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Database: PDB
Entry: 5DUQ
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Original site: 5DUQ 
HEADER    HYDROLASE                               20-SEP-15   5DUQ              
TITLE     ACTIVE HUMAN C1-INHIBITOR IN COMPLEX WITH DEXTRAN SULFATE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLASMA PROTEASE C1 INHIBITOR;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: C1INH,C1 ESTERASE INHIBITOR,C1-INHIBITING FACTOR,SERPIN G1; 
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: SERPING1, C1IN, C1NH;                                          
SOURCE   6 EXPRESSION_SYSTEM: ORYCTOLAGUS CUNICULUS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9986                                        
KEYWDS    SERINE PROTEIN INHIBITOR, COMPLEX WITH GLYCOSAMINOGLYCAN, HYDROLASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DIJK,J.HOLKERS,P.VOSKAMP,B.M.GIANNETTI,W.J.WATERREUS,H.A.VAN VEEN,  
AUTHOR   2 N.S.PANNU                                                            
REVDAT   3   29-JUL-20 5DUQ    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   25-JAN-17 5DUQ    1       JRNL                                     
REVDAT   1   31-AUG-16 5DUQ    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.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24919                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1294                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1856                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 111                          
REMARK   3   BIN FREE R VALUE                    : 0.4460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5749                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 24                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 94.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.70000                                              
REMARK   3    B22 (A**2) : -5.72000                                             
REMARK   3    B33 (A**2) : -2.34000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.33000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.310         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.399         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.442         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.283        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5940 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5775 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8056 ; 1.589 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13337 ; 1.175 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   725 ; 7.434 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   242 ;38.067 ;24.917       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1066 ;15.997 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;20.551 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   965 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6511 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1295 ; 0.003 ; 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):  2906 ; 6.502 ; 9.176       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2905 ; 6.501 ; 9.176       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3629 ;10.412 ;13.753       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3630 ;10.411 ;13.753       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3032 ; 6.433 ; 9.788       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3029 ; 6.424 ; 9.782       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4425 ;10.509 ;14.421       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6374 ;15.285 ;71.783       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6375 ;15.284 ;71.796       
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   115    475       B   115    475   47194  0.06  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5DUQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213811.                                   
