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Database: PDB
Entry: 1WZ9
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Original site: 1WZ9 
HEADER    SIGNALING PROTEIN                       03-MAR-05   1WZ9              
TITLE     THE 2.1 A STRUCTURE OF A TUMOUR SUPPRESSING SERPIN                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MASPIN PRECURSOR;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEASE INHIBITOR 5;                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SERPINB5;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSETC                                    
KEYWDS    MASPIN, SERPIN, TUMOR SUPPRESSOR, SERPINB5, SIGNALING PROTEIN         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.H.LAW,J.A.IRVING,A.M.BUCKLE,K.RUZYLA,M.BUZZA,T.A.BASHTANNYK-        
AUTHOR   2 PUHALOVICH,T.C.BEDDOE,N.KIM,D.M.WORRALL,S.P.BOTTOMLEY,P.I.BIRD,      
AUTHOR   3 J.ROSSJOHN,J.C.WHISSTOCK                                             
REVDAT   4   11-OCT-17 1WZ9    1       REMARK                                   
REVDAT   3   24-FEB-09 1WZ9    1       VERSN                                    
REVDAT   2   21-JUN-05 1WZ9    1       JRNL                                     
REVDAT   1   15-MAR-05 1WZ9    0                                                
JRNL        AUTH   R.H.LAW,J.A.IRVING,A.M.BUCKLE,K.RUZYLA,M.BUZZA,              
JRNL        AUTH 2 T.A.BASHTANNYK-PUHALOVICH,T.C.BEDDOE,K.NGUYEN,D.M.WORRALL,   
JRNL        AUTH 3 S.P.BOTTOMLEY,P.I.BIRD,J.ROSSJOHN,J.C.WHISSTOCK              
JRNL        TITL   THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN TUMOR     
JRNL        TITL 2 SUPPRESSOR MASPIN REVEALS A NOVEL CONFORMATIONAL SWITCH IN   
JRNL        TITL 3 THE G-HELIX.                                                 
JRNL        REF    J.BIOL.CHEM.                  V. 280 22356 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15760906                                                     
JRNL        DOI    10.1074/JBC.M412043200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 78.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 139.22                         
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 40352                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
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      : 2136                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2908                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 159                          
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5523                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 201                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.42000                                              
REMARK   3    B22 (A**2) : -0.23000                                             
REMARK   3    B33 (A**2) : -0.19000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.252         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.157         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.953        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5628 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7614 ; 1.152 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   718 ; 5.520 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   226 ;38.427 ;26.150       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   943 ;15.601 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;18.406 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   891 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4134 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2512 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3840 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   273 ; 0.128 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    27 ; 0.175 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.135 ; 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):  3721 ; 1.191 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5815 ; 2.039 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2125 ; 3.340 ; 7.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1799 ; 4.843 ;10.