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Database: PDB
Entry: 2RD7
LinkDB: 2RD7
Original site: 2RD7 
HEADER    IMMUNE SYSTEM                           21-SEP-07   2RD7              
TITLE     HUMAN COMPLEMENT MEMBRANE ATTACK PROTEINS SHARE A COMMON FOLD WITH    
TITLE    2 BACTERIAL CYTOLYSINS                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT COMPONENT C8 ALPHA CHAIN;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: COMPLEMENT COMPONENT 8 SUBUNIT ALPHA;                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: COMPLEMENT COMPONENT C8 GAMMA CHAIN;                       
COMPND   8 CHAIN: C;                                                            
COMPND   9 SYNONYM: COMPLEMENT COMPONENT 8 SUBUNIT GAMMA;                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: C8A;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 GENE: C8G;                                                           
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
KEYWDS    MEMBRANE ATTACK SYSTEM, CLEAVAGE ON PAIR OF BASIC RESIDUES,           
KEYWDS   2 COMPLEMENT ALTERNATE PATHWAY, COMPLEMENT PATHWAY, CYTOLYSIS, EGF-    
KEYWDS   3 LIKE DOMAIN, GLYCOPROTEIN, IMMUNE RESPONSE, INNATE IMMUNITY,         
KEYWDS   4 MEMBRANE ATTACK COMPLEX, POLYMORPHISM, SECRETED, IMMUNE SYSTEM       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.SLADE,L.L.LOVELACE,M.CHRUSZCZ,W.MINOR,L.LEBIODA,J.M.SODETZ        
REVDAT   3   20-DEC-17 2RD7    1       JRNL                                     
REVDAT   2   24-FEB-09 2RD7    1       VERSN                                    
REVDAT   1   27-MAY-08 2RD7    0                                                
JRNL        AUTH   L.L.LOVELACE,C.L.COOPER,J.M.SODETZ,L.LEBIODA                 
JRNL        TITL   STRUCTURE OF HUMAN C8 PROTEIN PROVIDES MECHANISTIC INSIGHT   
JRNL        TITL 2 INTO MEMBRANE PORE FORMATION BY COMPLEMENT.                  
JRNL        REF    J. BIOL. CHEM.                V. 286 17585 2011              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   21454577                                                     
JRNL        DOI    10.1074/JBC.M111.219766                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 30735                          
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                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1616                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1850                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 108                          
REMARK   3   BIN FREE R VALUE                    : 0.4230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3772                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 166                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11000                                              
REMARK   3    B22 (A**2) : -1.59000                                             
REMARK   3    B33 (A**2) : 1.48000                                              
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): 0.242         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.177         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.003        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3933 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3469 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5328 ; 1.630 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8014 ; 0.886 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   493 ; 7.395 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;34.382 ;23.716       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   630 ;16.557 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;19.409 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   579 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4465 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   857 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   782 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3487 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1924 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2329 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   190 ; 0.183 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    29 ; 0.223 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    63 ; 0.256 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.081 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2485 ; 1.022 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1022 ; 0.227 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3898 ; 1.705 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1643 ; 2.323 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1430 ; 3.613 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2RD7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044718.