ADHESIVE GLYCOPROTEIN MEDIATES CELL-CELL AND CELL-MATRIX            
REMARK 400  INTERACTIONS. BINDS TO FIBRINOGEN, FIBRONECTIN,                     
REMARK 400  LAMININ, TYPE V COLLAGEN AND INTEGRINS ALPHA-V/BETA-1, ALPHA-       
REMARK 400  V/BETA-3 AND ALPHA-IIB/BETA-3.                                      
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     ALA A   803                                                      
REMARK 465     PRO A   804                                                      
REMARK 465     LEU A   805                                                      
REMARK 465     VAL A   806                                                      
REMARK 465     HIS A   807                                                      
REMARK 465     HIS A   808                                                      
REMARK 465     HIS A   809                                                      
REMARK 465     HIS A   810                                                      
REMARK 465     HIS A   811                                                      
REMARK 465     HIS A   812                                                      
REMARK 465     ARG A   962                                                      
REMARK 465     HIS A   963                                                      
REMARK 465     GLN A   964                                                      
REMARK 465     GLY A   965                                                      
REMARK 465     LYS A   966                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A 1146   CD   CE   NZ                                        
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 929   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 816      -51.73   -164.88                                   
REMARK 500    ASP A 828       71.18   -154.23                                   
REMARK 500    ASN A 841       10.50     57.63                                   
REMARK 500    CYS A 856       72.58   -151.47                                   
REMARK 500    ASN A 861       75.95   -161.95                                   
REMARK 500    ASN A 897       73.94   -164.03                                   
REMARK 500    GLN A 900       29.27     49.54                                   
REMARK 500    PHE A 939       45.26    -72.04                                   
REMARK 500    LYS A 950      -65.02   -104.61                                   
REMARK 500    ASN A 986      -99.51   -101.03                                   
REMARK 500    THR A 998      154.23    177.96                                   
REMARK 500    ASP A1001      169.55     68.71                                   
REMARK 500    ASP A1002       44.52   -148.60                                   
REMARK 500    ASP A1003     -140.72   -103.55                                   
REMARK 500    GLN A1071      -68.85   -135.15                                   
REMARK 500    PHE A1087       50.21     39.60                                   
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 A2012  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 828   OD1                                                    
REMARK 620 2 ASP A 830   OD1  88.4                                              
REMARK 620 3 ASP A 832   OD1  86.4  83.9                                        
REMARK 620 4 ILE A 834   O    87.6 175.9  96.2                                  
REMARK 620 5 ASP A 839   OD2 171.4  85.5  86.9  98.6                            
REMARK 620 6 HOH A2110   O    99.2  80.9 163.6  99.4  85.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2011  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 830   OD2                                                    
REMARK 620 2 ASP A 832   OD2  92.7                                              
REMARK 620 3 ASP A 839   OD1 112.4 118.1                                        
REMARK 620 4 ASP A 839   OD2  84.0  76.2  53.4                                  
REMARK 620 5 ASN A 841   OD1  89.4 158.6  80.3 125.2                            
REMARK 620 6 HOH A2241   O   174.2  84.6  73.3 100.3  91.3                      
REMARK 620 7 HOH A2183   O    86.7  88.9 144.6 162.0  70.0  88.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2010  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 843   OD1                                                    
REMARK 620 2 ASP A 845   OD1  79.8                                              
