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Database: PDB
Entry: 5DU3
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Original site: 5DU3 
HEADER    HYDROLASE INHIBITOR                     18-SEP-15   5DU3              
TITLE     ACTIVE FORM OF HUMAN C1-INHIBITOR                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLASMA PROTEASE C1 INHIBITOR;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 119-500;                                      
COMPND   5 SYNONYM: C1INH,C1 ESTERASE INHIBITOR,C1-INHIBITING FACTOR,SERPIN G1; 
COMPND   6 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: SERPING1, C1IN, C1NH;                                          
SOURCE   6 EXPRESSION_SYSTEM: ORYCTOLAGUS CUNICULUS;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: RABBIT;                                    
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9986                                        
KEYWDS    SERINE PROTEASE INHIBITOR, HYDROLASE INHIBITOR                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.S.PANNU,M.DIJK,J.HOLKERS,P.VOSKAMP,B.M.GIANNETTI,W.J.WATERREUS,     
AUTHOR   2 H.A.VAN VEEN                                                         
REVDAT   2   25-JAN-17 5DU3    1       JRNL                                     
REVDAT   1   31-AUG-16 5DU3    0                                                
JRNL        AUTH   M.DIJK,J.HOLKERS,P.VOSKAMP,B.M.GIANNETTI,W.J.WATERREUS,      
JRNL        AUTH 2 H.A.VAN VEEN,N.S.PANNU                                       
JRNL        TITL   HOW DEXTRAN SULFATE AFFECTS C1-INHIBITOR ACTIVITY: A MODEL   
JRNL        TITL 2 FOR POLYSACCHARIDE POTENTIATION.                             
JRNL        REF    STRUCTURE                     V.  24  2182 2016              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   27818099                                                     
JRNL        DOI    10.1016/J.STR.2016.09.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
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) : 57.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 49868                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2647                            
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) : 3620                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 188                          
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5946                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 151                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.78000                                             
REMARK   3    B22 (A**2) : -0.92000                                             
REMARK   3    B33 (A**2) : 1.70000                                              
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): 0.215         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.192         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.170         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.723        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6077 ; 0.024 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5925 ; 0.009 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8244 ; 2.066 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13676 ; 1.628 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   753 ; 7.255 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   249 ;39.451 ;24.819       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1093 ;14.927 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;20.585 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   977 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6702 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1336 ; 0.008 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3011 ; 2.400 ; 2.385       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3010 ; 2.400 ; 2.384       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3755 ; 3.954 ; 3.549       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3756 ; 3.954 ; 3.550       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3066 ; 2.609 ; 2.691       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3067 ; 2.608 ; 2.692       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4490 ; 4.420 ; 3.902       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6623 ; 6.869 ;18.689       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6591 ; 6.864 ;18.601       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   101    476       B   101    476   43950  0.16  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   100        A   475                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1780  67.5780  44.6370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1868 T22:   0.3042                                     
