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Database: PDB
Entry: 2PVS
LinkDB: 2PVS
Original site: 2PVS 
HEADER    HYDROLASE                               10-MAY-07   2PVS              
TITLE     STRUCTURE OF HUMAN PANCREATIC LIPASE RELATED PROTEIN 2                
TITLE    2 MUTANT N336Q                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PANCREATIC LIPASE-RELATED PROTEIN 2;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.3;                                                         
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 GENE: PNLIPRP2, PLRP2;                                               
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SMD 1168;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGAPZB                                
KEYWDS    LIPASE, GALACTO LIPIDS HYDROLYSIS, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SPINELLI,C.EYDOUX,F.CARRIERE,C.CAMBILLAU                            
REVDAT   2   20-JAN-09 2PVS    1       JRNL   VERSN                             
REVDAT   1   18-DEC-07 2PVS    0                                                
JRNL        AUTH   C.EYDOUX,S.SPINELLI,T.L.DAVIS,J.R.WALKER,A.SEITOVA,          
JRNL        AUTH 2 S.DHE-PAGANON,A.DE CARO,C.CAMBILLAU,F.CARRIERE               
JRNL        TITL   STRUCTURE OF HUMAN PANCREATIC LIPASE-RELATED                 
JRNL        TITL 2 PROTEIN 2 WITH THE LID IN AN OPEN CONFORMATION.              
JRNL        REF    BIOCHEMISTRY                  V.  47  9553 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18702514                                                     
JRNL        DOI    10.1021/BI8005576                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 27791                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1477                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1993                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 118                          
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6868                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 67                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 88.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.43000                                              
REMARK   3    B22 (A**2) : 2.43000                                              
REMARK   3    B33 (A**2) : -4.86000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.383         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.279         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.566        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7078 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4827 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9586 ; 1.369 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11722 ; 0.880 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   873 ; 7.497 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   336 ;39.050 ;24.732       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1154 ;19.065 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;17.710 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1003 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7926 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1436 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1656 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5155 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3423 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3819 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   181 ; 0.174 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.156 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    12 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.330 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4503 ; 0.496 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1794 ; 0.078 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7010 ; 0.854 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2985 ; 1.071 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2576 ; 1.760 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     235      5                      
REMARK   3           1     B      1       B     235      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1374 ;  0.16 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1730 ;  0.53 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1374 ;  0.47 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1730 ;  1.06 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    255       A     320      5                      
REMARK   3           1     B    255       B     320      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    384 ;  0.19 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    496 ;  0.40 ;  5.00           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    384 ;  0.36 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    496 ;  0.72 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2PVS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB042827.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27791                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : 0.11800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1GPL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6 MICROLITER OF PROTEIN (14.5 MG/ML      
REMARK 280  IN 0.2 M NACL, 25 MM TRIS-HCL, PH 8.0) AND 2 MICROLITER OF          
REMARK 280  2.05 M AMMONIUM SULPHATE, 0.1 M HEPES, PH 6.7, VAPOR                