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                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26376                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11 MG/ML OF C1-INHIBITOR WAS MIXED       
REMARK 280  WITH 5KDA DEXTRAN SULFATE IN A 1:2 MOLAR RATIO AND INCUBATED ON     
REMARK 280  ICE FOR AN HOUR. CRYSTALS GREW IN0.1 M SPG (PH 9), 25% W/V PEG      
REMARK 280  1500 0.1 M MGCL HEXAHYDRATE AFTER 10 DAYS., VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       56.05000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.71200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       56.05000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       98.71200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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    96                                                      
REMARK 465     THR A    97                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     PHE A   100                                                      
REMARK 465     CYS A   101                                                      
REMARK 465     PRO A   102                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     VAL A   105                                                      
REMARK 465     THR A   106                                                      
REMARK 465     LEU A   107                                                      
REMARK 465     CYS A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     ASP A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     GLU A   112                                                      
REMARK 465     SER A   113                                                      
REMARK 465     HIS A   114                                                      
REMARK 465     ARG A   477                                                      
REMARK 465     ALA A   478                                                      
REMARK 465     THR B    96                                                      
REMARK 465     THR B    97                                                      
REMARK 465     GLY B    98                                                      
REMARK 465     SER B    99                                                      
REMARK 465     PHE B   100                                                      
REMARK 465     CYS B   101                                                      
REMARK 465     PRO B   102                                                      
REMARK 465     GLY B   103                                                      
REMARK 465     PRO B   104                                                      
REMARK 465     VAL B   105                                                      
REMARK 465     THR B   106                                                      
REMARK 465     LEU B   107                                                      
REMARK 465     CYS B   108                                                      
REMARK 465     SER B   109                                                      
REMARK 465     ASP B   110                                                      
REMARK 465     LEU B   111                                                      
REMARK 465     ARG B   477                                                      
REMARK 465     ALA B   478                                                      
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   OG1  THR A   317     CE   LYS A   363     2656     2.15            
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    LYS A 140     -174.35    -65.26                                   
REMARK 500    GLU A 165      -83.87     50.46                                   
REMARK 500    THR A 192      123.06    -38.87                                   
REMARK 500    SER A 200       89.97   -163.42                                   
REMARK 500    SER A 223       61.75     31.43                                   
REMARK 500    SER A 224     -179.47   -172.40                                   
REMARK 500    SER A 230     -172.53    -50.31                                   