REMARK   3      T33:   0.0264 T12:  -0.0024                                     
REMARK   3      T13:   0.0261 T23:  -0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1414 L22:   0.4196                                     
REMARK   3      L33:   1.4637 L12:   0.2201                                     
REMARK   3      L13:   0.2171 L23:   0.3085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0494 S12:   0.0066 S13:   0.0474                       
REMARK   3      S21:   0.0610 S22:  -0.0565 S23:   0.0624                       
REMARK   3      S31:   0.0922 S32:   0.0242 S33:   0.0071                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   101        B   475                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3290  77.7690   8.0230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1837 T22:   0.2949                                     
REMARK   3      T33:   0.0140 T12:   0.0042                                     
REMARK   3      T13:  -0.0202 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6196 L22:   0.3369                                     
REMARK   3      L33:   1.7729 L12:   0.0379                                     
REMARK   3      L13:  -0.1945 L23:   0.0260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0920 S12:  -0.0690 S13:  -0.0498                       
REMARK   3      S21:  -0.1130 S22:  -0.0258 S23:   0.0331                       
REMARK   3      S31:  -0.1308 S32:   0.0249 S33:   0.1178                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5DU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213808.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.953                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52693                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
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         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2OAY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350 W/V AND 200 MM KF WITH A     
REMARK 280  CRYSTALLIZATION DROP SIZE OF 1 MICROLITRE AND A PROTEIN CONTENT     
REMARK 280  OF 70% W/V, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  293K                                                                
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       28.70500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.98000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.69000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.98000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.70500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.69000            
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     THR A    97                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     ALA A   478                                                      
REMARK 465     THR B    97                                                      
REMARK 465     GLY B    98                                                      
REMARK 465     SER B    99                                                      
REMARK 465     PHE B   100                                                      
REMARK 465     ALA B   478                                                      
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     ALA A 439    O                                                   
REMARK 470     ILE A 440    O                                                   
REMARK 470     SER A 441    O                                                   
REMARK 470     SER B 438    O                                                   
REMARK 470     ALA B 439    O                                                   
REMARK 470     ILE B 440    O                                                   
REMARK 470     SER B 441    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 165   C     GLU A 165   O       0.162                       
REMARK 500    GLU A 450   CD    GLU A 450   OE1     0.069                       
REMARK 500    GLU B 165   CG    GLU B 165   CD      0.123                       
