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Database: PDB
Entry: 5NAX
LinkDB: 5NAX
Original site: 5NAX 
HEADER    STRUCTURAL PROTEIN                      28-FEB-17   5NAX              
TITLE     CRYSTAL STRUCTURES OF HOMOOLIGOMERS OF THE NON-COLLAGENOUS DOMAINS OF 
TITLE    2 COLLAGEN TYPE IV. ALPHA121NC1                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLAGEN ALPHA-1(IV) CHAIN;                                
COMPND   3 CHAIN: A, B, D, F;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 1443-1667;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: COLLAGEN ALPHA-2(IV) CHAIN;                                
COMPND   8 CHAIN: C, E;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 1485-1712;                                    
COMPND  10 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: COL4A1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: COL4A2;                                                        
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: SF9                                     
KEYWDS    NON-COLLAGENOUS DOMAIN OF COLLAGEN TYPE IV, A PRINCIPAL STRUCTURAL    
KEYWDS   2 COMPONENT OF BASEMENT MEMBRANES, STRUCTURAL PROTEIN                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.CASINO,A.MARINA                                                     
REVDAT   3   28-NOV-18 5NAX    1       JRNL                                     
REVDAT   2   24-OCT-18 5NAX    1       JRNL                                     
REVDAT   1   12-SEP-18 5NAX    0                                                
JRNL        AUTH   P.CASINO,R.GOZALBO-ROVIRA,J.RODRIGUEZ-DIAZ,S.BANERJEE,       
JRNL        AUTH 2 A.BOUTAUD,V.RUBIO,B.G.HUDSON,J.SAUS,J.CERVERA,A.MARINA       
JRNL        TITL   STRUCTURES OF COLLAGEN IV GLOBULAR DOMAINS: INSIGHT INTO     
JRNL        TITL 2 ASSOCIATED PATHOLOGIES, FOLDING AND NETWORK ASSEMBLY.        
JRNL        REF    IUCRJ                         V.   5   765 2018              
JRNL        REFN                   ESSN 2052-2525                               
JRNL        PMID   30443360                                                     
JRNL        DOI    10.1107/S2052252518012459                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
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) : 2.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45615                          
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) : 0.143                           
REMARK   3   R VALUE            (WORKING SET) : 0.141                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2457                            
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) : 2.82                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3342                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10391                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 30.05000                                             
REMARK   3    B22 (A**2) : 30.05000                                             
REMARK   3    B33 (A**2) : -60.10000                                            
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): 0.151         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.054         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.148         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.152         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10724 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14606 ; 1.187 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1350 ; 4.957 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   449 ;33.462 ;22.940       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1632 ;13.936 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    63 ;14.069 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1535 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8289 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.521                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.479                                           