REMARK 620 3 ASP A 847   OD1  92.4  82.7                                        
REMARK 620 4 HIS A 849   O    87.1 166.7  95.9                                  
REMARK 620 5 ASP A 854   OD2 174.8 101.5  82.8  91.3                            
REMARK 620 6 HOH A2122   O    97.7  82.1 159.9 101.9  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2009  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 845   OD2                                                    
REMARK 620 2 ASP A 847   OD2  88.2                                              
REMARK 620 3 ASP A 854   OD1 130.0 107.0                                        
REMARK 620 4 ASP A 854   OD2  88.4  81.6  49.4                                  
REMARK 620 5 CYS A 856   O    87.6 172.0  70.9  91.5                            
REMARK 620 6 VAL A 859   O    80.3 108.8 133.2 164.1  77.1                      
REMARK 620 7 ASN A 861   OD1 150.6  83.2  79.3 117.8 103.7  76.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 866   OD1                                                    
REMARK 620 2 ASP A 868   OD1  78.9                                              
REMARK 620 3 ASP A 870   OD1  95.3  77.4                                        
REMARK 620 4 LYS A 872   O    89.9 161.3  88.9                                  
REMARK 620 5 ASP A 877   OD2 178.4 102.3  86.0  89.2                            
REMARK 620 6 HOH A2118   O    89.7  84.2 159.6 111.0  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 868   OD2                                                    
REMARK 620 2 ASP A 870   OD2  78.0                                              
REMARK 620 3 ASP A 877   OD1 126.9 116.8                                        
REMARK 620 4 ASP A 877   OD2  88.7  77.9  51.1                                  
REMARK 620 5 ASP A 879   O    80.5 158.2  74.2  98.3                            
REMARK 620 6 ASN A 882   OD1  82.1  92.6 140.9 168.0  87.8                      
REMARK 620 7 HOH A2294   O   159.4  93.8  73.7 108.2 107.6  79.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 874   O                                                      
REMARK 620 2 ASP A 877   O    91.1                                              
REMARK 620 3 ASP A 880   OD1  84.8  85.8                                        
REMARK 620 4 ASP A 880   OD2 101.1 132.3  50.4                                  
REMARK 620 5 ASP A 887   OD2 177.2  88.4  92.4  77.2                            
REMARK 620 6 HOH A2280   O    90.0  75.6 160.5 149.0  92.6                      
REMARK 620 7 HOH A2142   O    89.7 162.9 111.2  64.0  91.6  87.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 879   OD1                                                    
REMARK 620 2 ASP A 881   OD1  82.5                                              
REMARK 620 3 ASP A 883   OD1  92.6  78.7                                        
REMARK 620 4 ILE A 885   O    87.0 167.3  94.8                                  
REMARK 620 5 ASP A 890   OD2 177.3  94.9  87.3  95.7                            
REMARK 620 6 HOH A2136   O    96.3  84.5 159.8 103.7  83.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 881   OD2                                                    
REMARK 620 2 ASP A 883   OD2  85.9                                              
REMARK 620 3 ASP A 890   OD1 134.8 106.8                                        
REMARK 620 4 ASP A 890   OD2  90.1  80.7  51.6                                  
REMARK 620 5 CYS A 892   O    87.2 167.6  71.4  89.0                            
REMARK 620 6 VAL A 895   O    74.2 108.0 135.8 161.1  79.8                      
REMARK 620 7 ASN A 897   OD1 145.9  83.2  79.3 119.6 108.2  78.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 902   OD1                                                    
REMARK 620 2 ASP A 904   OD1  81.4                                              
REMARK 620 3 ASP A 906   OD1  89.5  76.3                                        
REMARK 620 4 ARG A 908   O    84.1 161.9  92.9                                  
REMARK 620 5 HOH A2150   O   100.3  96.6 167.0  96.6                            
REMARK 620 6 HOH A2239   O   172.5  92.0  85.4 101.6  83.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 915   OD1                                                    
REMARK 620 2 ASP A 917   OD1  81.0                                              
REMARK 620 3 ASP A 919   OD1  93.3  82.1                                        
REMARK 620 4 VAL A 921   O    90.6 167.3  88.9                                  