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-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      108.09050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000      108.09050            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.83600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      108.09050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.91800            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      108.09050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       92.75400            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      108.09050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       92.75400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      108.09050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       30.91800            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000      108.09050            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000      108.09050            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.83600            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000      108.09050            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000      108.09050            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       61.83600            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000      108.09050            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       92.75400            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000      108.09050            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       30.91800            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      108.09050            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       30.91800            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000      108.09050            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       92.75400            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000      108.09050            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000      108.09050            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       61.83600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22220 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 134290 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -648.6 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000     -108.09050            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000      108.09050            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      309.18000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      216.18100            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000 -1.000000  0.000000      108.09050            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      108.09050            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      309.18000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   239                                                      
REMARK 465     ASN A   240                                                      
REMARK 465     VAL A   241                                                      
REMARK 465     LEU A   242                                                      
REMARK 465     SER A   243                                                      
REMARK 465     THR A   244                                                      
REMARK 465     ILE A   245                                                      
REMARK 465     THR A   246                                                      
REMARK 465     ASP A   247                                                      
REMARK 465     ILE A   248                                                      
REMARK 465     ASP A   249                                                      
REMARK 465     GLY A   250                                                      
REMARK 465     ILE A   251                                                      
REMARK 465     TRP A   252                                                      
REMARK 465     ARG A   406                                                      
REMARK 465     GLY A   407                                                      
REMARK 465     ILE A   408                                                      
REMARK 465     VAL B   241                                                      
REMARK 465     LEU B   242                                                      
REMARK 465     SER B   243                                                      
REMARK 465     THR B   244                                                      
REMARK 465     ILE B   245                                                      
REMARK 465     THR B   246                                                      
REMARK 465     ASP B   247                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   509     O    HOH A   510              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 188   CG    GLU A 188   CD      0.093                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  -1      148.69   -173.25                                   
REMARK 500    ASN A  63        0.72    -69.31                                   
REMARK 500    LEU A  78       69.03     32.17                                   
REMARK 500    ILE A 121      -38.02    -39.03                                   
REMARK 500    ASP A 145      -15.72    164.70                                   
REMARK 500    SER A 152     -119.31     57.35                                   