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 USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5NAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003805.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.25                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48121                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.36700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, PHASER                                        
REMARK 200 STARTING MODEL: 1T60                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG8000, MAGNESIUM ACETATE 0.2 M,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.07033            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      144.14067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      144.14067            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       72.07033            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 38600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -326.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     SER A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     THR A   229                                                      
REMARK 465     SER B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     SER C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     SER D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     THR D   229                                                      
REMARK 465     SER E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     ASN E   227                                                      
REMARK 465     LEU E   228                                                      
REMARK 465     SER F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     ASP F     3                                                      
REMARK 465     HIS F     4                                                      
REMARK 465     ARG F   228                                                      
REMARK 465     THR F   229                                                      
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   3    CG   OD1  OD2                                       
REMARK 470     GLU A 197    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 228    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 228    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 229    OG1  CG2                                            
REMARK 470     ARG D 228    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E   4    CG1  CG2  CD1                                       
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    LEU A  27      -61.48   -100.25                                   
REMARK 500    ARG A  76     -153.05   -118.86                                   
REMARK 500    ASN A  77       78.01   -110.88                                   
REMARK 500    MET A  93        5.18     58.39                                   
REMARK 500    VAL A 144      -61.41    -92.57                                   
REMARK 500    SER A 148      -86.60   -116.63                                   
REMARK 500    ALA A 151        6.88     59.01                                   
REMARK 500    LEU B  27      -60.48    -97.05                                   
REMARK 500    GLU B  40       -7.90     70.82                                   
