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Database: PDB
Entry: 1XU8
LinkDB: 1XU8
Original site: 1XU8 
HEADER    SIGNALING PROTEIN                       25-OCT-04   1XU8              
TITLE     THE 2.8 A STRUCTURE OF A TUMOUR SUPPRESSING SERPIN                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MASPIN;                                                    
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                 
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.IRVING,R.H.LAW,K.RUZYLA,T.A.BASHTANNYK-PUHALOVICH,N.KIM,          
AUTHOR   2 D.M.WORRALL,J.ROSSJOHN,J.C.WHISSTOCK                                 
REVDAT   3   24-FEB-09 1XU8    1       VERSN                                    
REVDAT   2   21-JUN-05 1XU8    1       JRNL                                     
REVDAT   1   15-MAR-05 1XU8    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,               
JRNL        AUTH 3 D.M.WORRALL,S.P.BOTTOMLEY,P.I.BIRD,J.ROSSJOHN,               
JRNL        AUTH 4 J.C.WHISSTOCK                                                
JRNL        TITL   THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN           
JRNL        TITL 2 TUMOR SUPPRESSOR MASPIN REVEALS A NOVEL                      
JRNL        TITL 3 CONFORMATIONAL SWITCH IN 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   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17231                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 945                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1150                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5815                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 123                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.65000                                              
REMARK   3    B22 (A**2) : 1.20000                                              
REMARK   3    B33 (A**2) : -1.85000                                             
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): 0.483         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.373         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.851        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.910                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.859                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5927 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7988 ; 1.280 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   734 ; 6.163 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   260 ;39.784 ;26.231       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1129 ;18.733 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;22.227 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   911 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4341 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2740 ; 0.226 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4005 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   251 ; 0.196 ; 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):   103 ; 0.265 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.380 ; 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):  3771 ; 1.071 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5977 ; 1.889 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2361 ; 3.188 ; 7.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2011 ; 5.045 ;10.000       
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      4       A     332      1                      
REMARK   3           1     B      4       B     332      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2578 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2578 ;  0.08 ;  0.50           
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    344       A     375      1                      
REMARK   3           1     B    344       B     375      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    275 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      2    A (A**2):    275 ;  0.09 ;  0.50           
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1XU8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030776.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-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          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18174                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OVA CHAIN A                               
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: AMMONIUM SULFATE, BIS-TRIS, 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       26.77000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.30500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.24000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.30500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.77000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.24000            