REMARK 500    ASP A 176       71.94     41.60                                   
REMARK 500    CYS A 181      -11.84     91.57                                   
REMARK 500    VAL A 221       31.31   -142.14                                   
REMARK 500    ILE A 255       20.70    -76.27                                   
REMARK 500    GLU A 293        5.27    -69.58                                   
REMARK 500    CYS A 296       25.99   -149.39                                   
REMARK 500    GLU A 302       42.80    -94.56                                   
REMARK 500    ASN A 364     -135.05    -54.26                                   
REMARK 500    ILE A 372      -31.59   -136.21                                   
REMARK 500    ASP A 380      -31.13     88.10                                   
REMARK 500    CYS A 385      124.16   -170.13                                   
REMARK 500    ASP A 427       22.95   -151.30                                   
REMARK 500    SER A 435       89.44    156.51                                   
REMARK 500    GLN B   5        0.88    -67.42                                   
REMARK 500    LYS B  24       72.66   -101.73                                   
REMARK 500    PRO B  56       19.77    -67.97                                   
REMARK 500    SER B  62     -169.29    -74.13                                   
REMARK 500    LEU B  78       62.19     34.94                                   
REMARK 500    PHE B  94        0.57    -62.43                                   
REMARK 500    SER B 152     -112.52     68.41                                   
REMARK 500    ASP B 176       64.27     33.75                                   
REMARK 500    CYS B 181       -7.85     97.17                                   
REMARK 500    ASP B 205       52.62   -142.50                                   
REMARK 500    LEU B 213       27.16   -141.34                                   
REMARK 500    VAL B 221       22.11   -146.27                                   
REMARK 500    LYS B 238      -89.27   -113.88                                   
REMARK 500    ASP B 249       24.33     96.19                                   
REMARK 500    SER B 260      130.28    -34.19                                   
REMARK 500    CYS B 285      141.14    174.49                                   
REMARK 500    SER B 294       35.67     72.72                                   
REMARK 500    PRO B 298     -163.02    -79.55                                   
REMARK 500    PHE B 335       -0.71     63.52                                   
REMARK 500    LYS B 349       17.32   -145.04                                   
REMARK 500    CYS B 385      135.54    178.35                                   
REMARK 500    ARG B 406       -5.80   -158.65                                   
REMARK 500    SER B 411      -39.53     97.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A  409     LEU A  410                 -143.70                    
REMARK 500 LEU A  410     SER A  411                  126.18                    
REMARK 500 GLU B  412     PRO B  413                 -148.23                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     CYS B 237        23.4      L          L   OUTSIDE RANGE          
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 A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 187   O                                                      
REMARK 620 2 ARG A 190   O    77.4                                              
REMARK 620 3 ASP A 192   OD2  90.7  90.0                                        
REMARK 620 4 ASP A 195   OD1 151.8 127.6  77.9                                  
REMARK 620 5 ASP A 195   OD2 143.4  79.9  61.0  49.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 187   O                                                      
REMARK 620 2 ARG B 190   O    78.8                                              
REMARK 620 3 ASP B 192   OD2  93.8  88.8                                        
REMARK 620 4 ASP B 195   OD1 144.8 135.9  83.4                                  
REMARK 620 5 ASP B 195   OD2 162.9  86.1  77.7  49.8                            
REMARK 620 6 HOH B 511   O    87.3  86.5 174.9  98.6  99.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 451                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 452                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 453                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 454                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 455                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 451                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 452                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 453                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 501                  
DBREF  2PVS A   -2   450  UNP    P54317   LIPR2_HUMAN     18    469             
DBREF  2PVS B   -2   450  UNP    P54317   LIPR2_HUMAN     18    469             
SEQADV 2PVS GLN A  334  UNP  P54317    ASN   353 ENGINEERED                     
SEQADV 2PVS GLN B  334  UNP  P54317    ASN   353 ENGINEERED                     
SEQRES   1 A  452  LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE SER ASP          
SEQRES   2 A  452  GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO VAL LYS          
SEQRES   3 A  452  LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR ARG PHE          
SEQRES   4 A  452  LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN LEU          