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1WZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000024180.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42714                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 36.80                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1XU8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS, 2.9M (NH4)2SO4, PH 8.3,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.05750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.61250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.52350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.61250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.05750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.52350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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     GLY A   331                                                      
REMARK 465     ASP A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     ILE A   334                                                      
REMARK 465     GLU A   335                                                      
REMARK 465     VAL A   336                                                      
REMARK 465     PRO A   337                                                      
REMARK 465     GLY A   338                                                      
REMARK 465     ALA A   339                                                      
REMARK 465     ARG A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     ASP B   150                                                      
REMARK 465     ASN B   151                                                      
REMARK 465     GLU B   237                                                      
REMARK 465     ASP B   238                                                      
REMARK 465     GLU B   239                                                      
REMARK 465     SER B   240                                                      
REMARK 465     ILE B   334                                                      
REMARK 465     GLU B   335                                                      
REMARK 465     VAL B   336                                                      
REMARK 465     PRO B   337                                                      
REMARK 465     GLY B   338                                                      
REMARK 465     ALA B   339                                                      
REMARK 465     ARG B   340                                                      
REMARK 465     ILE B   341                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  22    CD   CE   NZ                                        
REMARK 470     GLU A  61    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  64    CG   CD   CE   NZ                                   
REMARK 470     LYS A  96    CD   CE   NZ                                        
REMARK 470     GLU A 103    CD   OE1  OE2                                       
REMARK 470     LYS A 109    CD   CE   NZ                                        
REMARK 470     ARG A 110    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 114    CD   CE   NZ                                        
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     LYS A 124    CD   CE   NZ                                        
REMARK 470     LYS A 129    CE   NZ                                             
REMARK 470     ASP A 150    CG   OD1  OD2                                       
REMARK 470     ASN A 151    CG   OD1  ND2                                       
REMARK 470     LYS A 158    CE   NZ                                             
REMARK 470     LYS A 174    CD   CE   NZ                                        
REMARK 470     LYS A 181    CE   NZ                                             
REMARK 470     ILE A 212    CG1  CG2  CD1                                       
REMARK 470     LYS A 245    CE   NZ                                             
REMARK 470     LYS A 268    CG   CD   CE   NZ                                   
REMARK 470     LYS A 270    CD   CE   NZ                                        