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9565                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32462                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, DM, SHELXD, RESOLVE, CCP4,         
REMARK 200  MOLREP                                                              
REMARK 200 STARTING MODEL: LOWER RESOLUTION MODEL SOLVED BY SAD                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 20,000, 0.1 M CITRIC ACID,        
REMARK 280  0.025 M MG(NO3)2, PH 5.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       48.27650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.04350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.27650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.04350            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2160 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     HIS A    96                                                      
REMARK 465     HIS A    97                                                      
REMARK 465     HIS A    98                                                      
REMARK 465     HIS A    99                                                      
REMARK 465     HIS A   100                                                      
REMARK 465     HIS A   101                                                      
REMARK 465     MET A   102                                                      
REMARK 465     VAL A   103                                                      
REMARK 465     ARG A   104                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     ILE A   106                                                      
REMARK 465     ASP A   107                                                      
REMARK 465     GLU A   108                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     PRO A   226                                                      
REMARK 465     ALA A   227                                                      
REMARK 465     GLU A   355                                                      
REMARK 465     ASP A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     ILE A   358                                                      
REMARK 465     ASN A   359                                                      
REMARK 465     VAL A   360                                                      
REMARK 465     GLY A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     LEU A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     SER A   398                                                      
REMARK 465     GLY A   399                                                      
REMARK 465     TRP A   400                                                      
REMARK 465     SER A   401                                                      
REMARK 465     GLY A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     ALA A   405                                                      
REMARK 465     GLN A   406                                                      
REMARK 465     ASN A   407                                                      
REMARK 465     ARG A   408                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     ARG C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     ILE C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     GLN C    46                                                      
REMARK 465     GLY C    47                                                      
REMARK 465     HIS C    48                                                      
REMARK 465     ALA C    63                                                      
REMARK 465     GLY C    84                                                      
REMARK 465     ALA C    96                                                      