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 300 REMARK: THE BIOLOGICAL UNIT CONSISTS OF A MONOMER.                   
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     MET A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     ASN A    -1                                                      
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     GLN A   343                                                      
REMARK 465     MET B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     SER B   333                                                      
REMARK 465     ILE B   334                                                      
REMARK 465     GLU B   335                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL B 336    CG1  CG2                                            
REMARK 470     PRO B 337    CG   CD                                             
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  3245     O    HOH A  3287              1.91            
REMARK 500   O    HOH A  3267     O    HOH A  3287              2.00            
REMARK 500   O    HOH B   397     O    HOH B   422              2.08            
REMARK 500   SG   CYS B   183     O    HOH B   426              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN A   223     OE2  GLU B   239     2554     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A   4   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    LEU B   4   CA  -  CB  -  CG  ANGL. DEV. =  18.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A   1       38.76    -85.85                                   
REMARK 500    ASP A   2       37.57    -99.85                                   
REMARK 500    LYS A  64     -125.28    -72.97                                   
REMARK 500    ASP A  65       93.51    -54.92                                   
REMARK 500    SER A  97       -8.07    -58.68                                   
REMARK 500    LEU A  98       60.40   -108.75                                   
REMARK 500    ASN A  99      103.33    -25.86                                   
REMARK 500    LYS A 114       -8.47     65.12                                   
REMARK 500    LEU A 139      -19.37    -48.95                                   
REMARK 500    ASP A 150       28.61    163.54                                   
REMARK 500    SER A 152       78.67     26.61                                   
REMARK 500    ASN A 188     -164.59   -170.56                                   
REMARK 500    LYS A 294      -63.77    -96.43                                   
REMARK 500    ARG A 364        6.50     82.38                                   
REMARK 500    ALA B   3       47.77    -92.82                                   
REMARK 500    LYS B  64     -128.20    -74.47                                   
REMARK 500    ASP B  65       96.07    -55.56                                   
REMARK 500    SER B  97       -9.98    -56.02                                   
REMARK 500    LEU B  98       56.95   -108.77                                   
REMARK 500    ASN B  99      101.43    -21.94                                   
REMARK 500    LYS B 114       -7.25     65.85                                   
REMARK 500    ASP B 120       77.70   -104.42                                   
REMARK 500    ALA B 149       58.45    -91.16                                   
REMARK 500    ASP B 150       23.22    163.15                                   
REMARK 500    SER B 152       74.00     27.31                                   
REMARK 500    ASN B 188     -166.23   -172.79                                   
REMARK 500    LYS B 294      -63.97   -100.35                                   
REMARK 500    ALA B 339     -103.29    -75.58                                   
REMARK 500    ARG B 340     -165.63   -166.20                                   
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 MET A    1     ASP A    2                  147.45                    
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 3243                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3244                
DBREF  1XU8 A    1   375  UNP    P36952   MASP_HUMAN       1    375             
DBREF  1XU8 B    1   375  UNP    P36952   MASP_HUMAN       1    375             
SEQADV 1XU8 MET A   -4  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 GLY A   -3  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 GLN A   -2  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 ASN A   -1  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 SER A    0  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 VAL A   66  UNP  P36952    ILE    66 SEE REMARK 999                 