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     ILE A 296    CG1  CG2  CD1                                       
REMARK 470     ASP A 300    CG   OD1  OD2                                       
REMARK 470     GLN A 343    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 344    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 345    CD   CE   NZ                                        
REMARK 470     LYS A 362    CE   NZ                                             
REMARK 470     ARG A 364    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B   2    CG   OD1  OD2                                       
REMARK 470     CME B  20    SD   CE   CZ   OH                                   
REMARK 470     GLU B  21    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  23    OE1  OE2                                            
REMARK 470     ASN B  62    OD1  ND2                                            
REMARK 470     LYS B  64    CG   CD   CE   NZ                                   
REMARK 470     SER B  97    OG                                                  
REMARK 470     LEU B 100    CG   CD1  CD2                                       
REMARK 470     GLU B 103    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 109    CG   CD   CE   NZ                                   
REMARK 470     ARG B 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 114    CG   CD   CE   NZ                                   
REMARK 470     LYS B 122    CG   CD   CE   NZ                                   
REMARK 470     LYS B 124    CG   CD   CE   NZ                                   
REMARK 470     GLU B 126    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 127    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 131    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 146    CG   OD1  ND2                                       
REMARK 470     VAL B 153    CG1  CG2                                            
REMARK 470     GLU B 179    OE1  OE2                                            
REMARK 470     LYS B 181    CG   CD   CE   NZ                                   
REMARK 470     LYS B 189    CG   CD   CE   NZ                                   
REMARK 470     ASP B 210    CG   OD1  OD2                                       
REMARK 470     CME B 214    SD   CE   CZ   OH                                   
REMARK 470     LYS B 234    CD   CE   NZ                                        
REMARK 470     ASP B 235    CG   OD1  OD2                                       
REMARK 470     VAL B 236    CG1  CG2                                            
REMARK 470     THR B 241    OG1  CG2                                            
REMARK 470     GLU B 244    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 248    CG   CD   CE   NZ                                   
REMARK 470     GLU B 253    CD   OE1  OE2                                       
REMARK 470     LYS B 268    CG   CD   CE   NZ                                   
REMARK 470     LYS B 270    CG   CD   CE   NZ                                   
REMARK 470     MET B 281    CG   SD   CE                                        
REMARK 470     LYS B 294    CG   CD   CE   NZ                                   
REMARK 470     GLU B 309    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 311    CG   CD   CE   NZ                                   
REMARK 470     LYS B 321    CD   CE   NZ                                        
REMARK 470     CME B 323    SD   CE   CZ   OH                                   
REMARK 470     ASP B 332    CG   OD1  OD2                                       
REMARK 470     SER B 333    OG                                                  
REMARK 470     LEU B 342    CG   CD1  CD2                                       
REMARK 470     GLN B 343    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 345    CG   CD   CE   NZ                                   
REMARK 470     ARG B 364    CD   NE   CZ   NH1  NH2                             
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  65       72.26     48.74                                   
REMARK 500    ASN A  99       66.73     39.58                                   