REMARK 500    PRO A 260      177.18    -58.04                                   
REMARK 500    ASP A 262       32.47    -90.22                                   
REMARK 500    ASN A 269       99.02   -161.08                                   
REMARK 500    LYS A 285       55.85    -95.58                                   
REMARK 500    LYS A 294     -126.19     54.88                                   
REMARK 500    LYS A 319       69.32     61.74                                   
REMARK 500    LYS A 380       87.07   -151.56                                   
REMARK 500    ASP A 386       99.91    -68.33                                   
REMARK 500    LEU A 405       60.67   -108.39                                   
REMARK 500    THR A 428     -151.82   -109.20                                   
REMARK 500    SER A 438        0.24     54.12                                   
REMARK 500    SER A 441     -163.33   -115.33                                   
REMARK 500    VAL A 442       79.16   -116.48                                   
REMARK 500    ARG A 444      -70.60     90.47                                   
REMARK 500    LYS A 465       60.49     65.31                                   
REMARK 500    SER B 113     -138.81    -88.16                                   
REMARK 500    HIS B 114      -56.52     64.32                                   
REMARK 500    SER B 115      -48.67    -19.96                                   
REMARK 500    LYS B 140     -174.42    -64.79                                   
REMARK 500    GLU B 165      -86.85     54.95                                   
REMARK 500    THR B 192      122.69    -38.34                                   
REMARK 500    SER B 200       90.36   -162.75                                   
REMARK 500    SER B 223       62.34     29.44                                   
REMARK 500    SER B 230     -173.96    -49.34                                   
REMARK 500    PRO B 260      176.30    -59.00                                   
REMARK 500    ASP B 262       32.17    -88.97                                   
REMARK 500    ASN B 269       98.83   -161.47                                   
REMARK 500    LYS B 285       56.51    -96.13                                   
REMARK 500    LYS B 294     -125.81     54.90                                   
REMARK 500    LYS B 319       69.55     60.99                                   
REMARK 500    LYS B 380       87.43   -151.85                                   
REMARK 500    LEU B 405       61.18   -108.33                                   
REMARK 500    THR B 428     -151.66   -109.06                                   
REMARK 500    SER B 438       -0.01     54.43                                   
REMARK 500    SER B 441     -162.63   -115.18                                   
REMARK 500    ARG B 444      -28.11     87.23                                   
REMARK 500    LYS B 465       60.73     64.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE METABOLISM                            
REMARK 630 MOLECULE NAME: ALPHA-D-GLUCOPYRANOSE                                 
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     GLC A   502                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP: NULL                                                        
REMARK 630 DETAILS: OLIGOSACCHARIDE                                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DU3   RELATED DB: PDB                                   
REMARK 900 5DU3 IS UNCOMPLEXED ACTIVE HUMAN C1-INHIBITOR                        
DBREF  5DUQ A   96   478  UNP    P05155   IC1_HUMAN      118    500             
DBREF  5DUQ B   96   478  UNP    P05155   IC1_HUMAN      118    500             
SEQADV 5DUQ MET A  458  UNP  P05155    VAL   480 CONFLICT                       
SEQADV 5DUQ MET B  458  UNP  P05155    VAL   480 CONFLICT                       
SEQRES   1 A  383  THR THR GLY SER PHE CYS PRO GLY PRO VAL THR LEU CYS          
SEQRES   2 A  383  SER ASP LEU GLU SER HIS SER THR GLU ALA VAL LEU GLY          