REMARK 500    ARG B  76     -151.38   -118.48                                   
REMARK 500    SER B 148      -86.75   -124.51                                   
REMARK 500    ALA B 151        7.14     52.24                                   
REMARK 500    GLU B 200       39.81    -97.70                                   
REMARK 500    LEU C  34      -64.22    -90.74                                   
REMARK 500    PRO C  67        2.86    -62.80                                   
REMARK 500    ARG C  76     -153.27   -112.14                                   
REMARK 500    ASN C  77       40.72   -109.96                                   
REMARK 500    ALA C  95     -148.78   -115.76                                   
REMARK 500    GLU C  98        1.74    -68.95                                   
REMARK 500    LEU C 142      -64.26    -98.37                                   
REMARK 500    ALA C 146      -80.52   -127.38                                   
REMARK 500    LEU D  27      -63.07   -101.40                                   
REMARK 500    LEU D  34      -66.55    -92.61                                   
REMARK 500    ARG D  76     -151.24   -122.98                                   
REMARK 500    SER D 148      -87.00   -119.26                                   
REMARK 500    ALA D 151       15.55     55.06                                   
REMARK 500    ALA E  95     -155.10    -95.74                                   
REMARK 500    LEU E 142      -67.31    -92.54                                   
REMARK 500    ALA E 146      -83.53   -122.64                                   
REMARK 500    LEU F  27      -62.45   -103.80                                   
REMARK 500    LEU F  34      -64.51    -90.48                                   
REMARK 500    ASN F  66     -169.78   -109.92                                   
REMARK 500    ARG F  76     -161.38   -109.34                                   
REMARK 500    ASN F  77       66.71   -105.84                                   
REMARK 500    SER F 148      -85.19   -116.67                                   
REMARK 500    ALA F 151       24.76     49.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 419        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH D 420        DISTANCE =  7.94 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 302                  
DBREF  5NAX A    1   229  UNP    P02462   CO4A1_HUMAN   1441   1669             
DBREF  5NAX B    1   229  UNP    P02462   CO4A1_HUMAN   1441   1669             
DBREF  5NAX C    1   228  UNP    P08572   CO4A2_HUMAN   1485   1712             
DBREF  5NAX D    1   229  UNP    P02462   CO4A1_HUMAN   1441   1669             
DBREF  5NAX E    1   228  UNP    P08572   CO4A2_HUMAN   1485   1712             
DBREF  5NAX F    1   229  UNP    P02462   CO4A1_HUMAN   1441   1669             
SEQRES   1 A  229  SER VAL ASP HIS GLY PHE LEU VAL THR ARG HIS SER GLN          
SEQRES   2 A  229  THR ILE ASP ASP PRO GLN CYS PRO SER GLY THR LYS ILE          
SEQRES   3 A  229  LEU TYR HIS GLY TYR SER LEU LEU TYR VAL GLN GLY ASN          
SEQRES   4 A  229  GLU ARG ALA HIS GLY GLN ASP LEU GLY THR ALA GLY SER          
SEQRES   5 A  229  CYS LEU ARG LYS PHE SER THR MET PRO PHE LEU PHE CYS          
SEQRES   6 A  229  ASN ILE ASN ASN VAL CYS ASN PHE ALA SER ARG ASN ASP          
SEQRES   7 A  229  TYR SER TYR TRP LEU SER THR PRO GLU PRO MET PRO MET          
SEQRES   8 A  229  SER MET ALA PRO ILE THR GLY GLU ASN ILE ARG PRO PHE          
SEQRES   9 A  229  ILE SER ARG CYS ALA VAL CYS GLU ALA PRO ALA MET VAL          
SEQRES  10 A  229  MET ALA VAL HIS SER GLN THR ILE GLN ILE PRO PRO CYS          
SEQRES  11 A  229  PRO SER GLY TRP SER SER LEU TRP ILE GLY TYR SER PHE          