REMARK 500    LYS A 114       -5.93     74.23                                   
REMARK 500    ASP A 120       77.54   -109.31                                   
REMARK 500    LYS A 124       55.54   -140.91                                   
REMARK 500    ASN A 188     -161.45   -167.10                                   
REMARK 500    ASN B  99       72.22     45.15                                   
REMARK 500    LYS B 114       -2.41     70.32                                   
REMARK 500    LYS B 124       60.96   -115.87                                   
REMARK 500    LYS B 294      -62.55   -131.43                                   
REMARK 500    ASP B 332     -149.77    -85.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XU8   RELATED DB: PDB                                   
REMARK 900 THE 2.8 A STRUCTURE OF A TUMOUR SUPRESSING SERPIN                    
DBREF  1WZ9 A    1   375  UNP    P36952   MASP_HUMAN       1    375             
DBREF  1WZ9 B    1   375  UNP    P36952   MASP_HUMAN       1    375             
SEQADV 1WZ9 CME A   20  UNP  P36952    CYS    20 MODIFIED RESIDUE               
SEQADV 1WZ9 VAL A   66  UNP  P36952    ILE    66 SEE REMARK 999                 
SEQADV 1WZ9 CME A  183  UNP  P36952    CYS   183 MODIFIED RESIDUE               
SEQADV 1WZ9 CME A  205  UNP  P36952    CYS   205 MODIFIED RESIDUE               
SEQADV 1WZ9 CME A  214  UNP  P36952    CYS   214 MODIFIED RESIDUE               
SEQADV 1WZ9 CME A  323  UNP  P36952    CYS   323 MODIFIED RESIDUE               
SEQADV 1WZ9 CME A  373  UNP  P36952    CYS   373 MODIFIED RESIDUE               
SEQADV 1WZ9 CME B   20  UNP  P36952    CYS    20 MODIFIED RESIDUE               
SEQADV 1WZ9 VAL B   66  UNP  P36952    ILE    66 SEE REMARK 999                 
SEQADV 1WZ9 CME B  183  UNP  P36952    CYS   183 MODIFIED RESIDUE               
SEQADV 1WZ9 CME B  205  UNP  P36952    CYS   205 MODIFIED RESIDUE               
SEQADV 1WZ9 CME B  214  UNP  P36952    CYS   214 MODIFIED RESIDUE               
SEQADV 1WZ9 CME B  323  UNP  P36952    CYS   323 MODIFIED RESIDUE               
SEQADV 1WZ9 CME B  373  UNP  P36952    CYS   373 MODIFIED RESIDUE               
SEQRES   1 A  375  MET ASP ALA LEU GLN LEU ALA ASN SER ALA PHE ALA VAL          
SEQRES   2 A  375  ASP LEU PHE LYS GLN LEU CME GLU LYS GLU PRO LEU GLY          
SEQRES   3 A  375  ASN VAL LEU PHE SER PRO ILE CYS LEU SER THR SER LEU          
SEQRES   4 A  375  SER LEU ALA GLN VAL GLY ALA LYS GLY ASP THR ALA ASN          
SEQRES   5 A  375  GLU ILE GLY GLN VAL LEU HIS PHE GLU ASN VAL LYS ASP          
SEQRES   6 A  375  VAL PRO PHE GLY PHE GLN THR VAL THR SER ASP VAL ASN          
SEQRES   7 A  375  LYS LEU SER SER PHE TYR SER LEU LYS LEU ILE LYS ARG          
SEQRES   8 A  375  LEU TYR VAL ASP LYS SER LEU ASN LEU SER THR GLU PHE          
SEQRES   9 A  375  ILE SER SER THR LYS ARG PRO TYR ALA LYS GLU LEU GLU          
SEQRES  10 A  375  THR VAL ASP PHE LYS ASP LYS LEU GLU GLU THR LYS GLY          
SEQRES  11 A  375  GLN ILE ASN ASN SER ILE LYS ASP LEU THR ASP GLY HIS          
SEQRES  12 A  375  PHE GLU ASN ILE LEU ALA ASP ASN SER VAL ASN ASP GLN          
SEQRES  13 A  375  THR LYS ILE LEU VAL VAL ASN ALA ALA TYR PHE VAL GLY          
SEQRES  14 A  375  LYS TRP MET LYS LYS PHE PRO GLU SER GLU THR LYS GLU          
SEQRES  15 A  375  CME PRO PHE ARG LEU ASN LYS THR ASP THR LYS PRO VAL          
SEQRES  16 A  375  GLN MET MET ASN MET GLU ALA THR PHE CME MET GLY ASN          
SEQRES  17 A  375  ILE ASP SER ILE ASN CME LYS ILE ILE GLU LEU PRO PHE          
SEQRES  18 A  375  GLN ASN LYS HIS LEU SER MET PHE ILE LEU LEU PRO LYS          
SEQRES  19 A  375  ASP VAL GLU ASP GLU SER THR GLY LEU GLU LYS ILE GLU          
SEQRES  20 A  375  LYS GLN LEU ASN SER GLU SER LEU SER GLN TRP THR ASN          
SEQRES  21 A  375  PRO SER THR MET ALA ASN ALA LYS VAL LYS LEU SER ILE          
SEQRES  22 A  375  PRO LYS PHE LYS VAL GLU LYS MET ILE ASP PRO LYS ALA          
SEQRES  23 A  375  CYS LEU GLU ASN LEU GLY LEU LYS HIS ILE PHE SER GLU          
SEQRES  24 A  375  ASP THR SER ASP PHE SER GLY MET SER GLU THR LYS GLY          
SEQRES  25 A  375  VAL ALA LEU SER ASN VAL ILE HIS LYS VAL CME LEU GLU          