REMARK 620 5 ASP A 926   OD2 175.1  94.5  87.9  94.2                            
REMARK 620 6 HOH A2154   O    93.4  84.5 163.9 105.6  84.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 917   OD2                                                    
REMARK 620 2 ASP A 919   OD2  91.4                                              
REMARK 620 3 ASP A 926   OD1 125.4 103.6                                        
REMARK 620 4 ASP A 926   OD2  83.0  77.9  50.9                                  
REMARK 620 5 CYS A 928   O    83.0 169.0  72.6  92.0                            
REMARK 620 6 ASN A 931   O    76.5 100.6 146.5 159.4  87.3                      
REMARK 620 7 ILE A 934   O   153.9  96.1  77.0 123.0  93.0  77.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2016  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 948   O                                                      
REMARK 620 2 GLY A 951   O    95.2                                              
REMARK 620 3 ASP A 956   OD1  88.0 174.9                                        
REMARK 620 4 ASP A 975   OD1  98.3  90.2  93.2                                  
REMARK 620 5 HOH A2149   O    84.5  94.1  82.2 174.6                            
REMARK 620 6 HOH A2187   O   166.5  96.7  79.8  88.2  88.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2013  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 973   OD1                                                    
REMARK 620 2 ASP A1001   OD2  78.9                                              
REMARK 620 3 ASP A1003   OD2 158.3 100.9                                        
REMARK 620 4 SER A1136   O    82.2  85.0  76.2                                  
REMARK 620 5 SER A1136   OG   83.6 156.6  89.6  77.2                            
REMARK 620 6 ASP A 825   OD1  49.3 112.9 113.5  53.3  43.9                      
REMARK 620 7 ASP A 825   OD2  50.3 113.1 112.2  52.3  43.6   1.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2014  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 999   O                                                      
REMARK 620 2 ASP A1001   O    98.0                                              
REMARK 620 3 GLN A1024   OE1 166.2  84.4                                        
REMARK 620 4 ASP A1086   OD1  99.7 140.3  86.6                                  
REMARK 620 5 HOH A2244   O    82.0  71.0  86.0 146.7                            
REMARK 620 6 HOH A2184   O    83.0  78.6 110.8  68.7 143.7                      
REMARK 620 7 HOH A2179   O    85.4 141.4  84.3  75.5  71.5 139.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2015  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1001   OD1                                                    
REMARK 620 2 ASP A1002   OD1  81.4                                              
REMARK 620 3 ASP A1003   OD1 100.0  77.1                                        
REMARK 620 4 ASP A1003   OD2  72.4 114.0  51.1                                  
REMARK 620 5 GLN A1027   OE1 173.6  93.2  75.3 107.1                            
REMARK 620 6 ASP A 825   OD2  70.5 123.6  61.9  11.3 110.3                      
REMARK 620 7 HOH A2203   O    91.0  84.3 156.6 152.1  91.9 141.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2001                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2002                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2004                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2005                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2006                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2007                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2008                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2009                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2010                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2011                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2012                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2013                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2014                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2015                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2016                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LSL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE THROMBOSPONDIN-1 TYPE 1 REPEATS             