SEQRES  12 A  229  VAL MET HIS THR SER ALA GLY ALA GLU GLY SER GLY GLN          
SEQRES  13 A  229  ALA LEU ALA SER PRO GLY SER CYS LEU GLU GLU PHE ARG          
SEQRES  14 A  229  SER ALA PRO PHE ILE GLU CYS HIS GLY ARG GLY THR CYS          
SEQRES  15 A  229  ASN TYR TYR ALA ASN ALA TYR SER PHE TRP LEU ALA THR          
SEQRES  16 A  229  ILE GLU ARG SER GLU MET PHE LYS LYS PRO THR PRO SER          
SEQRES  17 A  229  THR LEU LYS ALA GLY GLU LEU ARG THR HIS VAL SER ARG          
SEQRES  18 A  229  CYS GLN VAL CYS MET ARG ARG THR                              
SEQRES   1 B  229  SER VAL ASP HIS GLY PHE LEU VAL THR ARG HIS SER GLN          
SEQRES   2 B  229  THR ILE ASP ASP PRO GLN CYS PRO SER GLY THR LYS ILE          
SEQRES   3 B  229  LEU TYR HIS GLY TYR SER LEU LEU TYR VAL GLN GLY ASN          
SEQRES   4 B  229  GLU ARG ALA HIS GLY GLN ASP LEU GLY THR ALA GLY SER          
SEQRES   5 B  229  CYS LEU ARG LYS PHE SER THR MET PRO PHE LEU PHE CYS          
SEQRES   6 B  229  ASN ILE ASN ASN VAL CYS ASN PHE ALA SER ARG ASN ASP          
SEQRES   7 B  229  TYR SER TYR TRP LEU SER THR PRO GLU PRO MET PRO MET          
SEQRES   8 B  229  SER MET ALA PRO ILE THR GLY GLU ASN ILE ARG PRO PHE          
SEQRES   9 B  229  ILE SER ARG CYS ALA VAL CYS GLU ALA PRO ALA MET VAL          
SEQRES  10 B  229  MET ALA VAL HIS SER GLN THR ILE GLN ILE PRO PRO CYS          
SEQRES  11 B  229  PRO SER GLY TRP SER SER LEU TRP ILE GLY TYR SER PHE          
SEQRES  12 B  229  VAL MET HIS THR SER ALA GLY ALA GLU GLY SER GLY GLN          
SEQRES  13 B  229  ALA LEU ALA SER PRO GLY SER CYS LEU GLU GLU PHE ARG          
SEQRES  14 B  229  SER ALA PRO PHE ILE GLU CYS HIS GLY ARG GLY THR CYS          
SEQRES  15 B  229  ASN TYR TYR ALA ASN ALA TYR SER PHE TRP LEU ALA THR          
SEQRES  16 B  229  ILE GLU ARG SER GLU MET PHE LYS LYS PRO THR PRO SER          
SEQRES  17 B  229  THR LEU LYS ALA GLY GLU LEU ARG THR HIS VAL SER ARG          
SEQRES  18 B  229  CYS GLN VAL CYS MET ARG ARG THR                              
SEQRES   1 C  228  SER VAL SER ILE GLY TYR LEU LEU VAL LYS HIS SER GLN          
SEQRES   2 C  228  THR ASP GLN GLU PRO MET CYS PRO VAL GLY MET ASN LYS          
SEQRES   3 C  228  LEU TRP SER GLY TYR SER LEU LEU TYR PHE GLU GLY GLN          
SEQRES   4 C  228  GLU LYS ALA HIS ASN GLN ASP LEU GLY LEU ALA GLY SER          
SEQRES   5 C  228  CYS LEU ALA ARG PHE SER THR MET PRO PHE LEU TYR CYS          
SEQRES   6 C  228  ASN PRO GLY ASP VAL CYS TYR TYR ALA SER ARG ASN ASP          
SEQRES   7 C  228  LYS SER TYR TRP LEU SER THR THR ALA PRO LEU PRO MET          
SEQRES   8 C  228  MET PRO VAL ALA GLU ASP GLU ILE LYS PRO TYR ILE SER          
SEQRES   9 C  228  ARG CYS SER VAL CYS GLU ALA PRO ALA ILE ALA ILE ALA          
SEQRES  10 C  228  VAL HIS SER GLN ASP VAL SER ILE PRO HIS CYS PRO ALA          
SEQRES  11 C  228  GLY TRP ARG SER LEU TRP ILE GLY TYR SER PHE LEU MET          
SEQRES  12 C  228  HIS THR ALA ALA GLY ASP GLU GLY GLY GLY GLN SER LEU          
SEQRES  13 C  228  VAL SER PRO GLY SER CYS LEU GLU ASP PHE ARG ALA THR          
SEQRES  14 C  228  PRO PHE ILE GLU CYS ASN GLY GLY ARG GLY THR CYS HIS          
SEQRES  15 C  228  TYR TYR ALA ASN LYS TYR SER PHE TRP LEU THR THR ILE          
SEQRES  16 C  228  PRO GLU GLN SER PHE GLN GLY SER PRO SER ALA ASP THR          
SEQRES  17 C  228  LEU LYS ALA GLY LEU ILE ARG THR HIS ILE SER ARG CYS          
SEQRES  18 C  228  GLN VAL CYS MET LYS ASN LEU                                  
SEQRES   1 D  229  SER VAL ASP HIS GLY PHE LEU VAL THR ARG HIS SER GLN          
SEQRES   2 D  229  THR ILE ASP ASP PRO GLN CYS PRO SER GLY THR LYS ILE          
SEQRES   3 D  229  LEU TYR HIS GLY TYR SER LEU LEU TYR VAL GLN GLY ASN          
SEQRES   4 D  229  GLU ARG ALA HIS GLY GLN ASP LEU GLY THR ALA GLY SER          