SEQRES   3 A  383  ASP ALA LEU VAL ASP PHE SER LEU LYS LEU TYR HIS ALA          
SEQRES   4 A  383  PHE SER ALA MET LYS LYS VAL GLU THR ASN MET ALA PHE          
SEQRES   5 A  383  SER PRO PHE SER ILE ALA SER LEU LEU THR GLN VAL LEU          
SEQRES   6 A  383  LEU GLY ALA GLY GLU ASN THR LYS THR ASN LEU GLU SER          
SEQRES   7 A  383  ILE LEU SER TYR PRO LYS ASP PHE THR CYS VAL HIS GLN          
SEQRES   8 A  383  ALA LEU LYS GLY PHE THR THR LYS GLY VAL THR SER VAL          
SEQRES   9 A  383  SER GLN ILE PHE HIS SER PRO ASP LEU ALA ILE ARG ASP          
SEQRES  10 A  383  THR PHE VAL ASN ALA SER ARG THR LEU TYR SER SER SER          
SEQRES  11 A  383  PRO ARG VAL LEU SER ASN ASN SER ASP ALA ASN LEU GLU          
SEQRES  12 A  383  LEU ILE ASN THR TRP VAL ALA LYS ASN THR ASN ASN LYS          
SEQRES  13 A  383  ILE SER ARG LEU LEU ASP SER LEU PRO SER ASP THR ARG          
SEQRES  14 A  383  LEU VAL LEU LEU ASN ALA ILE TYR LEU SER ALA LYS TRP          
SEQRES  15 A  383  LYS THR THR PHE ASP PRO LYS LYS THR ARG MET GLU PRO          
SEQRES  16 A  383  PHE HIS PHE LYS ASN SER VAL ILE LYS VAL PRO MET MET          
SEQRES  17 A  383  ASN SER LYS LYS TYR PRO VAL ALA HIS PHE ILE ASP GLN          
SEQRES  18 A  383  THR LEU LYS ALA LYS VAL GLY GLN LEU GLN LEU SER HIS          
SEQRES  19 A  383  ASN LEU SER LEU VAL ILE LEU VAL PRO GLN ASN LEU LYS          
SEQRES  20 A  383  HIS ARG LEU GLU ASP MET GLU GLN ALA LEU SER PRO SER          
SEQRES  21 A  383  VAL PHE LYS ALA ILE MET GLU LYS LEU GLU MET SER LYS          
SEQRES  22 A  383  PHE GLN PRO THR LEU LEU THR LEU PRO ARG ILE LYS VAL          
SEQRES  23 A  383  THR THR SER GLN ASP MET LEU SER ILE MET GLU LYS LEU          
SEQRES  24 A  383  GLU PHE PHE ASP PHE SER TYR ASP LEU ASN LEU CYS GLY          
SEQRES  25 A  383  LEU THR GLU ASP PRO ASP LEU GLN VAL SER ALA MET GLN          
SEQRES  26 A  383  HIS GLN THR VAL LEU GLU LEU THR GLU THR GLY VAL GLU          
SEQRES  27 A  383  ALA ALA ALA ALA SER ALA ILE SER VAL ALA ARG THR LEU          
SEQRES  28 A  383  LEU VAL PHE GLU VAL GLN GLN PRO PHE LEU PHE MET LEU          
SEQRES  29 A  383  TRP ASP GLN GLN HIS LYS PHE PRO VAL PHE MET GLY ARG          
SEQRES  30 A  383  VAL TYR ASP PRO ARG ALA                                      
SEQRES   1 B  383  THR THR GLY SER PHE CYS PRO GLY PRO VAL THR LEU CYS          
SEQRES   2 B  383  SER ASP LEU GLU SER HIS SER THR GLU ALA VAL LEU GLY          
SEQRES   3 B  383  ASP ALA LEU VAL ASP PHE SER LEU LYS LEU TYR HIS ALA          
SEQRES   4 B  383  PHE SER ALA MET LYS LYS VAL GLU THR ASN MET ALA PHE          
SEQRES   5 B  383  SER PRO PHE SER ILE ALA SER LEU LEU THR GLN VAL LEU          
SEQRES   6 B  383  LEU GLY ALA GLY GLU ASN THR LYS THR ASN LEU GLU SER          
SEQRES   7 B  383  ILE LEU SER TYR PRO LYS ASP PHE THR CYS VAL HIS GLN          
SEQRES   8 B  383  ALA LEU LYS GLY PHE THR THR LYS GLY VAL THR SER VAL          
SEQRES   9 B  383  SER GLN ILE PHE HIS SER PRO ASP LEU ALA ILE ARG ASP          
SEQRES  10 B  383  THR PHE VAL ASN ALA SER ARG THR LEU TYR SER SER SER          
SEQRES  11 B  383  PRO ARG VAL LEU SER ASN ASN SER ASP ALA ASN LEU GLU          
SEQRES  12 B  383  LEU ILE ASN THR TRP VAL ALA LYS ASN THR ASN ASN LYS          
SEQRES  13 B  383  ILE SER ARG LEU LEU ASP SER LEU PRO SER ASP THR ARG          
SEQRES  14 B  383  LEU VAL LEU LEU ASN ALA ILE TYR LEU SER ALA LYS TRP          
SEQRES  15 B  383  LYS THR THR PHE ASP PRO LYS LYS THR ARG MET GLU PRO          
SEQRES  16 B  383  PHE HIS PHE LYS ASN SER VAL ILE LYS VAL PRO MET MET          
SEQRES  17 B  383  ASN SER LYS LYS TYR PRO VAL ALA HIS PHE ILE ASP GLN          
SEQRES  18 B  383  THR LEU LYS ALA LYS VAL GLY GLN LEU GLN LEU SER HIS          
SEQRES  19 B  383  ASN LEU SER LEU VAL ILE LEU VAL PRO GLN ASN LEU LYS          
SEQRES  20 B  383  HIS ARG LEU GLU ASP MET GLU GLN ALA LEU SER PRO SER          
SEQRES  21 B  383  VAL PHE LYS ALA ILE MET GLU LYS LEU GLU MET SER LYS          
SEQRES  22 B  383  PHE GLN PRO THR LEU LEU THR LEU PRO ARG ILE LYS VAL          
SEQRES  23 B  383  THR THR SER GLN ASP MET LEU SER ILE MET GLU LYS LEU          