DBREF  1UX6 A  803   812  PDB    1UX6     1UX6           803    812             
DBREF  1UX6 A  813  1152  UNP    P07996   TSP1_HUMAN     831   1170             
SEQADV 1UX6 SER A  974  UNP  P07996    CYS   992 ENGINEERED MUTATION            
SEQADV 1UX6 LYS A 1049  UNP  P07996    ASN  1067 ENGINEERED MUTATION            
SEQRES   1 A  350  ALA PRO LEU VAL HIS HIS HIS HIS HIS HIS ALA LEU ALA          
SEQRES   2 A  350  ASP ASN CYS PRO LEU GLU HIS ASN PRO ASP GLN LEU ASP          
SEQRES   3 A  350  SER ASP SER ASP ARG ILE GLY ASP THR CYS ASP ASN ASN          
SEQRES   4 A  350  GLN ASP ILE ASP GLU ASP GLY HIS GLN ASN ASN LEU ASP          
SEQRES   5 A  350  ASN CYS PRO TYR VAL PRO ASN ALA ASN GLN ALA ASP HIS          
SEQRES   6 A  350  ASP LYS ASP GLY LYS GLY ASP ALA CYS ASP HIS ASP ASP          
SEQRES   7 A  350  ASP ASN ASP GLY ILE PRO ASP ASP LYS ASP ASN CYS ARG          
SEQRES   8 A  350  LEU VAL PRO ASN PRO ASP GLN LYS ASP SER ASP GLY ASP          
SEQRES   9 A  350  GLY ARG GLY ASP ALA CYS LYS ASP ASP PHE ASP HIS ASP          
SEQRES  10 A  350  SER VAL PRO ASP ILE ASP ASP ILE CYS PRO GLU ASN VAL          
SEQRES  11 A  350  ASP ILE SER GLU THR ASP PHE ARG ARG PHE GLN MET ILE          
SEQRES  12 A  350  PRO LEU ASP PRO LYS GLY THR SER GLN ASN ASP PRO ASN          
SEQRES  13 A  350  TRP VAL VAL ARG HIS GLN GLY LYS GLU LEU VAL GLN THR          
SEQRES  14 A  350  VAL ASN SER ASP PRO GLY LEU ALA VAL GLY TYR ASP GLU          
SEQRES  15 A  350  PHE ASN ALA VAL ASP PHE SER GLY THR PHE PHE ILE ASN          
SEQRES  16 A  350  THR GLU ARG ASP ASP ASP TYR ALA GLY PHE VAL PHE GLY          
SEQRES  17 A  350  TYR GLN SER SER SER ARG PHE TYR VAL VAL MET TRP LYS          
SEQRES  18 A  350  GLN VAL THR GLN SER TYR TRP ASP THR ASN PRO THR ARG          
SEQRES  19 A  350  ALA GLN GLY TYR SER GLY LEU SER VAL LYS VAL VAL LYS          
SEQRES  20 A  350  SER THR THR GLY PRO GLY GLU HIS LEU ARG ASN ALA LEU          
SEQRES  21 A  350  TRP HIS THR GLY ASN THR PRO GLY GLN VAL ARG THR LEU          
SEQRES  22 A  350  TRP HIS ASP PRO ARG HIS ILE GLY TRP LYS ASP PHE THR          
SEQRES  23 A  350  ALA TYR ARG TRP ARG LEU SER HIS ARG PRO LYS THR GLY          
SEQRES  24 A  350  PHE ILE ARG VAL VAL MET TYR GLU GLY LYS LYS ILE MET          
SEQRES  25 A  350  ALA ASP SER GLY PRO ILE TYR ASP LYS THR TYR ALA GLY          
SEQRES  26 A  350  GLY ARG LEU GLY LEU PHE VAL PHE SER GLN GLU MET VAL          
SEQRES  27 A  350  PHE PHE SER ASP LEU LYS TYR GLU CYS ARG ASP PRO              
HET     CA  A2001       1                                                       
HET     CA  A2002       1                                                       
HET     CA  A2003       1                                                       
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET     CA  A2008       1                                                       
HET     CA  A2009       1                                                       
HET     CA  A2010       1                                                       
HET     CA  A2011       1                                                       
HET     CA  A2012       1                                                       
HET     CA  A2013       1                                                       
HET     CA  A2014       1                                                       
HET     CA  A2015       1                                                       
HET     CA  A2016       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    16(CA 2+)                                                    
FORMUL  18  HOH   *262(H2 O)                                                    
HELIX    1   1 ALA A  813  CYS A  818  1                                   6    
HELIX    2   2 GLN A  850  ASP A  854  5                                   5    
HELIX    3   3 GLY A  873  ASP A  877  5                                   5    
HELIX    4   4 PRO A  886  ASP A  890  5                                   5    
HELIX    5   5 GLY A  909  LYS A  913  5                                   5    
HELIX    6   6 GLY A 1055  HIS A 1064  1                                  10    
SHEET    1  AA 7 GLN A 943  PRO A 946  0                                        
SHEET    2  AA 7 GLY A 977  PHE A 985 -1  O  LEU A 978   N  ILE A 945           
SHEET    3  AA 7 GLY A1128  PHE A1135 -1  O  GLY A1128   N  PHE A 985           
SHEET    4  AA 7 TYR A1004  SER A1013 -1  O  TYR A1004   N  PHE A1135           