SEQRES  26 A  375  ILE THR GLU ASP GLY GLY ASP SER ILE GLU VAL PRO GLY          
SEQRES  27 A  375  ALA ARG ILE LEU GLN HIS LYS ASP GLU LEU ASN ALA ASP          
SEQRES  28 A  375  HIS PRO PHE ILE TYR ILE ILE ARG HIS ASN LYS THR ARG          
SEQRES  29 A  375  ASN ILE ILE PHE PHE GLY LYS PHE CME SER PRO                  
SEQRES   1 B  375  MET ASP ALA LEU GLN LEU ALA ASN SER ALA PHE ALA VAL          
SEQRES   2 B  375  ASP LEU PHE LYS GLN LEU CME GLU LYS GLU PRO LEU GLY          
SEQRES   3 B  375  ASN VAL LEU PHE SER PRO ILE CYS LEU SER THR SER LEU          
SEQRES   4 B  375  SER LEU ALA GLN VAL GLY ALA LYS GLY ASP THR ALA ASN          
SEQRES   5 B  375  GLU ILE GLY GLN VAL LEU HIS PHE GLU ASN VAL LYS ASP          
SEQRES   6 B  375  VAL PRO PHE GLY PHE GLN THR VAL THR SER ASP VAL ASN          
SEQRES   7 B  375  LYS LEU SER SER PHE TYR SER LEU LYS LEU ILE LYS ARG          
SEQRES   8 B  375  LEU TYR VAL ASP LYS SER LEU ASN LEU SER THR GLU PHE          
SEQRES   9 B  375  ILE SER SER THR LYS ARG PRO TYR ALA LYS GLU LEU GLU          
SEQRES  10 B  375  THR VAL ASP PHE LYS ASP LYS LEU GLU GLU THR LYS GLY          
SEQRES  11 B  375  GLN ILE ASN ASN SER ILE LYS ASP LEU THR ASP GLY HIS          
SEQRES  12 B  375  PHE GLU ASN ILE LEU ALA ASP ASN SER VAL ASN ASP GLN          
SEQRES  13 B  375  THR LYS ILE LEU VAL VAL ASN ALA ALA TYR PHE VAL GLY          
SEQRES  14 B  375  LYS TRP MET LYS LYS PHE PRO GLU SER GLU THR LYS GLU          
SEQRES  15 B  375  CME PRO PHE ARG LEU ASN LYS THR ASP THR LYS PRO VAL          
SEQRES  16 B  375  GLN MET MET ASN MET GLU ALA THR PHE CME MET GLY ASN          
SEQRES  17 B  375  ILE ASP SER ILE ASN CME LYS ILE ILE GLU LEU PRO PHE          
SEQRES  18 B  375  GLN ASN LYS HIS LEU SER MET PHE ILE LEU LEU PRO LYS          
SEQRES  19 B  375  ASP VAL GLU ASP GLU SER THR GLY LEU GLU LYS ILE GLU          
SEQRES  20 B  375  LYS GLN LEU ASN SER GLU SER LEU SER GLN TRP THR ASN          
SEQRES  21 B  375  PRO SER THR MET ALA ASN ALA LYS VAL LYS LEU SER ILE          
SEQRES  22 B  375  PRO LYS PHE LYS VAL GLU LYS MET ILE ASP PRO LYS ALA          
SEQRES  23 B  375  CYS LEU GLU ASN LEU GLY LEU LYS HIS ILE PHE SER GLU          
SEQRES  24 B  375  ASP THR SER ASP PHE SER GLY MET SER GLU THR LYS GLY          
SEQRES  25 B  375  VAL ALA LEU SER ASN VAL ILE HIS LYS VAL CME LEU GLU          
SEQRES  26 B  375  ILE THR GLU ASP GLY GLY ASP SER ILE GLU VAL PRO GLY          
SEQRES  27 B  375  ALA ARG ILE LEU GLN HIS LYS ASP GLU LEU ASN ALA ASP          
SEQRES  28 B  375  HIS PRO PHE ILE TYR ILE ILE ARG HIS ASN LYS THR ARG          
SEQRES  29 B  375  ASN ILE ILE PHE PHE GLY LYS PHE CME SER PRO                  
MODRES 1WZ9 CME A   20  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME A  183  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME A  205  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME A  214  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME A  323  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME A  373  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME B   20  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME B  183  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME B  205  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME B  214  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME B  323  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 1WZ9 CME B  373  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A  20      10                                                       
HET    CME  A 183      10                                                       
HET    CME  A 205      10                                                       
HET    CME  A 214      10                                                       
HET    CME  A 323      10                                                       
HET    CME  A 373      10                                                       
HET    CME  B  20       6                                                       
HET    CME  B 183      10                                                       
HET    CME  B 205      10                                                       