REMARK 465     GLN C   125                                                      
REMARK 465     ARG C   181                                                      
REMARK 465     ARG C   182                                                      
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     ASP A 109    CG   OD1  OD2                                       
REMARK 470     GLN A 112    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 148    CD   OE1  OE2                                       
REMARK 470     ARG A 159    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 211    CE   NZ                                             
REMARK 470     ASP A 216    CG   OD1  OD2                                       
REMARK 470     ILE A 224    CG1  CG2  CD1                                       
REMARK 470     LYS A 255    CG   CD   CE   NZ                                   
REMARK 470     LYS A 272    CE   NZ                                             
REMARK 470     LYS A 275    CD   CE   NZ                                        
REMARK 470     GLU A 282    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 331    CD   CE   NZ                                        
REMARK 470     GLN A 353    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 367    CG   OD1  OD2                                       
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     LYS A 371    CG   CD   CE   NZ                                   
REMARK 470     LYS A 376    CG   CD   CE   NZ                                   
REMARK 470     TYR A 422    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     ARG C  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE C  42    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN C  44    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  45    CG   CD   OE1  OE2                                  
REMARK 470     THR C  62    CB   OG1  CG2                                       
REMARK 470     ASP C  85    CG   OD1  OD2                                       
REMARK 470     ARG C  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C  98    CB   CG   OD1  OD2                                  
REMARK 470     ARG C 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 121    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 122    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN C 147    CD   OE1  NE2                                       
REMARK 470     GLU C 156    CG   CD   OE1  OE2                                  
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    CYS C 168   CB    CYS C 168   SG     -0.097                       
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    ASP A 171       42.04    -79.07                                   
REMARK 500    LEU A 446       57.94   -142.53                                   
REMARK 500    ASN C  21       41.76     75.48                                   
REMARK 500    SER C  38      140.35   -171.39                                   
REMARK 500    VAL C  88     -167.27   -109.63                                   
REMARK 500    LEU C  89      -69.08    -96.72                                   
REMARK 500    ASP C  98     -159.64     68.66                                   
REMARK 500    TYR C 112      -23.29     72.39                                   
REMARK 500    SER C 114      -32.19   -147.20                                   
REMARK 500    ARG C 122      -73.99    -71.87                                   
REMARK 500    ALA C 123      108.98   -163.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY C   87     VAL C   88                  147.12                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 183                  
DBREF  2RD7 A  103   462  UNP    P07357   CO8A_HUMAN     133    492             
DBREF  2RD7 C    1   182  UNP    P07360   CO8G_HUMAN      21    202             
SEQADV 2RD7 HIS A   96  UNP  P07357              EXPRESSION TAG                 
SEQADV 2RD7 HIS A   97  UNP  P07357              EXPRESSION TAG                 
SEQADV 2RD7 HIS A   98  UNP  P07357              EXPRESSION TAG                 
SEQADV 2RD7 HIS A   99  UNP  P07357              EXPRESSION TAG                 
SEQADV 2RD7 HIS A  100  UNP  P07357              EXPRESSION TAG                 
SEQADV 2RD7 HIS A  101  UNP  P07357              EXPRESSION TAG                 