SHEET    5  AA 7 ARG A1016  LYS A1023 -1  O  ARG A1016   N  GLN A1012           
SHEET    6  AA 7 GLY A1042  LYS A1049 -1  O  GLY A1042   N  LYS A1023           
SHEET    7  AA 7 VAL A1072  HIS A1077 -1  O  ARG A1073   N  VAL A1047           
SHEET    1  AB 7 TRP A 959  VAL A 960  0                                        
SHEET    2  AB 7 LEU A 968  GLN A 970 -1  O  VAL A 969   N  VAL A 960           
SHEET    3  AB 7 VAL A1140  CYS A1149 -1  O  VAL A1140   N  GLN A 970           
SHEET    4  AB 7 VAL A 988  ILE A 996 -1  O  ASP A 989   N  GLU A1148           
SHEET    5  AB 7 ALA A1089  ARG A1097 -1  O  TYR A1090   N  PHE A 994           
SHEET    6  AB 7 PHE A1102  GLU A1109 -1  O  PHE A1102   N  ARG A1097           
SHEET    7  AB 7 ILE A1120  TYR A1121 -1  O  ILE A1120   N  ILE A1103           
SHEET    1  AC 7 TRP A 959  VAL A 960  0                                        
SHEET    2  AC 7 LEU A 968  GLN A 970 -1  O  VAL A 969   N  VAL A 960           
SHEET    3  AC 7 VAL A1140  CYS A1149 -1  O  VAL A1140   N  GLN A 970           
SHEET    4  AC 7 VAL A 988  ILE A 996 -1  O  ASP A 989   N  GLU A1148           
SHEET    5  AC 7 ALA A1089  ARG A1097 -1  O  TYR A1090   N  PHE A 994           
SHEET    6  AC 7 PHE A1102  GLU A1109 -1  O  PHE A1102   N  ARG A1097           
SHEET    7  AC 7 LYS A1112  ASP A1116 -1  O  LYS A1112   N  GLU A1109           
SHEET    1  AD 2 GLN A1027  SER A1028  0                                        
SHEET    2  AD 2 GLN A1038  GLY A1039 -1  O  GLY A1039   N  GLN A1027           
SSBOND   1 CYS A  818    CYS A  838                          1555   1555  2.03  
SSBOND   2 CYS A  856    CYS A  876                          1555   1555  2.04  
SSBOND   3 CYS A  892    CYS A  912                          1555   1555  2.04  
SSBOND   4 CYS A  928    CYS A 1149                          1555   1555  2.04  
LINK         OD1 ASP A 828                CA    CA A2012     1555   1555  2.17  
LINK         OD1 ASP A 830                CA    CA A2012     1555   1555  2.28  
LINK         OD2 ASP A 830                CA    CA A2011     1555   1555  2.43  
LINK         OD1 ASP A 832                CA    CA A2012     1555   1555  2.23  
LINK         OD2 ASP A 832                CA    CA A2011     1555   1555  2.38  
LINK         O   ILE A 834                CA    CA A2012     1555   1555  2.32  
LINK         OD1 ASP A 839                CA    CA A2011     1555   1555  2.39  
LINK         OD2 ASP A 839                CA    CA A2012     1555   1555  2.39  
LINK         OD2 ASP A 839                CA    CA A2011     1555   1555  2.49  
LINK         OD1 ASN A 841                CA    CA A2011     1555   1555  2.36  
LINK         OD1 ASP A 843                CA    CA A2010     1555   1555  2.26  
LINK         OD1 ASP A 845                CA    CA A2010     1555   1555  2.25  
LINK         OD2 ASP A 845                CA    CA A2009     1555   1555  2.29  
LINK         OD1 ASP A 847                CA    CA A2010     1555   1555  2.39  
LINK         OD2 ASP A 847                CA    CA A2009     1555   1555  2.19  
LINK         O   HIS A 849                CA    CA A2010     1555   1555  2.30  
LINK         OD1 ASP A 854                CA    CA A2009     1555   1555  2.69  
LINK         OD2 ASP A 854                CA    CA A2010     1555   1555  2.35  
LINK         OD2 ASP A 854                CA    CA A2009     1555   1555  2.54  
LINK         O   CYS A 856                CA    CA A2009     1555   1555  2.31  
LINK         O   VAL A 859                CA    CA A2009     1555   1555  2.41  
LINK         OD1 ASN A 861                CA    CA A2009     1555   1555  2.28  
LINK         OD1 ASP A 866                CA    CA A2007     1555   1555  2.32  
LINK         OD1 ASP A 868                CA    CA A2007     1555   1555  2.32  
LINK         OD2 ASP A 868                CA    CA A2006     1555   1555  2.34  
LINK         OD1 ASP A 870                CA    CA A2007     1555   1555  2.44  
LINK         OD2 ASP A 870                CA    CA A2006     1555   1555  2.37  
LINK         O   LYS A 872                CA    CA A2007     1555   1555  2.30  
LINK         O   ASP A 874                CA    CA A2008     1555   1555  2.34  
LINK         O   ASP A 877                CA    CA A2008     1555   1555  2.26  
LINK         OD1 ASP A 877                CA    CA A2006     1555   1555  2.60  
LINK         OD2 ASP A 877                CA    CA A2006     1555   1555  2.48  
LINK         OD2 ASP A 877                CA    CA A2007     1555   1555  2.35  