SEQRES   5 A  452  ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA SER ASN          
SEQRES   6 A  452  PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE HIS GLY          
SEQRES   7 A  452  PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER ASP MET          
SEQRES   8 A  452  CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN CYS ILE          
SEQRES   9 A  452  CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET TYR THR          
SEQRES  10 A  452  GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA GLU THR          
SEQRES  11 A  452  ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU GLY TYR          
SEQRES  12 A  452  SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER LEU GLY          
SEQRES  13 A  452  ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU GLY GLY          
SEQRES  14 A  452  ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA GLY PRO          
SEQRES  15 A  452  CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU ASP PRO          
SEQRES  16 A  452  SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR ASP SER          
SEQRES  17 A  452  SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET SER GLN          
SEQRES  18 A  452  LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS          
SEQRES  19 A  452  GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER THR ILE          
SEQRES  20 A  452  THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY GLY PHE          
SEQRES  21 A  452  VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR TYR SER          
SEQRES  22 A  452  SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY TYR PRO          
SEQRES  23 A  452  CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS CYS PHE          
SEQRES  24 A  452  PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY HIS TYR          
SEQRES  25 A  452  ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL GLU GLN          
SEQRES  26 A  452  THR PHE PHE LEU ASN THR GLY GLU SER GLY GLN PHE THR          
SEQRES  27 A  452  SER TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS          
SEQRES  28 A  452  GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU TYR GLY          
SEQRES  29 A  452  SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE LYS GLY          
SEQRES  30 A  452  SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA ILE ASP          
SEQRES  31 A  452  VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL LYS PHE          
SEQRES  32 A  452  LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU PRO LYS          
SEQRES  33 A  452  LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY GLU ASP          
SEQRES  34 A  452  GLY THR GLU TYR ASN PHE CYS SER SER ASP THR VAL GLU          
SEQRES  35 A  452  GLU ASN VAL LEU GLN SER LEU TYR PRO CYS                      
SEQRES   1 B  452  LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE SER ASP          
SEQRES   2 B  452  GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO VAL LYS          
SEQRES   3 B  452  LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR ARG PHE          
SEQRES   4 B  452  LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN LEU          
SEQRES   5 B  452  ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA SER ASN          
SEQRES   6 B  452  PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE HIS GLY          
SEQRES   7 B  452  PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER ASP MET          
SEQRES   8 B  452  CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN CYS ILE          
SEQRES   9 B  452  CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET TYR THR          
SEQRES  10 B  452  GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA GLU THR          
SEQRES  11 B  452  ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU GLY TYR          
SEQRES  12 B  452  SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER LEU GLY          
SEQRES  13 B  452  ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU GLY GLY          
SEQRES  14 B  452  ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA GLY PRO          
SEQRES  15 B  452  CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU ASP PRO          
SEQRES  16 B  452  SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR ASP SER          
SEQRES  17 B  452  SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET SER GLN          
SEQRES  18 B  452  LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS          
SEQRES  19 B  452  GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER THR ILE          
SEQRES  20 B  452  THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY GLY PHE          
SEQRES  21 B  452  VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR TYR SER          
SEQRES  22 B  452  SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY TYR PRO          
SEQRES  23 B  452  CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS CYS PHE          
SEQRES  24 B  452  PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY HIS TYR          
SEQRES  25 B  452  ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL GLU GLN          
SEQRES  26 B  452  THR PHE PHE LEU ASN THR GLY GLU SER GLY GLN PHE THR          
SEQRES  27 B  452  SER TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS          
SEQRES  28 B  452  GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU TYR GLY          
SEQRES  29 B  452  SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE LYS GLY          
SEQRES  30 B  452  SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA ILE ASP          