SEQADV 1XU8 MET B   -4  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 GLY B   -3  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 GLN B   -2  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 ASN B   -1  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 SER B    0  UNP  P36952              CLONING ARTIFACT               
SEQADV 1XU8 VAL B   66  UNP  P36952    ILE    66 SEE REMARK 999                 
SEQRES   1 A  380  MET GLY GLN ASN SER MET ASP ALA LEU GLN LEU ALA ASN          
SEQRES   2 A  380  SER ALA PHE ALA VAL ASP LEU PHE LYS GLN LEU CYS GLU          
SEQRES   3 A  380  LYS GLU PRO LEU GLY ASN VAL LEU PHE SER PRO ILE CYS          
SEQRES   4 A  380  LEU SER THR SER LEU SER LEU ALA GLN VAL GLY ALA LYS          
SEQRES   5 A  380  GLY ASP THR ALA ASN GLU ILE GLY GLN VAL LEU HIS PHE          
SEQRES   6 A  380  GLU ASN VAL LYS ASP VAL PRO PHE GLY PHE GLN THR VAL          
SEQRES   7 A  380  THR SER ASP VAL ASN LYS LEU SER SER PHE TYR SER LEU          
SEQRES   8 A  380  LYS LEU ILE LYS ARG LEU TYR VAL ASP LYS SER LEU ASN          
SEQRES   9 A  380  LEU SER THR GLU PHE ILE SER SER THR LYS ARG PRO TYR          
SEQRES  10 A  380  ALA LYS GLU LEU GLU THR VAL ASP PHE LYS ASP LYS LEU          
SEQRES  11 A  380  GLU GLU THR LYS GLY GLN ILE ASN ASN SER ILE LYS ASP          
SEQRES  12 A  380  LEU THR ASP GLY HIS PHE GLU ASN ILE LEU ALA ASP ASN          
SEQRES  13 A  380  SER VAL ASN ASP GLN THR LYS ILE LEU VAL VAL ASN ALA          
SEQRES  14 A  380  ALA TYR PHE VAL GLY LYS TRP MET LYS LYS PHE PRO GLU          
SEQRES  15 A  380  SER GLU THR LYS GLU CYS PRO PHE ARG LEU ASN LYS THR          
SEQRES  16 A  380  ASP THR LYS PRO VAL GLN MET MET ASN MET GLU ALA THR          
SEQRES  17 A  380  PHE CYS MET GLY ASN ILE ASP SER ILE ASN CYS LYS ILE          
SEQRES  18 A  380  ILE GLU LEU PRO PHE GLN ASN LYS HIS LEU SER MET PHE          
SEQRES  19 A  380  ILE LEU LEU PRO LYS ASP VAL GLU ASP GLU SER THR GLY          
SEQRES  20 A  380  LEU GLU LYS ILE GLU LYS GLN LEU ASN SER GLU SER LEU          
SEQRES  21 A  380  SER GLN TRP THR ASN PRO SER THR MET ALA ASN ALA LYS          
SEQRES  22 A  380  VAL LYS LEU SER ILE PRO LYS PHE LYS VAL GLU LYS MET          
SEQRES  23 A  380  ILE ASP PRO LYS ALA CYS LEU GLU ASN LEU GLY LEU LYS          
SEQRES  24 A  380  HIS ILE PHE SER GLU ASP THR SER ASP PHE SER GLY MET          
SEQRES  25 A  380  SER GLU THR LYS GLY VAL ALA LEU SER ASN VAL ILE HIS          
SEQRES  26 A  380  LYS VAL CYS LEU GLU ILE THR GLU ASP GLY GLY ASP SER          
SEQRES  27 A  380  ILE GLU VAL PRO GLY ALA ARG ILE LEU GLN HIS LYS ASP          
SEQRES  28 A  380  GLU LEU ASN ALA ASP HIS PRO PHE ILE TYR ILE ILE ARG          
SEQRES  29 A  380  HIS ASN LYS THR ARG ASN ILE ILE PHE PHE GLY LYS PHE          
SEQRES  30 A  380  CYS SER PRO                                                  
SEQRES   1 B  380  MET GLY GLN ASN SER MET ASP ALA LEU GLN LEU ALA ASN          
SEQRES   2 B  380  SER ALA PHE ALA VAL ASP LEU PHE LYS GLN LEU CYS GLU          
SEQRES   3 B  380  LYS GLU PRO LEU GLY ASN VAL LEU PHE SER PRO ILE CYS          
SEQRES   4 B  380  LEU SER THR SER LEU SER LEU ALA GLN VAL GLY ALA LYS          
SEQRES   5 B  380  GLY ASP THR ALA ASN GLU ILE GLY GLN VAL LEU HIS PHE          
SEQRES   6 B  380  GLU ASN VAL LYS ASP VAL PRO PHE GLY PHE GLN THR VAL          
SEQRES   7 B  380  THR SER ASP VAL ASN LYS LEU SER SER PHE TYR SER LEU          
SEQRES   8 B  380  LYS LEU ILE LYS ARG LEU TYR VAL ASP LYS SER LEU ASN          
SEQRES   9 B  380  LEU SER THR GLU PHE ILE SER SER THR LYS ARG PRO TYR          
SEQRES  10 B  380  ALA LYS GLU LEU GLU THR VAL ASP PHE LYS ASP LYS LEU          
SEQRES  11 B  380  GLU GLU THR LYS GLY GLN ILE ASN ASN SER ILE LYS ASP          
SEQRES  12 B  380  LEU THR ASP GLY HIS PHE GLU ASN ILE LEU ALA ASP ASN          
SEQRES  13 B  380  SER VAL ASN ASP GLN THR LYS ILE LEU VAL VAL ASN ALA          
SEQRES  14 B  380  ALA TYR PHE VAL GLY LYS TRP MET LYS LYS PHE PRO GLU          
SEQRES  15 B  380  SER GLU THR LYS GLU CYS PRO PHE ARG LEU ASN LYS THR          
SEQRES  16 B  380  ASP THR LYS PRO VAL GLN MET MET ASN MET GLU ALA THR          
SEQRES  17 B  380  PHE CYS MET GLY ASN ILE ASP SER ILE ASN CYS LYS ILE          
SEQRES  18 B  380  ILE GLU LEU PRO PHE GLN ASN LYS HIS LEU SER MET PHE          
SEQRES  19 B  380  ILE LEU LEU PRO LYS ASP VAL GLU ASP GLU SER THR GLY          
SEQRES  20 B  380  LEU GLU LYS ILE GLU LYS GLN LEU ASN SER GLU SER LEU          
SEQRES  21 B  380  SER GLN TRP THR ASN PRO SER THR MET ALA ASN ALA LYS          
SEQRES  22 B  380  VAL LYS LEU SER ILE PRO LYS PHE LYS VAL GLU LYS MET          
SEQRES  23 B  380  ILE ASP PRO LYS ALA CYS LEU GLU ASN LEU GLY LEU LYS          
SEQRES  24 B  380  HIS ILE PHE SER GLU ASP THR SER ASP PHE SER GLY MET          
SEQRES  25 B  380  SER GLU THR LYS GLY VAL ALA LEU SER ASN VAL ILE HIS          
SEQRES  26 B  380  LYS VAL CYS LEU GLU ILE THR GLU ASP GLY GLY ASP SER          
SEQRES  27 B  380  ILE GLU VAL PRO GLY ALA ARG ILE LEU GLN HIS LYS ASP          