SEQADV 2RD7 MET A  102  UNP  P07357              EXPRESSION TAG                 
SEQADV 2RD7 MET C   -1  UNP  P07360              EXPRESSION TAG                 
SEQADV 2RD7 ALA C    0  UNP  P07360              EXPRESSION TAG                 
SEQRES   1 A  367  HIS HIS HIS HIS HIS HIS MET VAL ARG ALA ILE ASP GLU          
SEQRES   2 A  367  ASP CYS SER GLN TYR GLU PRO ILE PRO GLY SER GLN LYS          
SEQRES   3 A  367  ALA ALA LEU GLY TYR ASN ILE LEU THR GLN GLU ASP ALA          
SEQRES   4 A  367  GLN SER VAL TYR ASP ALA SER TYR TYR GLY GLY GLN CYS          
SEQRES   5 A  367  GLU THR VAL TYR ASN GLY GLU TRP ARG GLU LEU ARG TYR          
SEQRES   6 A  367  ASP SER THR CYS GLU ARG LEU TYR TYR GLY ASP ASP GLU          
SEQRES   7 A  367  LYS TYR PHE ARG LYS PRO TYR ASN PHE LEU LYS TYR HIS          
SEQRES   8 A  367  PHE GLU ALA LEU ALA ASP THR GLY ILE SER SER GLU PHE          
SEQRES   9 A  367  TYR ASP ASN ALA ASN ASP LEU LEU SER LYS VAL LYS LYS          
SEQRES  10 A  367  ASP LYS SER ASP SER PHE GLY VAL THR ILE GLY ILE GLY          
SEQRES  11 A  367  PRO ALA GLY SER PRO LEU LEU VAL GLY VAL GLY VAL SER          
SEQRES  12 A  367  HIS SER GLN ASP THR SER PHE LEU ASN GLU LEU ASN LYS          
SEQRES  13 A  367  TYR ASN GLU LYS LYS PHE ILE PHE THR ARG ILE PHE THR          
SEQRES  14 A  367  LYS VAL GLN THR ALA HIS PHE LYS MET ARG LYS ASP ASP          
SEQRES  15 A  367  ILE MET LEU ASP GLU GLY MET LEU GLN SER LEU MET GLU          
SEQRES  16 A  367  LEU PRO ASP GLN TYR ASN TYR GLY MET TYR ALA LYS PHE          
SEQRES  17 A  367  ILE ASN ASP TYR GLY THR HIS TYR ILE THR SER GLY SER          
SEQRES  18 A  367  MET GLY GLY ILE TYR GLU TYR ILE LEU VAL ILE ASP LYS          
SEQRES  19 A  367  ALA LYS MET GLU SER LEU GLY ILE THR SER ARG ASP ILE          
SEQRES  20 A  367  THR THR CYS PHE GLY GLY SER LEU GLY ILE GLN TYR GLU          
SEQRES  21 A  367  ASP LYS ILE ASN VAL GLY GLY GLY LEU SER GLY ASP HIS          
SEQRES  22 A  367  CYS LYS LYS PHE GLY GLY GLY LYS THR GLU ARG ALA ARG          
SEQRES  23 A  367  LYS ALA MET ALA VAL GLU ASP ILE ILE SER ARG VAL ARG          
SEQRES  24 A  367  GLY GLY SER SER GLY TRP SER GLY GLY LEU ALA GLN ASN          
SEQRES  25 A  367  ARG SER THR ILE THR TYR ARG SER TRP GLY ARG SER LEU          
SEQRES  26 A  367  LYS TYR ASN PRO VAL VAL ILE ASP PHE GLU MET GLN PRO          
SEQRES  27 A  367  ILE HIS GLU VAL LEU ARG HIS THR SER LEU GLY PRO LEU          
SEQRES  28 A  367  GLU ALA LYS ARG GLN ASN LEU ARG ARG ALA LEU ASP GLN          
SEQRES  29 A  367  TYR LEU MET                                                  
SEQRES   1 C  184  MET ALA GLN LYS PRO GLN ARG PRO ARG ARG PRO ALA SER          
SEQRES   2 C  184  PRO ILE SER THR ILE GLN PRO LYS ALA ASN PHE ASP ALA          
SEQRES   3 C  184  GLN GLN PHE ALA GLY THR TRP LEU LEU VAL ALA VAL GLY          
SEQRES   4 C  184  SER ALA CYS ARG PHE LEU GLN GLU GLN GLY HIS ARG ALA          
SEQRES   5 C  184  GLU ALA THR THR LEU HIS VAL ALA PRO GLN GLY THR ALA          
SEQRES   6 C  184  MET ALA VAL SER THR PHE ARG LYS LEU ASP GLY ILE CYS          
SEQRES   7 C  184  TRP GLN VAL ARG GLN LEU TYR GLY ASP THR GLY VAL LEU          
SEQRES   8 C  184  GLY ARG PHE LEU LEU GLN ALA ARG ASP ALA ARG GLY ALA          
SEQRES   9 C  184  VAL HIS VAL VAL VAL ALA GLU THR ASP TYR GLN SER PHE          
SEQRES  10 C  184  ALA VAL LEU TYR LEU GLU ARG ALA GLY GLN LEU SER VAL          
SEQRES  11 C  184  LYS LEU TYR ALA ARG SER LEU PRO VAL SER ASP SER VAL          
SEQRES  12 C  184  LEU SER GLY PHE GLU GLN ARG VAL GLN GLU ALA HIS LEU          
SEQRES  13 C  184  THR GLU ASP GLN ILE PHE TYR PHE PRO LYS TYR GLY PHE          
SEQRES  14 C  184  CYS GLU ALA ALA ASP GLN PHE HIS VAL LEU ASP GLU VAL          
SEQRES  15 C  184  ARG ARG                                                      
HET     CL  C 183       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *166(H2 O)                                                    
HELIX    1   1 GLY A  118  ALA A  123  1                                   6    
HELIX    2   2 ASN A  202  LYS A  214  1                                  13    
HELIX    3   3 ASP A  242  LYS A  251  1                                  10    
HELIX    4   4 ASP A  281  GLU A  290  1                                  10    
HELIX    5   5 ASN A  296  GLY A  308  1                                  13    
HELIX    6   6 LYS A  329  GLY A  336  1                                   8    