SEQRES  31 B  452  VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL LYS PHE          
SEQRES  32 B  452  LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU PRO LYS          
SEQRES  33 B  452  LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY GLU ASP          
SEQRES  34 B  452  GLY THR GLU TYR ASN PHE CYS SER SER ASP THR VAL GLU          
SEQRES  35 B  452  GLU ASN VAL LEU GLN SER LEU TYR PRO CYS                      
HET    SO4  A 451       5                                                       
HET    SO4  A 452       5                                                       
HET    SO4  A 453       5                                                       
HET    SO4  A 454       5                                                       
HET    SO4  A 455       5                                                       
HET     CA  A 502       1                                                       
HET    SO4  B 451       5                                                       
HET    SO4  B 452       5                                                       
HET    SO4  B 453       5                                                       
HET     CA  B 501       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  SO4    8(O4 S 2-)                                                   
FORMUL   8   CA    2(CA 2+)                                                     
FORMUL  13  HOH   *67(H2 O)                                                     
HELIX    1   1 TYR A    3  GLY A    7  5                                   5    
HELIX    2   2 SER A   29  ASP A   34  1                                   6    
HELIX    3   3 PRO A   56  ALA A   61  1                                   6    
HELIX    4   4 SER A   84  GLU A   97  1                                  14    
HELIX    5   5 TRP A  106  ARG A  111  1                                   6    
HELIX    6   6 MET A  113  GLY A  140  1                                  28    
HELIX    7   7 SER A  152  LEU A  165  1                                  14    
HELIX    8   8 PRO A  186  ARG A  190  5                                   5    
HELIX    9   9 ASP A  192  ALA A  196  5                                   5    
HELIX   10  10 GLY A  256  VAL A  259  5                                   4    
HELIX   11  11 SER A  260  VAL A  274  1                                  15    
HELIX   12  12 SER A  287  GLU A  293  1                                   7    
HELIX   13  13 GLY A  308  PHE A  314  5                                   7    
HELIX   14  14 TYR B    3  GLY B    7  5                                   5    
HELIX   15  15 SER B   29  ASP B   34  1                                   6    
HELIX   16  16 GLU B   55  SER B   62  1                                   8    
HELIX   17  17 SER B   84  PHE B   94  1                                  11    
HELIX   18  18 TRP B  106  ARG B  111  1                                   6    
HELIX   19  19 MET B  113  GLY B  140  1                                  28    
HELIX   20  20 SER B  142  GLU B  144  5                                   3    
HELIX   21  21 SER B  152  LEU B  165  1                                  14    
HELIX   22  22 PRO B  186  ARG B  190  5                                   5    
HELIX   23  23 ASP B  192  ALA B  196  5                                   5    
HELIX   24  24 GLY B  256  VAL B  259  5                                   4    
HELIX   25  25 SER B  260  ASN B  276  1                                  17    
HELIX   26  26 TYR B  288  GLU B  293  1                                   6    
HELIX   27  27 GLY B  308  PHE B  314  5                                   7    
SHEET    1   A10 GLN A  49  ILE A  51  0                                        
SHEET    2   A10 ARG A  36  TYR A  40 -1  N  LEU A  39   O  GLN A  49           
SHEET    3   A10 VAL A  99  ASP A 105 -1  O  ASP A 105   N  ARG A  36           
SHEET    4   A10 LYS A  69  ILE A  74  1  N  ARG A  71   O  ILE A 102           
SHEET    5   A10 VAL A 146  HIS A 151  1  O  ILE A 149   N  ILE A  74           
SHEET    6   A10 ARG A 171  LEU A 175  1  O  LEU A 175   N  GLY A 150           
SHEET    7   A10 PHE A 198  ILE A 202  1  O  ILE A 202   N  GLY A 174           
SHEET    8   A10 LEU A 224  PRO A 228  1  O  PHE A 226   N  VAL A 201           
SHEET    9   A10 GLN A 323  LEU A 327  1  O  GLN A 323   N  ASP A 225           
SHEET   10   A10 TYR A 283  PRO A 284 -1  N  TYR A 283   O  PHE A 326           
SHEET    1   B 2 SER A 206  SER A 207  0                                        
SHEET    2   B 2 GLY A 216  MET A 217  1  O  GLY A 216   N  SER A 207           
SHEET    1   C 8 TYR A 370  LEU A 377  0                                        
SHEET    2   C 8 VAL A 352  TYR A 361 -1  N  VAL A 352   O  LEU A 377           
SHEET    3   C 8 LYS A 398  ASN A 404 -1  O  LYS A 400   N  ALA A 359           
SHEET    4   C 8 GLN A 445  PRO A 449 -1  O  GLN A 445   N  PHE A 401           
SHEET    5   C 8 GLU A 430  CYS A 434 -1  N  CYS A 434   O  TYR A 448           
SHEET    6   C 8 LEU A 415  SER A 424 -1  N  VAL A 422   O  TYR A 431           
SHEET    7   C 8 TRP A 338  GLY A 348 -1  N  LYS A 341   O  GLN A 423           
SHEET    8   C 8 SER A 382  VAL A 389 -1  O  ILE A 387   N  TYR A 340           
SHEET    1   D10 ASN B  44  ILE B  51  0                                        
SHEET    2   D10 ARG B  36  THR B  41 -1  N  LEU B  39   O  GLN B  49           
SHEET    3   D10 VAL B  99  ASP B 105 -1  O  CYS B 101   N  TYR B  40           
SHEET    4   D10 LYS B  69  ILE B  74  1  N  ARG B  71   O  ILE B 102           