LINK         O   ASP A 879                CA    CA A2006     1555   1555  2.41  
LINK         OD1 ASP A 879                CA    CA A2004     1555   1555  2.24  
LINK         OD1 ASP A 880                CA    CA A2008     1555   1555  2.33  
LINK         OD2 ASP A 880                CA    CA A2008     1555   1555  2.73  
LINK         OD1 ASP A 881                CA    CA A2004     1555   1555  2.32  
LINK         OD2 ASP A 881                CA    CA A2005     1555   1555  2.25  
LINK         OD1 ASN A 882                CA    CA A2006     1555   1555  2.34  
LINK         OD1 ASP A 883                CA    CA A2004     1555   1555  2.30  
LINK         OD2 ASP A 883                CA    CA A2005     1555   1555  2.35  
LINK         O   ILE A 885                CA    CA A2004     1555   1555  2.22  
LINK         OD2 ASP A 887                CA    CA A2008     1555   1555  2.30  
LINK         OD1 ASP A 890                CA    CA A2005     1555   1555  2.65  
LINK         OD2 ASP A 890                CA    CA A2004     1555   1555  2.35  
LINK         OD2 ASP A 890                CA    CA A2005     1555   1555  2.40  
LINK         O   CYS A 892                CA    CA A2005     1555   1555  2.25  
LINK         O   VAL A 895                CA    CA A2005     1555   1555  2.44  
LINK         OD1 ASN A 897                CA    CA A2005     1555   1555  2.36  
LINK         OD1 ASP A 902                CA    CA A2003     1555   1555  2.29  
LINK         OD1 ASP A 904                CA    CA A2003     1555   1555  2.45  
LINK         OD1 ASP A 906                CA    CA A2003     1555   1555  2.29  
LINK         O   ARG A 908                CA    CA A2003     1555   1555  2.30  
LINK         OD1 ASP A 915                CA    CA A2002     1555   1555  2.22  
LINK         OD1 ASP A 917                CA    CA A2002     1555   1555  2.32  
LINK         OD2 ASP A 917                CA    CA A2001     1555   1555  2.30  
LINK         OD1 ASP A 919                CA    CA A2002     1555   1555  2.36  
LINK         OD2 ASP A 919                CA    CA A2001     1555   1555  2.28  
LINK         O   VAL A 921                CA    CA A2002     1555   1555  2.37  
LINK         OD1 ASP A 926                CA    CA A2001     1555   1555  2.66  
LINK         OD2 ASP A 926                CA    CA A2001     1555   1555  2.40  
LINK         OD2 ASP A 926                CA    CA A2002     1555   1555  2.32  
LINK         O   CYS A 928                CA    CA A2001     1555   1555  2.25  
LINK         O   ASN A 931                CA    CA A2001     1555   1555  2.36  
LINK         O   ILE A 934                CA    CA A2001     1555   1555  2.33  
LINK         O   ASP A 948                CA    CA A2016     1555   1555  2.38  
LINK         O   GLY A 951                CA    CA A2016     1555   1555  2.34  
LINK         OD1 ASP A 956                CA    CA A2016     1555   1555  2.50  
LINK         OD1 ASN A 973                CA    CA A2013     1555   1555  2.20  
LINK         OD1 ASP A 975                CA    CA A2016     1555   1555  2.32  
LINK         O   GLU A 999                CA    CA A2014     1555   1555  2.49  
LINK         O   ASP A1001                CA    CA A2014     1555   1555  2.28  
LINK         OD1 ASP A1001                CA    CA A2015     1555   1555  2.52  
LINK         OD2 ASP A1001                CA    CA A2013     1555   1555  2.40  
LINK         OD1 ASP A1002                CA    CA A2015     1555   1555  2.57  
LINK         OD1 ASP A1003                CA    CA A2015     1555   1555  2.44  
LINK         OD2 ASP A1003                CA    CA A2013     1555   1555  2.28  
LINK         OD2 ASP A1003                CA    CA A2015     1555   1555  2.61  
LINK         OE1 GLN A1024                CA    CA A2014     1555   1555  2.34  
LINK         OE1 GLN A1027                CA    CA A2015     1555   1555  2.40  
LINK         OD1 ASP A1086                CA    CA A2014     1555   1555  2.53  
LINK         O   SER A1136                CA    CA A2013     1555   1555  2.37  
LINK         OG  SER A1136                CA    CA A2013     1555   1555  2.23  
LINK        CA    CA A2002                 O   HOH A2154     1555   1555  2.44  
LINK        CA    CA A2003                 O   HOH A2150     1555   1555  2.40  
LINK        CA    CA A2003                 O   HOH A2239     1555   1555  2.53  
LINK        CA    CA A2004                 O   HOH A2136     1555   1555  2.48  
LINK        CA    CA A2006                 O   HOH A2294     1555   1555  2.44  