SEQRES  24 B  383  GLU PHE PHE ASP PHE SER TYR ASP LEU ASN LEU CYS GLY          
SEQRES  25 B  383  LEU THR GLU ASP PRO ASP LEU GLN VAL SER ALA MET GLN          
SEQRES  26 B  383  HIS GLN THR VAL LEU GLU LEU THR GLU THR GLY VAL GLU          
SEQRES  27 B  383  ALA ALA ALA ALA SER ALA ILE SER VAL ALA ARG THR LEU          
SEQRES  28 B  383  LEU VAL PHE GLU VAL GLN GLN PRO PHE LEU PHE MET LEU          
SEQRES  29 B  383  TRP ASP GLN GLN HIS LYS PHE PRO VAL PHE MET GLY ARG          
SEQRES  30 B  383  VAL TYR ASP PRO ARG ALA                                      
HET    GLC  C   1      12                                                       
HET    BGC  C   2      11                                                       
HET    NAG  A 501      14                                                       
HET    GLC  A 502      12                                                       
HET    NAG  B 501      14                                                       
HET    SO3  B 504       4                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     BGC BETA-D-GLUCOPYRANOSE                                             
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO3 SULFITE ION                                                      
FORMUL   3  GLC    2(C6 H12 O6)                                                 
FORMUL   3  BGC    C6 H12 O6                                                    
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   7  SO3    O3 S 2-                                                      
FORMUL   8  HOH   *24(H2 O)                                                     
HELIX    1 AA1 SER A  115  LYS A  139  1                                  25    
HELIX    2 AA2 SER A  148  GLY A  162  1                                  15    
HELIX    3 AA3 GLY A  164  LEU A  175  1                                  12    
HELIX    4 AA4 CYS A  183  THR A  192  1                                  10    
HELIX    5 AA5 ARG A  211  TYR A  222  1                                  12    
HELIX    6 AA6 ASN A  232  ASN A  247  1                                  16    
HELIX    7 AA7 ASP A  282  THR A  286  5                                   5    
HELIX    8 AA8 ARG A  344  GLN A  350  1                                   7    
HELIX    9 AA9 SER A  353  SER A  367  1                                  15    
HELIX   10 AB1 MET A  387  LEU A  394  1                                   8    
HELIX   11 AB2 ALA A  435  ILE A  440  5                                   6    
HELIX   12 AB3 HIS B  114  LYS B  139  1                                  26    
HELIX   13 AB4 SER B  148  GLY B  162  1                                  15    
HELIX   14 AB5 GLY B  164  LEU B  175  1                                  12    
HELIX   15 AB6 CYS B  183  THR B  192  1                                  10    
HELIX   16 AB7 ARG B  211  TYR B  222  1                                  12    
HELIX   17 AB8 ASN B  232  THR B  248  1                                  17    
HELIX   18 AB9 ASP B  282  THR B  286  5                                   5    
HELIX   19 AC1 ARG B  344  GLN B  350  1                                   7    
HELIX   20 AC2 SER B  353  SER B  367  1                                  15    
HELIX   21 AC3 MET B  387  LEU B  394  1                                   8    
HELIX   22 AC4 ALA B  435  ILE B  440  5                                   6    
SHEET    1 AA1 7 MET A 145  PHE A 147  0                                        
SHEET    2 AA1 7 PHE A 466  VAL A 473 -1  O  MET A 470   N  PHE A 147           
SHEET    3 AA1 7 PHE A 455  ASP A 461 -1  N  PHE A 455   O  VAL A 473           
SHEET    4 AA1 7 LEU A 331  PRO A 338 -1  N  LEU A 336   O  LEU A 456           
SHEET    5 AA1 7 ALA A 320  GLN A 326 -1  N  LYS A 321   O  VAL A 337           
SHEET    6 AA1 7 ILE A 298  ASP A 315 -1  N  ALA A 311   O  GLN A 324           
SHEET    7 AA1 7 MET A 288  PHE A 291 -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  MET A 470   N  PHE A 147           
SHEET    3 AA2 8 PHE A 455  ASP A 461 -1  N  PHE A 455   O  VAL A 473           