SHEET    5   D10 VAL B 146  HIS B 151  1  O  ILE B 149   N  PHE B  72           
SHEET    6   D10 ARG B 171  LEU B 175  1  O  LEU B 175   N  GLY B 150           
SHEET    7   D10 PHE B 198  ILE B 202  1  O  PHE B 198   N  ILE B 172           
SHEET    8   D10 LEU B 224  PRO B 228  1  O  PHE B 226   N  VAL B 201           
SHEET    9   D10 GLN B 323  LEU B 327  1  O  PHE B 325   N  PHE B 227           
SHEET   10   D10 TYR B 283  PRO B 284 -1  N  TYR B 283   O  PHE B 326           
SHEET    1   E 2 SER B 206  SER B 207  0                                        
SHEET    2   E 2 GLY B 216  MET B 217  1  O  GLY B 216   N  SER B 207           
SHEET    1   F 3 ASN B 366  PHE B 373  0                                        
SHEET    2   F 3 VAL B 352  TYR B 361 -1  N  LEU B 360   O  SER B 367           
SHEET    3   F 3 SER B 376  LEU B 377 -1  O  LEU B 377   N  VAL B 352           
SHEET    1   G 8 ASN B 366  PHE B 373  0                                        
SHEET    2   G 8 VAL B 352  TYR B 361 -1  N  LEU B 360   O  SER B 367           
SHEET    3   G 8 LYS B 398  LYS B 405 -1  O  LEU B 402   N  ARG B 357           
SHEET    4   G 8 GLN B 445  PRO B 449 -1  O  GLN B 445   N  PHE B 401           
SHEET    5   G 8 GLU B 430  CYS B 434 -1  N  CYS B 434   O  TYR B 448           
SHEET    6   G 8 GLN B 419  SER B 424 -1  N  ILE B 420   O  PHE B 433           
SHEET    7   G 8 TRP B 338  SER B 343 -1  N  SER B 343   O  THR B 421           
SHEET    8   G 8 THR B 384  VAL B 389 -1  O  ILE B 387   N  TYR B 340           
SHEET    1   H 2 LEU B 346  SER B 347  0                                        
SHEET    2   H 2 GLY B 416  ALA B 417 -1  O  GLY B 416   N  SER B 347           
SSBOND   1 CYS A    2    CYS A    8                          1555   1555  2.08  
SSBOND   2 CYS A   90    CYS A  101                          1555   1555  2.07  
SSBOND   3 CYS A  237    CYS A  261                          1555   1555  2.07  
SSBOND   4 CYS A  285    CYS A  296                          1555   1555  2.06  
SSBOND   5 CYS A  299    CYS A  304                          1555   1555  2.03  
SSBOND   6 CYS A  434    CYS A  450                          1555   1555  2.07  
SSBOND   7 CYS B    2    CYS B    8                          1555   1555  2.07  
SSBOND   8 CYS B   90    CYS B  101                          1555   1555  2.08  
SSBOND   9 CYS B  237    CYS B  261                          1555   1555  2.08  
SSBOND  10 CYS B  285    CYS B  296                          1555   1555  2.09  
SSBOND  11 CYS B  299    CYS B  304                          1555   1555  2.04  
SSBOND  12 CYS B  434    CYS B  450                          1555   1555  2.07  
LINK         O   GLU A 187                CA    CA A 502     1555   1555  2.26  
LINK         O   ARG A 190                CA    CA A 502     1555   1555  2.38  
LINK         OD2 ASP A 192                CA    CA A 502     1555   1555  2.32  
LINK         OD1 ASP A 195                CA    CA A 502     1555   1555  2.59  
LINK         OD2 ASP A 195                CA    CA A 502     1555   1555  2.66  
LINK         O   GLU B 187                CA    CA B 501     1555   1555  2.40  
LINK         O   ARG B 190                CA    CA B 501     1555   1555  2.31  
LINK         OD2 ASP B 192                CA    CA B 501     1555   1555  2.11  
LINK         OD1 ASP B 195                CA    CA B 501     1555   1555  2.73  
LINK         OD2 ASP B 195                CA    CA B 501     1555   1555  2.53  
LINK        CA    CA B 501                 O   HOH B 511     1555   1555  2.43  
CISPEP   1 LYS A   13    PRO A   14          0        12.73                     
CISPEP   2 VAL A  210    PRO A  211          0         4.26                     
CISPEP   3 PHE A  297    PRO A  298          0        -6.09                     
CISPEP   4 LYS B   13    PRO B   14          0         7.26                     
CISPEP   5 VAL B  210    PRO B  211          0       -18.36                     
CISPEP   6 CYS B  237    LYS B  238          0       -15.16                     
CISPEP   7 PHE B  297    PRO B  298          0        -0.02                     
SITE     1 AC1  4 ARG A 107  HIS A 108  ARG A 111  LYS B  80                    
SITE     1 AC2  2 HIS A 108  ARG A 111                                          
SITE     1 AC3  5 LYS A  80  ASP A  83  ARG B 107  HIS B 108                    
SITE     2 AC3  5 ARG B 111                                                     
SITE     1 AC4  5 GLU A  43  ASN A  44  PRO A  45  ASN A  46                    
SITE     2 AC4  5 ASN A  47                                                     
SITE     1 AC5  4 PHE A 314  GLY A 316  LYS A 317  THR A 318                    
SITE     1 AC6  4 GLU A 187  ARG A 190  ASP A 192  ASP A 195                    
SITE     1 AC7  2 HIS B 108  ARG B 111                                          
SITE     1 AC8  4 ASN B  44  PRO B  45  ASN B  46  ASN B  47                    
SITE     1 AC9  5 LYS B 315  GLY B 316  LYS B 317  THR B 318                    
SITE     2 AC9  5 SER B 319                                                     
SITE     1 BC1  5 GLU B 187  ARG B 190  ASP B 192  ASP B 195                    
SITE     2 BC1  5 HOH B 511                                                     
CRYST1  216.181  216.181  123.672  90.00  90.00  90.00 I 41 2 2     32          
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      0.004626  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004626  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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