HELIX    7   7 THR A  338  LEU A  350  1                                  13    
HELIX    8   8 ASP A  367  GLY A  373  1                                   7    
HELIX    9   9 THR A  377  MET A  384  1                                   8    
HELIX   10  10 THR A  412  LEU A  420  1                                   9    
HELIX   11  11 HIS A  435  THR A  441  5                                   7    
HELIX   12  12 LEU A  446  MET A  462  1                                  17    
HELIX   13  13 CYS C   40  GLU C   45  1                                   6    
HELIX   14  14 SER C  138  ALA C  152  1                                  15    
HELIX   15  15 THR C  155  ASP C  157  5                                   3    
HELIX   16  16 ASP C  172  PHE C  174  5                                   3    
SHEET    1   A 6 GLU A 132  SER A 136  0                                        
SHEET    2   A 6 LEU A 124  ASN A 127 -1  N  ASN A 127   O  GLU A 132           
SHEET    3   A 6 HIS A 310  ASP A 328 -1  O  HIS A 310   N  TYR A 126           
SHEET    4   A 6 VAL A 425  PRO A 433 -1  O  ASP A 428   N  SER A 316           
SHEET    5   A 6 PRO A 230  VAL A 235 -1  N  LEU A 232   O  MET A 431           
SHEET    6   A 6 PHE A 218  ILE A 222 -1  N  THR A 221   O  LEU A 231           
SHEET    1   B 4 PHE A 182  PHE A 187  0                                        
SHEET    2   B 4 PHE A 257  MET A 273 -1  O  HIS A 270   N  HIS A 186           
SHEET    3   B 4 HIS A 310  ASP A 328 -1  O  ILE A 327   N  ILE A 258           
SHEET    4   B 4 VAL A 386  SER A 391 -1  O  ASP A 388   N  VAL A 326           
SHEET    1   C 4 SER A 196  TYR A 200  0                                        
SHEET    2   C 4 PHE A 257  MET A 273 -1  O  PHE A 263   N  SER A 196           
SHEET    3   C 4 HIS A 310  ASP A 328 -1  O  ILE A 327   N  ILE A 258           
SHEET    4   C 4 VAL A 386  SER A 391 -1  O  ASP A 388   N  VAL A 326           
SHEET    1   D 2 THR A 149  ASN A 152  0                                        
SHEET    2   D 2 LYS A 174  ARG A 177 -1  O  LYS A 174   N  ASN A 152           
SHEET    1   E 2 LEU A 158  ASP A 161  0                                        
SHEET    2   E 2 ARG A 166  TYR A 169 -1  O  ARG A 166   N  ASP A 161           
SHEET    1   F 6 ARG C  91  LEU C  94  0                                        
SHEET    2   F 6 VAL C 103  THR C 110 -1  O  VAL C 105   N  PHE C  92           
SHEET    3   F 6 PHE C 115  GLU C 121 -1  O  VAL C 117   N  GLU C 109           
SHEET    4   F 6 SER C 127  ALA C 132 -1  O  LYS C 129   N  LEU C 118           
SHEET    5   F 6 GLY C  29  SER C  38 -1  N  GLY C  37   O  VAL C 128           
SHEET    6   F 6 ILE C 159  TYR C 161 -1  O  PHE C 160   N  VAL C  36           
SHEET    1   G 9 ARG C  91  LEU C  94  0                                        
SHEET    2   G 9 VAL C 103  THR C 110 -1  O  VAL C 105   N  PHE C  92           
SHEET    3   G 9 PHE C 115  GLU C 121 -1  O  VAL C 117   N  GLU C 109           
SHEET    4   G 9 SER C 127  ALA C 132 -1  O  LYS C 129   N  LEU C 118           
SHEET    5   G 9 GLY C  29  SER C  38 -1  N  GLY C  37   O  VAL C 128           
SHEET    6   G 9 THR C  54  ALA C  58 -1  O  LEU C  55   N  TRP C  31           
SHEET    7   G 9 ALA C  65  LEU C  72 -1  O  ALA C  65   N  ALA C  58           
SHEET    8   G 9 ILE C  75  LEU C  82 -1  O  VAL C  79   N  THR C  68           
SHEET    9   G 9 VAL C 176  ASP C 178  1  O  LEU C 177   N  ARG C  80           
SSBOND   1 CYS A  110    CYS A  147                          1555   1555  2.03  
SSBOND   2 CYS A  164    CYS C   40                          1555   1555  2.07  
SSBOND   3 CYS A  345    CYS A  369                          1555   1555  2.74  
SSBOND   4 CYS C   76    CYS C  168                          1555   1555  2.11  
CISPEP   1 LEU C  135    PRO C  136          0         2.61                     
SITE     1 AC1  2 HIS A 310  GLY C 166                                          
CRYST1   96.553  126.087   51.887  90.00  90.00  90.00 P 21 21 2     4          
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      0.010357  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007931  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019273        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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