SEQRES  28 B  380  GLU LEU ASN ALA ASP HIS PRO PHE ILE TYR ILE ILE ARG          
SEQRES  29 B  380  HIS ASN LYS THR ARG ASN ILE ILE PHE PHE GLY LYS PHE          
SEQRES  30 B  380  CYS SER PRO                                                  
HET    SO4  A3243       5                                                       
HET    SO4  A3244       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *123(H2 O)                                                    
HELIX    1   1 ALA A    3  GLU A   23  1                                  21    
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  101  SER A  107  1                                   7    
HELIX    6   6 LYS A  124  THR A  140  1                                  17    
HELIX    7   7 PRO A  176  THR A  180  5                                   5    
HELIX    8   8 GLN A  222  LYS A  224  5                                   3    
HELIX    9   9 ASP A  238  GLN A  249  1                                  12    
HELIX   10  10 ASN A  251  THR A  259  1                                   9    
HELIX   11  11 PRO A  284  GLY A  292  1                                   9    
HELIX   12  12 LEU B    4  GLU B   23  1                                  20    
HELIX   13  13 SER B   31  ALA B   46  1                                  16    
HELIX   14  14 LYS B   47  LEU B   58  1                                  12    
HELIX   15  15 ASP B   65  SER B   81  1                                  17    
HELIX   16  16 SER B  101  LYS B  109  1                                   9    
HELIX   17  17 LYS B  124  THR B  140  1                                  17    
HELIX   18  18 PRO B  176  THR B  180  5                                   5    
HELIX   19  19 GLN B  222  LYS B  224  5                                   3    
HELIX   20  20 ASP B  238  GLN B  249  1                                  12    
HELIX   21  21 ASN B  251  ASN B  260  1                                  10    
HELIX   22  22 PRO B  284  LEU B  291  1                                   8    
SHEET    1   A 7 LEU A  29  PHE A  30  0                                        
SHEET    2   A 7 ILE A 366  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  PHE A 368           
SHEET    4   A 7 LEU A 226  PRO A 233 -1  N  PHE A 229   O  ILE A 357           
SHEET    5   A 7 CYS A 214  PRO A 220 -1  N  LYS A 215   O  LEU A 232           
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 ILE A 366  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  PHE A 368           
SHEET    4   B 8 LEU A 226  PRO A 233 -1  N  PHE A 229   O  ILE A 357           
SHEET    5   B 8 CYS A 214  PRO A 220 -1  N  LYS A 215   O  LEU A 232           
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 LYS A 345  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 LEU A  86  ASP A  95  1  N  VAL A  94   O  VAL A 119           
SHEET    3   C 5 ILE A 159  VAL A 168 -1  O  LEU A 160   N  TYR A  93           
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  LYS A 280   O  VAL A 322           
SHEET    1   D 7 LEU B  29  PHE B  30  0                                        
SHEET    2   D 7 ILE B 366  PHE B 372 -1  O  PHE B 369   N  PHE B  30           
SHEET    3   D 7 PHE B 354  HIS B 360 -1  N  TYR B 356   O  GLY B 370           
SHEET    4   D 7 LEU B 226  PRO B 233 -1  N  PHE B 229   O  ILE B 357           
SHEET    5   D 7 CYS 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  GLY B 207   O  ILE B 216           
SHEET    7   D 7 LYS B 181  ARG B 186 -1  N  PHE B 185   O  LYS B 193           
SHEET    1   E 8 LEU B  29  PHE B  30  0                                        
SHEET    2   E 8 ILE B 366  PHE B 372 -1  O  PHE B 369   N  PHE B  30           
SHEET    3   E 8 PHE B 354  HIS B 360 -1  N  TYR B 356   O  GLY B 370           
SHEET    4   E 8 LEU B 226  PRO B 233 -1  N  PHE B 229   O  ILE B 357           
SHEET    5   E 8 CYS 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  GLY B 207   O  ILE B 216           
SHEET    7   E 8 ALA B 265  PRO B 274 -1  O  ALA B 265   N  MET B 206           
SHEET    8   E 8 HIS B 344  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  VAL B 119           
SHEET    3   F 5 ILE B 159  VAL B 168 -1  O  LEU B 160   N  TYR B  93           
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  VAL B 278   O  LEU B 324           
SITE     1 AC1  4 LYS A 109  LYS B 173  ALA B 202  THR B 203                    
SITE     1 AC2  5 LYS A 129  LEU A 148  ASP A 150  ASN A 151                    
SITE     2 AC2  5 SER A 152                                                     
CRYST1   53.540  100.480  136.610  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      0.018679  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009953  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007320        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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