HET    CME  B 214       6                                                       
HET    CME  B 323       6                                                       
HET    CME  B 373      10                                                       
HET    SO4  A1001       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  CME    12(C5 H11 N O3 S2)                                           
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *201(H2 O)                                                    
HELIX    1   1 MET A    1  GLU A   23  1                                  23    
HELIX    2   2 SER A   31  ALA A   46  1                                  16    
HELIX    3   3 LYS A   47  LEU A   58  1                                  12    
HELIX    4   4 ASP A   65  SER A   81  1                                  17    
HELIX    5   5 SER A   97  ASN A   99  5                                   3    
HELIX    6   6 SER A  101  LYS A  109  1                                   9    
HELIX    7   7 LYS A  124  THR A  140  1                                  17    
HELIX    8   8 PRO A  176  THR A  180  5                                   5    
HELIX    9   9 GLN A  222  LYS A  224  5                                   3    
HELIX   10  10 ASP A  238  LEU A  250  1                                  13    
HELIX   11  11 ASN A  251  THR A  259  1                                   9    
HELIX   12  12 ASN A  260  MET A  264  5                                   5    
HELIX   13  13 ASP A  283  GLY A  292  1                                  10    
HELIX   14  14 MET B    1  GLU B   23  1                                  23    
HELIX   15  15 SER B   31  GLY B   45  1                                  15    
HELIX   16  16 LYS B   47  LEU B   58  1                                  12    
HELIX   17  17 HIS B   59  VAL B   63  5                                   5    
HELIX   18  18 ASP B   65  SER B   81  1                                  17    
HELIX   19  19 SER B   97  ASN B   99  5                                   3    
HELIX   20  20 SER B  101  ARG B  110  1                                  10    
HELIX   21  21 LYS B  124  THR B  140  1                                  17    
HELIX   22  22 PRO B  176  THR B  180  5                                   5    
HELIX   23  23 GLN B  222  LYS B  224  5                                   3    
HELIX   24  24 GLY B  242  GLN B  249  1                                   8    
HELIX   25  25 ASN B  251  THR B  259  1                                   9    
HELIX   26  26 ASN B  260  MET B  264  5                                   5    
HELIX   27  27 PRO B  284  GLY B  292  1                                   9    
HELIX   28  28 LYS B  294  SER B  298  5                                   5    
SHEET    1   A 7 LEU A  29  PHE A  30  0                                        
SHEET    2   A 7 ASN A 365  PHE A 372 -1  O  PHE A 369   N  PHE A  30           
SHEET    3   A 7 PHE A 354  HIS A 360 -1  N  ILE A 358   O  ILE A 367           
SHEET    4   A 7 LEU A 226  PRO A 233 -1  N  LEU A 231   O  ILE A 355           
SHEET    5   A 7 CME A 214  PRO A 220 -1  N  LEU A 219   O  MET A 228           
SHEET    6   A 7 THR A 192  ILE A 209 -1  N  GLY A 207   O  ILE A 216           
SHEET    7   A 7 LYS A 181  ARG A 186 -1  N  PHE A 185   O  LYS A 193           
SHEET    1   B 8 LEU A  29  PHE A  30  0                                        
SHEET    2   B 8 ASN A 365  PHE A 372 -1  O  PHE A 369   N  PHE A  30           
SHEET    3   B 8 PHE A 354  HIS A 360 -1  N  ILE A 358   O  ILE A 367           
SHEET    4   B 8 LEU A 226  PRO A 233 -1  N  LEU A 231   O  ILE A 355           
SHEET    5   B 8 CME A 214  PRO A 220 -1  N  LEU A 219   O  MET A 228           
SHEET    6   B 8 THR A 192  ILE A 209 -1  N  GLY A 207   O  ILE A 216           
SHEET    7   B 8 ALA A 265  PRO A 274 -1  O  ILE A 273   N  MET A 198           
SHEET    8   B 8 HIS A 344  ASN A 349  1  O  LEU A 348   N  SER A 272           
SHEET    1   C 5 LEU A 116  VAL A 119  0                                        
SHEET    2   C 5 SER A  85  ASP A  95  1  N  LEU A  92   O  GLU A 117           
SHEET    3   C 5 ILE A 159  VAL A 168 -1  O  ALA A 164   N  ILE A  89           