SHEET    4 AA2 8 LEU A 331  PRO A 338 -1  N  LEU A 336   O  LEU A 456           
SHEET    5 AA2 8 ALA A 320  GLN A 326 -1  N  LYS A 321   O  VAL A 337           
SHEET    6 AA2 8 ILE A 298  ASP A 315 -1  N  ALA A 311   O  GLN A 324           
SHEET    7 AA2 8 GLN A 370  PRO A 377 -1  O  THR A 372   N  TYR A 308           
SHEET    8 AA2 8 VAL A 448  GLU A 450  1  O  PHE A 449   N  LEU A 373           
SHEET    1 AA3 5 VAL A 196  VAL A 199  0                                        
SHEET    2 AA3 5 ALA A 270  LEU A 273 -1  O  TYR A 272   N  THR A 197           
SHEET    3 AA3 5 ALA A 418  LEU A 427  1  O  VAL A 424   N  ILE A 271           
SHEET    4 AA3 5 LEU A 265  LEU A 267  1  N  LEU A 267   O  ALA A 418           
SHEET    5 AA3 5 ILE A 202  HIS A 204 -1  N  PHE A 203   O  VAL A 266           
SHEET    1 AA4 4 VAL A 196  VAL A 199  0                                        
SHEET    2 AA4 4 ALA A 270  LEU A 273 -1  O  TYR A 272   N  THR A 197           
SHEET    3 AA4 4 ALA A 418  LEU A 427  1  O  VAL A 424   N  ILE A 271           
SHEET    4 AA4 4 ILE A 379  ASP A 386 -1  N  ILE A 379   O  LEU A 427           
SHEET    1 AA5 2 TRP A 277  THR A 279  0                                        
SHEET    2 AA5 2 GLY A 431  GLU A 433  1  O  GLU A 433   N  LYS A 278           
SHEET    1 AA6 7 MET B 145  PHE B 147  0                                        
SHEET    2 AA6 7 PHE B 466  VAL B 473 -1  O  MET B 470   N  PHE B 147           
SHEET    3 AA6 7 PHE B 455  ASP B 461 -1  N  PHE B 455   O  VAL B 473           
SHEET    4 AA6 7 LEU B 331  PRO B 338 -1  N  LEU B 336   O  LEU B 456           
SHEET    5 AA6 7 ALA B 320  GLN B 326 -1  N  LYS B 321   O  VAL B 337           
SHEET    6 AA6 7 ILE B 298  ASP B 315 -1  N  ALA B 311   O  GLN B 324           
SHEET    7 AA6 7 MET B 288  PHE B 291 -1  N  PHE B 291   O  ILE B 298           
SHEET    1 AA7 8 MET B 145  PHE B 147  0                                        
SHEET    2 AA7 8 PHE B 466  VAL B 473 -1  O  MET B 470   N  PHE B 147           
SHEET    3 AA7 8 PHE B 455  ASP B 461 -1  N  PHE B 455   O  VAL B 473           
SHEET    4 AA7 8 LEU B 331  PRO B 338 -1  N  LEU B 336   O  LEU B 456           
SHEET    5 AA7 8 ALA B 320  GLN B 326 -1  N  LYS B 321   O  VAL B 337           
SHEET    6 AA7 8 ILE B 298  ASP B 315 -1  N  ALA B 311   O  GLN B 324           
SHEET    7 AA7 8 GLN B 370  PRO B 377 -1  O  THR B 372   N  TYR B 308           
SHEET    8 AA7 8 VAL B 448  GLU B 450  1  O  PHE B 449   N  LEU B 373           
SHEET    1 AA8 5 VAL B 196  VAL B 199  0                                        
SHEET    2 AA8 5 ALA B 270  LEU B 273 -1  O  TYR B 272   N  THR B 197           
SHEET    3 AA8 5 ALA B 418  LEU B 427  1  O  VAL B 424   N  ILE B 271           
SHEET    4 AA8 5 LEU B 265  LEU B 267  1  N  LEU B 267   O  ALA B 418           
SHEET    5 AA8 5 ILE B 202  HIS B 204 -1  N  PHE B 203   O  VAL B 266           
SHEET    1 AA9 4 VAL B 196  VAL B 199  0                                        
SHEET    2 AA9 4 ALA B 270  LEU B 273 -1  O  TYR B 272   N  THR B 197           
SHEET    3 AA9 4 ALA B 418  LEU B 427  1  O  VAL B 424   N  ILE B 271           
SHEET    4 AA9 4 ILE B 379  ASP B 386 -1  N  ILE B 379   O  LEU B 427           
SHEET    1 AB1 2 TRP B 277  THR B 279  0                                        
SHEET    2 AB1 2 GLY B 431  GLU B 433  1  O  GLU B 433   N  LYS B 278           
LINK         ND2 ASN A 216                 C1  NAG A 501     1555   1555  1.43  
LINK         ND2 ASN B 216                 C1  NAG B 501     1555   1555  1.49  
LINK         S   SO3 B 504                 O2  GLC C   1     1555   1555  1.69  
LINK         O4  GLC C   1                 C1  BGC C   2     1555   1555  1.46  
CRYST1  112.100  197.424   56.779  90.00 103.31  90.00 C 1 2 1       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      0.008921  0.000000  0.002110        0.00000                         
SCALE2      0.000000  0.005065  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018098        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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