REMARK 500    GLU B 165   C     GLU B 165   O       0.131                       
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    ASP A 207   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 282   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    LEU A 459   CB  -  CG  -  CD2 ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG B 227   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B 227   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP B 282   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 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    GLU A 142       57.98   -140.23                                   
REMARK 500    GLU A 165     -130.64     54.86                                   
REMARK 500    ASN A 249       48.90     38.61                                   
REMARK 500    ASN A 250       14.82     59.89                                   
REMARK 500    ASP A 262       30.93    -95.78                                   
REMARK 500    LYS A 294     -143.25     64.23                                   
REMARK 500    LYS A 307       47.86   -147.41                                   
REMARK 500    LEU A 405       52.81   -108.49                                   
REMARK 500    THR A 428     -156.93   -110.70                                   
REMARK 500    ILE A 440     -110.79     89.30                                   
REMARK 500    VAL A 442      -64.14     50.32                                   
REMARK 500    GLU B 165     -130.97     55.38                                   
REMARK 500    MET B 288      109.71    -59.40                                   
REMARK 500    LYS B 294     -144.59     60.46                                   
REMARK 500    LYS B 307       53.89   -148.65                                   
REMARK 500    LEU B 405       56.72   -105.34                                   
REMARK 500    THR B 428     -155.22   -107.53                                   
REMARK 500    ALA B 437      172.86     64.78                                   
REMARK 500    ALA B 439       77.28     63.96                                   
REMARK 500    SER B 441      145.79     74.90                                   
REMARK 500    VAL B 442      -36.71   -173.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5DU3 A   97   478  UNP    P05155   IC1_HUMAN      119    500             
DBREF  5DU3 B   97   478  UNP    P05155   IC1_HUMAN      119    500             
SEQRES   1 A  382  THR GLY SER PHE CYS PRO GLY PRO VAL THR LEU CYS SER          
SEQRES   2 A  382  ASP LEU GLU SER HIS SER THR GLU ALA VAL LEU GLY ASP          
SEQRES   3 A  382  ALA LEU VAL ASP PHE SER LEU LYS LEU TYR HIS ALA PHE          
SEQRES   4 A  382  SER ALA MET LYS LYS VAL GLU THR ASN MET ALA PHE SER          
SEQRES   5 A  382  PRO PHE SER ILE ALA SER LEU LEU THR GLN VAL LEU LEU          
SEQRES   6 A  382  GLY ALA GLY GLU ASN THR LYS THR ASN LEU GLU SER ILE          
SEQRES   7 A  382  LEU SER TYR PRO LYS ASP PHE THR CYS VAL HIS GLN ALA          
SEQRES   8 A  382  LEU LYS GLY PHE THR THR LYS GLY VAL THR SER VAL SER          
SEQRES   9 A  382  GLN ILE PHE HIS SER PRO ASP LEU ALA ILE ARG ASP THR          
SEQRES  10 A  382  PHE VAL ASN ALA SER ARG THR LEU TYR SER SER SER PRO          
SEQRES  11 A  382  ARG VAL LEU SER ASN ASN SER ASP ALA ASN LEU GLU LEU          
SEQRES  12 A  382  ILE ASN THR TRP VAL ALA LYS ASN THR ASN ASN LYS ILE          
SEQRES  13 A  382  SER ARG LEU LEU ASP SER LEU PRO SER ASP THR ARG LEU          
SEQRES  14 A  382  VAL LEU LEU ASN ALA ILE TYR LEU SER ALA LYS TRP LYS          
SEQRES  15 A  382  THR THR PHE ASP PRO LYS LYS THR ARG MET GLU PRO PHE          
SEQRES  16 A  382  HIS PHE LYS ASN SER VAL ILE LYS VAL PRO MET MET ASN          
SEQRES  17 A  382  SER LYS LYS TYR PRO VAL ALA HIS PHE ILE ASP GLN THR          
SEQRES  18 A  382  LEU LYS ALA LYS VAL GLY GLN LEU GLN LEU SER HIS ASN          
SEQRES  19 A  382  LEU SER LEU VAL ILE LEU VAL PRO GLN ASN LEU LYS HIS          
SEQRES  20 A  382  ARG LEU GLU ASP MET GLU GLN ALA LEU SER PRO SER VAL          
SEQRES  21 A  382  PHE LYS ALA ILE MET GLU LYS LEU GLU MET SER LYS PHE          
SEQRES  22 A  382  GLN PRO THR LEU LEU THR LEU PRO ARG ILE LYS VAL THR          
SEQRES  23 A  382  THR SER GLN ASP MET LEU SER ILE MET GLU LYS LEU GLU          
SEQRES  24 A  382  PHE PHE ASP PHE SER TYR ASP LEU ASN LEU CYS GLY LEU          
SEQRES  25 A  382  THR GLU ASP PRO ASP LEU GLN VAL SER ALA MET GLN HIS          