SEQRES   5 D  229  CYS LEU ARG LYS PHE SER THR MET PRO PHE LEU PHE CYS          
SEQRES   6 D  229  ASN ILE ASN ASN VAL CYS ASN PHE ALA SER ARG ASN ASP          
SEQRES   7 D  229  TYR SER TYR TRP LEU SER THR PRO GLU PRO MET PRO MET          
SEQRES   8 D  229  SER MET ALA PRO ILE THR GLY GLU ASN ILE ARG PRO PHE          
SEQRES   9 D  229  ILE SER ARG CYS ALA VAL CYS GLU ALA PRO ALA MET VAL          
SEQRES  10 D  229  MET ALA VAL HIS SER GLN THR ILE GLN ILE PRO PRO CYS          
SEQRES  11 D  229  PRO SER GLY TRP SER SER LEU TRP ILE GLY TYR SER PHE          
SEQRES  12 D  229  VAL MET HIS THR SER ALA GLY ALA GLU GLY SER GLY GLN          
SEQRES  13 D  229  ALA LEU ALA SER PRO GLY SER CYS LEU GLU GLU PHE ARG          
SEQRES  14 D  229  SER ALA PRO PHE ILE GLU CYS HIS GLY ARG GLY THR CYS          
SEQRES  15 D  229  ASN TYR TYR ALA ASN ALA TYR SER PHE TRP LEU ALA THR          
SEQRES  16 D  229  ILE GLU ARG SER GLU MET PHE LYS LYS PRO THR PRO SER          
SEQRES  17 D  229  THR LEU LYS ALA GLY GLU LEU ARG THR HIS VAL SER ARG          
SEQRES  18 D  229  CYS GLN VAL CYS MET ARG ARG THR                              
SEQRES   1 E  228  SER VAL SER ILE GLY TYR LEU LEU VAL LYS HIS SER GLN          
SEQRES   2 E  228  THR ASP GLN GLU PRO MET CYS PRO VAL GLY MET ASN LYS          
SEQRES   3 E  228  LEU TRP SER GLY TYR SER LEU LEU TYR PHE GLU GLY GLN          
SEQRES   4 E  228  GLU LYS ALA HIS ASN GLN ASP LEU GLY LEU ALA GLY SER          
SEQRES   5 E  228  CYS LEU ALA ARG PHE SER THR MET PRO PHE LEU TYR CYS          
SEQRES   6 E  228  ASN PRO GLY ASP VAL CYS TYR TYR ALA SER ARG ASN ASP          
SEQRES   7 E  228  LYS SER TYR TRP LEU SER THR THR ALA PRO LEU PRO MET          
SEQRES   8 E  228  MET PRO VAL ALA GLU ASP GLU ILE LYS PRO TYR ILE SER          
SEQRES   9 E  228  ARG CYS SER VAL CYS GLU ALA PRO ALA ILE ALA ILE ALA          
SEQRES  10 E  228  VAL HIS SER GLN ASP VAL SER ILE PRO HIS CYS PRO ALA          
SEQRES  11 E  228  GLY TRP ARG SER LEU TRP ILE GLY TYR SER PHE LEU MET          
SEQRES  12 E  228  HIS THR ALA ALA GLY ASP GLU GLY GLY GLY GLN SER LEU          
SEQRES  13 E  228  VAL SER PRO GLY SER CYS LEU GLU ASP PHE ARG ALA THR          
SEQRES  14 E  228  PRO PHE ILE GLU CYS ASN GLY GLY ARG GLY THR CYS HIS          
SEQRES  15 E  228  TYR TYR ALA ASN LYS TYR SER PHE TRP LEU THR THR ILE          
SEQRES  16 E  228  PRO GLU GLN SER PHE GLN GLY SER PRO SER ALA ASP THR          
SEQRES  17 E  228  LEU LYS ALA GLY LEU ILE ARG THR HIS ILE SER ARG CYS          
SEQRES  18 E  228  GLN VAL CYS MET LYS ASN LEU                                  
SEQRES   1 F  229  SER VAL ASP HIS GLY PHE LEU VAL THR ARG HIS SER GLN          
SEQRES   2 F  229  THR ILE ASP ASP PRO GLN CYS PRO SER GLY THR LYS ILE          
SEQRES   3 F  229  LEU TYR HIS GLY TYR SER LEU LEU TYR VAL GLN GLY ASN          
SEQRES   4 F  229  GLU ARG ALA HIS GLY GLN ASP LEU GLY THR ALA GLY SER          
SEQRES   5 F  229  CYS LEU ARG LYS PHE SER THR MET PRO PHE LEU PHE CYS          
SEQRES   6 F  229  ASN ILE ASN ASN VAL CYS ASN PHE ALA SER ARG ASN ASP          
SEQRES   7 F  229  TYR SER TYR TRP LEU SER THR PRO GLU PRO MET PRO MET          
SEQRES   8 F  229  SER MET ALA PRO ILE THR GLY GLU ASN ILE ARG PRO PHE          
SEQRES   9 F  229  ILE SER ARG CYS ALA VAL CYS GLU ALA PRO ALA MET VAL          
SEQRES  10 F  229  MET ALA VAL HIS SER GLN THR ILE GLN ILE PRO PRO CYS          
SEQRES  11 F  229  PRO SER GLY TRP SER SER LEU TRP ILE GLY TYR SER PHE          
SEQRES  12 F  229  VAL MET HIS THR SER ALA GLY ALA GLU GLY SER GLY GLN          
SEQRES  13 F  229  ALA LEU ALA SER PRO GLY SER CYS LEU GLU GLU PHE ARG          
SEQRES  14 F  229  SER ALA PRO PHE ILE GLU CYS HIS GLY ARG GLY THR CYS          