LINK        CA    CA A2007                 O   HOH A2118     1555   1555  2.40  
LINK        CA    CA A2008                 O   HOH A2280     1555   1555  2.50  
LINK        CA    CA A2008                 O   HOH A2142     1555   1555  2.21  
LINK        CA    CA A2010                 O   HOH A2122     1555   1555  2.52  
LINK        CA    CA A2011                 O   HOH A2241     1555   1555  2.34  
LINK        CA    CA A2011                 O   HOH A2183     1555   1555  2.37  
LINK        CA    CA A2012                 O   HOH A2110     1555   1555  2.37  
LINK        CA    CA A2014                 O   HOH A2244     1555   1555  2.57  
LINK        CA    CA A2014                 O   HOH A2184     1555   1555  2.45  
LINK        CA    CA A2014                 O   HOH A2179     1555   1555  2.70  
LINK        CA    CA A2016                 O   HOH A2149     1555   1555  2.73  
LINK        CA    CA A2016                 O   HOH A2187     1555   1555  2.41  
LINK         OD1 ASP A 825                CA    CA A2013     1555   2555  2.29  
LINK         OD2 ASP A 825                CA    CA A2015     1555   2555  2.28  
LINK         OD2 ASP A 825                CA    CA A2013     1555   2555  3.19  
LINK        CA    CA A2015                 O   HOH A2203     1555   3555  2.46  
CISPEP   1 ASN A 1033    PRO A 1034          0        -0.04                     
CISPEP   2 ASP A 1151    PRO A 1152          0         0.08                     
SITE     1 AC1  6 ASP A 917  ASP A 919  ASP A 926  CYS A 928                    
SITE     2 AC1  6 ASN A 931  ILE A 934                                          
SITE     1 AC2  6 ASP A 915  ASP A 917  ASP A 919  VAL A 921                    
SITE     2 AC2  6 ASP A 926  HOH A2154                                          
SITE     1 AC3  6 ASP A 902  ASP A 904  ASP A 906  ARG A 908                    
SITE     2 AC3  6 HOH A2239  HOH A2150                                          
SITE     1 AC4  6 ASP A 879  ASP A 881  ASP A 883  ILE A 885                    
SITE     2 AC4  6 ASP A 890  HOH A2136                                          
SITE     1 AC5  6 ASP A 881  ASP A 883  ASP A 890  CYS A 892                    
SITE     2 AC5  6 VAL A 895  ASN A 897                                          
SITE     1 AC6  6 ASP A 868  ASP A 870  ASP A 877  ASP A 879                    
SITE     2 AC6  6 ASN A 882  HOH A2294                                          
SITE     1 AC7  6 ASP A 866  ASP A 868  ASP A 870  LYS A 872                    
SITE     2 AC7  6 ASP A 877  HOH A2118                                          
SITE     1 AC8  6 ASP A 874  ASP A 877  ASP A 880  ASP A 887                    
SITE     2 AC8  6 HOH A2280  HOH A2142                                          
SITE     1 AC9  6 ASP A 845  ASP A 847  ASP A 854  CYS A 856                    
SITE     2 AC9  6 VAL A 859  ASN A 861                                          
SITE     1 BC1  6 ASP A 843  ASP A 845  ASP A 847  HIS A 849                    
SITE     2 BC1  6 ASP A 854  HOH A2122                                          
SITE     1 BC2  6 ASP A 830  ASP A 832  ASP A 839  ASN A 841                    
SITE     2 BC2  6 HOH A2241  HOH A2183                                          
SITE     1 BC3  6 ASP A 828  ASP A 830  ASP A 832  ILE A 834                    
SITE     2 BC3  6 ASP A 839  HOH A2110                                          
SITE     1 BC4  5 ASP A 825  ASN A 973  ASP A1001  ASP A1003                    
SITE     2 BC4  5 SER A1136                                                     
SITE     1 BC5  7 GLU A 999  ASP A1001  GLN A1024  ASP A1086                    
SITE     2 BC5  7 HOH A2184  HOH A2244  HOH A2179                               
SITE     1 BC6  6 ASP A 825  ASP A1001  ASP A1002  ASP A1003                    
SITE     2 BC6  6 GLN A1027  HOH A2203                                          
SITE     1 BC7  6 ASP A 948  GLY A 951  ASP A 956  ASP A 975                    
SITE     2 BC7  6 HOH A2187  HOH A2149                                          
CRYST1  162.340  162.340   85.140  90.00  90.00 120.00 H 3 2        18          
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      0.006160  0.003556  0.000000        0.00000                         
SCALE2      0.000000  0.007113  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011745        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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