SEQRES  26 A  382  GLN THR VAL LEU GLU LEU THR GLU THR GLY VAL GLU ALA          
SEQRES  27 A  382  ALA ALA ALA SER ALA ILE SER VAL ALA ARG THR LEU LEU          
SEQRES  28 A  382  VAL PHE GLU VAL GLN GLN PRO PHE LEU PHE VAL LEU TRP          
SEQRES  29 A  382  ASP GLN GLN HIS LYS PHE PRO VAL PHE MET GLY ARG VAL          
SEQRES  30 A  382  TYR ASP PRO ARG ALA                                          
SEQRES   1 B  382  THR GLY SER PHE CYS PRO GLY PRO VAL THR LEU CYS SER          
SEQRES   2 B  382  ASP LEU GLU SER HIS SER THR GLU ALA VAL LEU GLY ASP          
SEQRES   3 B  382  ALA LEU VAL ASP PHE SER LEU LYS LEU TYR HIS ALA PHE          
SEQRES   4 B  382  SER ALA MET LYS LYS VAL GLU THR ASN MET ALA PHE SER          
SEQRES   5 B  382  PRO PHE SER ILE ALA SER LEU LEU THR GLN VAL LEU LEU          
SEQRES   6 B  382  GLY ALA GLY GLU ASN THR LYS THR ASN LEU GLU SER ILE          
SEQRES   7 B  382  LEU SER TYR PRO LYS ASP PHE THR CYS VAL HIS GLN ALA          
SEQRES   8 B  382  LEU LYS GLY PHE THR THR LYS GLY VAL THR SER VAL SER          
SEQRES   9 B  382  GLN ILE PHE HIS SER PRO ASP LEU ALA ILE ARG ASP THR          
SEQRES  10 B  382  PHE VAL ASN ALA SER ARG THR LEU TYR SER SER SER PRO          
SEQRES  11 B  382  ARG VAL LEU SER ASN ASN SER ASP ALA ASN LEU GLU LEU          
SEQRES  12 B  382  ILE ASN THR TRP VAL ALA LYS ASN THR ASN ASN LYS ILE          
SEQRES  13 B  382  SER ARG LEU LEU ASP SER LEU PRO SER ASP THR ARG LEU          
SEQRES  14 B  382  VAL LEU LEU ASN ALA ILE TYR LEU SER ALA LYS TRP LYS          
SEQRES  15 B  382  THR THR PHE ASP PRO LYS LYS THR ARG MET GLU PRO PHE          
SEQRES  16 B  382  HIS PHE LYS ASN SER VAL ILE LYS VAL PRO MET MET ASN          
SEQRES  17 B  382  SER LYS LYS TYR PRO VAL ALA HIS PHE ILE ASP GLN THR          
SEQRES  18 B  382  LEU LYS ALA LYS VAL GLY GLN LEU GLN LEU SER HIS ASN          
SEQRES  19 B  382  LEU SER LEU VAL ILE LEU VAL PRO GLN ASN LEU LYS HIS          
SEQRES  20 B  382  ARG LEU GLU ASP MET GLU GLN ALA LEU SER PRO SER VAL          
SEQRES  21 B  382  PHE LYS ALA ILE MET GLU LYS LEU GLU MET SER LYS PHE          
SEQRES  22 B  382  GLN PRO THR LEU LEU THR LEU PRO ARG ILE LYS VAL THR          
SEQRES  23 B  382  THR SER GLN ASP MET LEU SER ILE MET GLU LYS LEU GLU          
SEQRES  24 B  382  PHE PHE ASP PHE SER TYR ASP LEU ASN LEU CYS GLY LEU          
SEQRES  25 B  382  THR GLU ASP PRO ASP LEU GLN VAL SER ALA MET GLN HIS          
SEQRES  26 B  382  GLN THR VAL LEU GLU LEU THR GLU THR GLY VAL GLU ALA          
SEQRES  27 B  382  ALA ALA ALA SER ALA ILE SER VAL ALA ARG THR LEU LEU          
SEQRES  28 B  382  VAL PHE GLU VAL GLN GLN PRO PHE LEU PHE VAL LEU TRP          
SEQRES  29 B  382  ASP GLN GLN HIS LYS PHE PRO VAL PHE MET GLY ARG VAL          
SEQRES  30 B  382  TYR ASP PRO ARG ALA                                          
FORMUL   3  HOH   *151(H2 O)                                                    
HELIX    1 AA1 SER A  109  THR A  116  1                                   8    
HELIX    2 AA2 THR A  116  LYS A  139  1                                  24    
HELIX    3 AA3 SER A  148  LEU A  161  1                                  14    
HELIX    4 AA4 GLY A  164  SER A  176  1                                  13    
HELIX    5 AA5 CYS A  183  PHE A  191  1                                   9    
HELIX    6 AA6 ARG A  211  SER A  223  1                                  13    
HELIX    7 AA7 ASN A  232  THR A  248  1                                  17    
HELIX    8 AA8 ASP A  282  THR A  286  5                                   5    
HELIX    9 AA9 ARG A  344  LEU A  352  1                                   9    
HELIX   10 AB1 SER A  353  MET A  366  1                                  14    
HELIX   11 AB2 MET A  387  LEU A  394  1                                   8    
HELIX   12 AB3 SER B  109  SER B  115  1                                   7    
HELIX   13 AB4 THR B  116  LYS B  139  1                                  24    
HELIX   14 AB5 SER B  148  LEU B  161  1                                  14    
HELIX   15 AB6 GLY B  164  SER B  176  1                                  13    
HELIX   16 AB7 CYS B  183  PHE B  191  1                                   9    
HELIX   17 AB8 ARG B  211  TYR B  222  1                                  12    
HELIX   18 AB9 ASN B  232  THR B  248  1                                  17    
HELIX   19 AC1 ASP B  282  THR B  286  5                                   5    