SEQRES  15 F  229  ASN TYR TYR ALA ASN ALA TYR SER PHE TRP LEU ALA THR          
SEQRES  16 F  229  ILE GLU ARG SER GLU MET PHE LYS LYS PRO THR PRO SER          
SEQRES  17 F  229  THR LEU LYS ALA GLY GLU LEU ARG THR HIS VAL SER ARG          
SEQRES  18 F  229  CYS GLN VAL CYS MET ARG ARG THR                              
HET     CL  A 301       1                                                       
HET     CL  A 302       1                                                       
HET     CL  B 301       1                                                       
HET     CL  B 302       1                                                       
HET     CL  C 301       1                                                       
HET     CL  C 302       1                                                       
HET     CL  D 301       1                                                       
HET     CL  D 302       1                                                       
HET     CL  E 301       1                                                       
HET     CL  F 301       1                                                       
HET     CL  F 302       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   7   CL    11(CL 1-)                                                    
FORMUL  18  HOH   *141(H2 O)                                                    
HELIX    1 AA1 THR A   49  GLY A   51  5                                   3    
HELIX    2 AA2 GLU A   99  ILE A  105  5                                   7    
HELIX    3 AA3 SER A  148  GLU A  152  5                                   5    
HELIX    4 AA4 SER A  160  GLY A  162  5                                   3    
HELIX    5 AA5 GLU A  214  HIS A  218  5                                   5    
HELIX    6 AA6 THR B   49  GLY B   51  5                                   3    
HELIX    7 AA7 GLU B   99  ILE B  105  5                                   7    
HELIX    8 AA8 ALA B  149  ALA B  151  5                                   3    
HELIX    9 AA9 SER B  160  GLY B  162  5                                   3    
HELIX   10 AB1 GLU B  214  HIS B  218  5                                   5    
HELIX   11 AB2 LEU C   49  GLY C   51  5                                   3    
HELIX   12 AB3 ILE C   99  ILE C  103  5                                   5    
HELIX   13 AB4 SER C  158  GLY C  160  5                                   3    
HELIX   14 AB5 ILE C  214  ILE C  218  5                                   5    
HELIX   15 AB6 THR D   49  GLY D   51  5                                   3    
HELIX   16 AB7 GLU D   99  ILE D  105  5                                   7    
HELIX   17 AB8 SER D  160  GLY D  162  5                                   3    
HELIX   18 AB9 GLU D  214  VAL D  219  5                                   6    
HELIX   19 AC1 LEU E   49  GLY E   51  5                                   3    
HELIX   20 AC2 ILE E   99  ILE E  103  5                                   5    
HELIX   21 AC3 SER E  158  GLY E  160  5                                   3    
HELIX   22 AC4 THR F   49  GLY F   51  5                                   3    
HELIX   23 AC5 GLU F   99  ILE F  105  5                                   7    
HELIX   24 AC6 SER F  148  GLU F  152  5                                   5    
HELIX   25 AC7 SER F  160  GLY F  162  5                                   3    
HELIX   26 AC8 GLU F  197  MET F  201  5                                   5    
HELIX   27 AC9 GLU F  214  VAL F  219  5                                   6    
SHEET    1 AA1 4 PHE A   6  HIS A  11  0                                        
SHEET    2 AA1 4 ARG A 107  ALA A 113 -1  O  CYS A 111   N  VAL A   8           