SHEET    4   C 5 LEU A 315  ILE A 326  1  O  ILE A 319   N  VAL A 161           
SHEET    5   C 5 PHE A 276  ILE A 282 -1  N  PHE A 276   O  ILE A 326           
SHEET    1   D 7 VAL B  28  PHE B  30  0                                        
SHEET    2   D 7 ILE B 366  PHE B 372 -1  O  LYS B 371   N  VAL B  28           
SHEET    3   D 7 PHE B 354  HIS B 360 -1  N  PHE B 354   O  PHE B 372           
SHEET    4   D 7 LEU B 226  PRO B 233 -1  N  PHE B 229   O  ILE B 357           
SHEET    5   D 7 CME B 214  PRO B 220 -1  N  LEU B 219   O  MET B 228           
SHEET    6   D 7 THR B 192  ILE B 209 -1  N  CME B 205   O  GLU B 218           
SHEET    7   D 7 LYS B 181  ARG B 186 -1  N  LYS B 181   O  MET B 197           
SHEET    1   E 8 VAL B  28  PHE B  30  0                                        
SHEET    2   E 8 ILE B 366  PHE B 372 -1  O  LYS B 371   N  VAL B  28           
SHEET    3   E 8 PHE B 354  HIS B 360 -1  N  PHE B 354   O  PHE B 372           
SHEET    4   E 8 LEU B 226  PRO B 233 -1  N  PHE B 229   O  ILE B 357           
SHEET    5   E 8 CME B 214  PRO B 220 -1  N  LEU B 219   O  MET B 228           
SHEET    6   E 8 THR B 192  ILE B 209 -1  N  CME B 205   O  GLU B 218           
SHEET    7   E 8 ALA B 265  PRO B 274 -1  O  ILE B 273   N  MET B 198           
SHEET    8   E 8 LYS B 345  ASN B 349  1  O  LEU B 348   N  SER B 272           
SHEET    1   F 5 LEU B 116  VAL B 119  0                                        
SHEET    2   F 5 SER B  85  ASP B  95  1  N  VAL B  94   O  GLU B 117           
SHEET    3   F 5 ILE B 159  VAL B 168 -1  O  ALA B 164   N  ILE B  89           
SHEET    4   F 5 LEU B 315  ILE B 326  1  O  ILE B 319   N  VAL B 161           
SHEET    5   F 5 PHE B 276  ILE B 282 -1  N  PHE B 276   O  ILE B 326           
LINK         C   LEU A  19                 N   CME A  20     1555   1555  1.34  
LINK         C   CME A  20                 N   GLU A  21     1555   1555  1.33  
LINK         C   GLU A 182                 N   CME A 183     1555   1555  1.33  
LINK         C   CME A 183                 N   PRO A 184     1555   1555  1.34  
LINK         C   PHE A 204                 N   CME A 205     1555   1555  1.33  
LINK         C   CME A 205                 N   MET A 206     1555   1555  1.33  
LINK         C   ASN A 213                 N   CME A 214     1555   1555  1.33  
LINK         C   CME A 214                 N   LYS A 215     1555   1555  1.33  
LINK         C   VAL A 322                 N   CME A 323     1555   1555  1.33  
LINK         C   CME A 323                 N   LEU A 324     1555   1555  1.33  
LINK         C   PHE A 372                 N   CME A 373     1555   1555  1.34  
LINK         C   CME A 373                 N   SER A 374     1555   1555  1.33  
LINK         C   LEU B  19                 N   CME B  20     1555   1555  1.33  
LINK         C   CME B  20                 N   GLU B  21     1555   1555  1.34  
LINK         C   GLU B 182                 N   CME B 183     1555   1555  1.33  
LINK         C   CME B 183                 N   PRO B 184     1555   1555  1.35  
LINK         C   PHE B 204                 N   CME B 205     1555   1555  1.33  
LINK         C   CME B 205                 N   MET B 206     1555   1555  1.33  
LINK         C   ASN B 213                 N   CME B 214     1555   1555  1.33  
LINK         C   CME B 214                 N   LYS B 215     1555   1555  1.33  
LINK         C   VAL B 322                 N   CME B 323     1555   1555  1.33  
LINK         C   CME B 323                 N   LEU B 324     1555   1555  1.33  
LINK         C   PHE B 372                 N   CME B 373     1555   1555  1.33  
LINK         C   CME B 373                 N   SER B 374     1555   1555  1.33  
SITE     1 AC1  6 GLY A  26  ASN A  27  LYS A 280  HOH A1024                    
SITE     2 AC1  6 GLY B 331  ASP B 332                                          
CRYST1   54.115   95.047  139.225  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018479  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010521  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007183        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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