HELIX   20 AC2 ARG B  344  LEU B  352  1                                   9    
HELIX   21 AC3 SER B  353  SER B  367  1                                  15    
HELIX   22 AC4 MET B  387  LEU B  394  1                                   8    
SHEET    1 AA1 7 MET A 145  PHE A 147  0                                        
SHEET    2 AA1 7 PHE A 466  VAL A 473 -1  O  ARG A 472   N  MET A 145           
SHEET    3 AA1 7 PHE A 455  ASP A 461 -1  N  ASP A 461   O  PHE A 466           
SHEET    4 AA1 7 LEU A 331  PRO A 338 -1  N  VAL A 334   O  VAL A 458           
SHEET    5 AA1 7 ALA A 320  GLN A 326 -1  N  GLY A 323   O  ILE A 335           
SHEET    6 AA1 7 SER A 296  ASP A 315 -1  N  ALA A 311   O  GLN A 324           
SHEET    7 AA1 7 ARG A 287  PHE A 293 -1  N  PHE A 291   O  ILE A 298           
SHEET    1 AA2 8 MET A 145  PHE A 147  0                                        
SHEET    2 AA2 8 PHE A 466  VAL A 473 -1  O  ARG A 472   N  MET A 145           
SHEET    3 AA2 8 PHE A 455  ASP A 461 -1  N  ASP A 461   O  PHE A 466           
SHEET    4 AA2 8 LEU A 331  PRO A 338 -1  N  VAL A 334   O  VAL A 458           
SHEET    5 AA2 8 ALA A 320  GLN A 326 -1  N  GLY A 323   O  ILE A 335           
SHEET    6 AA2 8 SER A 296  ASP A 315 -1  N  ALA A 311   O  GLN A 324           
SHEET    7 AA2 8 GLN A 370  PRO A 377 -1  O  LEU A 376   N  MET A 303           
SHEET    8 AA2 8 LEU A 447  GLU A 450  1  O  LEU A 447   N  LEU A 373           
SHEET    1 AA3 5 ARG A 227  VAL A 228  0                                        
SHEET    2 AA3 5 VAL A 196  HIS A 204  1  N  ILE A 202   O  ARG A 227           
SHEET    3 AA3 5 LEU A 265  LEU A 273 -1  O  ALA A 270   N  VAL A 199           
SHEET    4 AA3 5 ALA A 418  LEU A 427  1  O  GLN A 422   N  ILE A 271           
SHEET    5 AA3 5 ILE A 379  ASP A 386 -1  N  ILE A 379   O  LEU A 427           
SHEET    1 AA4 2 TRP A 277  THR A 279  0                                        
SHEET    2 AA4 2 GLY A 431  GLU A 433  1  O  GLU A 433   N  LYS A 278           
SHEET    1 AA5 7 MET B 145  PHE B 147  0                                        
SHEET    2 AA5 7 PHE B 466  VAL B 473 -1  O  ARG B 472   N  MET B 145           
SHEET    3 AA5 7 PHE B 455  ASP B 461 -1  N  ASP B 461   O  PHE B 466           
SHEET    4 AA5 7 LEU B 331  PRO B 338 -1  N  VAL B 334   O  VAL B 458           
SHEET    5 AA5 7 ALA B 320  GLN B 326 -1  N  GLY B 323   O  ILE B 335           
SHEET    6 AA5 7 SER B 296  ASP B 315 -1  N  ALA B 311   O  GLN B 324           
SHEET    7 AA5 7 ARG B 287  PHE B 293 -1  N  PHE B 291   O  ILE B 298           
SHEET    1 AA6 8 MET B 145  PHE B 147  0                                        
SHEET    2 AA6 8 PHE B 466  VAL B 473 -1  O  ARG B 472   N  MET B 145           
SHEET    3 AA6 8 PHE B 455  ASP B 461 -1  N  ASP B 461   O  PHE B 466           
SHEET    4 AA6 8 LEU B 331  PRO B 338 -1  N  VAL B 334   O  VAL B 458           
SHEET    5 AA6 8 ALA B 320  GLN B 326 -1  N  GLY B 323   O  ILE B 335           
SHEET    6 AA6 8 SER B 296  ASP B 315 -1  N  ALA B 311   O  GLN B 324           
SHEET    7 AA6 8 GLN B 370  PRO B 377 -1  O  LEU B 376   N  MET B 303           
SHEET    8 AA6 8 LEU B 447  GLU B 450  1  O  LEU B 447   N  LEU B 373           
SHEET    1 AA7 5 ARG B 227  VAL B 228  0                                        
SHEET    2 AA7 5 VAL B 196  HIS B 204  1  N  ILE B 202   O  ARG B 227           
SHEET    3 AA7 5 LEU B 265  LEU B 273 -1  O  ALA B 270   N  VAL B 199           
SHEET    4 AA7 5 ALA B 418  LEU B 427  1  O  ALA B 418   N  LEU B 267           
SHEET    5 AA7 5 ILE B 379  ASP B 386 -1  N  ILE B 379   O  LEU B 427           
SHEET    1 AA8 2 TRP B 277  THR B 279  0                                        
SHEET    2 AA8 2 GLY B 431  GLU B 433  1  O  GLU B 433   N  LYS B 278           
SSBOND   1 CYS A  101    CYS A  406                          1555   1555  2.08  
SSBOND   2 CYS A  108    CYS A  183                          1555   1555  2.10  
SSBOND   3 CYS B  101    CYS B  406                          1555   1555  2.15  
SSBOND   4 CYS B  108    CYS B  183                          1555   1555  2.07  
CRYST1   57.410   75.380  203.960  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      0.017419  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013266  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004903        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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