SHEET    3 AA1 4 LYS A  25  GLY A  38 -1  N  LYS A  25   O  GLU A 112           
SHEET    4 AA1 4 CYS A  53  LEU A  54 -1  O  LEU A  54   N  TYR A  31           
SHEET    1 AA2 6 ARG A  41  GLY A  44  0                                        
SHEET    2 AA2 6 LYS A  25  GLY A  38 -1  N  VAL A  36   O  HIS A  43           
SHEET    3 AA2 6 TYR A  79  LEU A  83 -1  O  TYR A  79   N  GLN A  37           
SHEET    4 AA2 6 PHE A 173  HIS A 177 -1  O  CYS A 176   N  SER A  80           
SHEET    5 AA2 6 THR A 181  ASN A 183 -1  O  ASN A 183   N  GLU A 175           
SHEET    6 AA2 6 ILE A  96  THR A  97 -1  N  ILE A  96   O  CYS A 182           
SHEET    1 AA3 4 VAL B 117  HIS B 121  0                                        
SHEET    2 AA3 4 ARG B 221  ARG B 227 -1  O  CYS B 225   N  MET B 118           
SHEET    3 AA3 4 TRP B 134  THR B 147 -1  N  SER B 135   O  MET B 226           
SHEET    4 AA3 4 CYS B 164  LEU B 165 -1  O  LEU B 165   N  TYR B 141           
SHEET    1 AA4 6 GLY B 153  GLY B 155  0                                        
SHEET    2 AA4 6 TRP B 134  THR B 147 -1  N  HIS B 146   O  SER B 154           
SHEET    3 AA4 6 TYR B 189  LEU B 193 -1  O  PHE B 191   N  MET B 145           
SHEET    4 AA4 6 PHE A  62  CYS A  65 -1  N  LEU A  63   O  TRP B 192           
SHEET    5 AA4 6 CYS A  71  PHE A  73 -1  O  ASN A  72   N  PHE A  64           
SHEET    6 AA4 6 SER B 208  LEU B 210 -1  O  SER B 208   N  PHE A  73           
SHEET    1 AA5 4 VAL A 117  HIS A 121  0                                        
SHEET    2 AA5 4 ARG A 221  ARG A 227 -1  O  CYS A 225   N  MET A 118           
SHEET    3 AA5 4 TRP A 134  THR A 147 -1  N  SER A 135   O  MET A 226           
SHEET    4 AA5 4 CYS A 164  LEU A 165 -1  O  LEU A 165   N  TYR A 141           
SHEET    1 AA6 7 VAL A 117  HIS A 121  0                                        
SHEET    2 AA6 7 ARG A 221  ARG A 227 -1  O  CYS A 225   N  MET A 118           
SHEET    3 AA6 7 TRP A 134  THR A 147 -1  N  SER A 135   O  MET A 226           
SHEET    4 AA6 7 TYR A 189  LEU A 193 -1  O  PHE A 191   N  MET A 145           
SHEET    5 AA6 7 PHE C  62  ASN C  66 -1  O  LEU C  63   N  TRP A 192           
SHEET    6 AA6 7 VAL C  70  TYR C  73 -1  O  TYR C  72   N  TYR C  64           
SHEET    7 AA6 7 SER A 208  LEU A 210 -1  N  LEU A 210   O  CYS C  71           
SHEET    1 AA7 4 PHE B   6  HIS B  11  0                                        
SHEET    2 AA7 4 ARG B 107  ALA B 113 -1  O  CYS B 111   N  VAL B   8           
SHEET    3 AA7 4 LYS B  25  GLY B  38 -1  N  LYS B  25   O  GLU B 112           
SHEET    4 AA7 4 CYS B  53  LEU B  54 -1  O  LEU B  54   N  TYR B  31           
SHEET    1 AA8 6 ARG B  41  GLY B  44  0                                        
SHEET    2 AA8 6 LYS B  25  GLY B  38 -1  N  VAL B  36   O  HIS B  43           
SHEET    3 AA8 6 TYR B  79  LEU B  83 -1  O  TYR B  81   N  TYR B  35           
SHEET    4 AA8 6 PHE B 173  HIS B 177 -1  O  CYS B 176   N  SER B  80           
SHEET    5 AA8 6 THR B 181  ASN B 183 -1  O  THR B 181   N  HIS B 177           
SHEET    6 AA8 6 ILE B  96  THR B  97 -1  N  ILE B  96   O  CYS B 182           
SHEET    1 AA9 4 ALA C 115  HIS C 119  0                                        
SHEET    2 AA9 4 ARG C 220  LYS C 226 -1  O  CYS C 224   N  ILE C 116           
SHEET    3 AA9 4 TRP C 132  THR C 145 -1  N  ARG C 133   O  MET C 225           
SHEET    4 AA9 4 CYS C 162  LEU C 163 -1  O  LEU C 163   N  TYR C 139           
SHEET    1 AB1 6 GLY C 151  GLY C 153  0                                        
SHEET    2 AB1 6 TRP C 132  THR C 145 -1  N  HIS C 144   O  GLY C 152           
SHEET    3 AB1 6 TYR C 188  LEU C 192 -1  O  PHE C 190   N  MET C 143           
SHEET    4 AB1 6 PHE B  62  CYS B  65 -1  N  LEU B  63   O  TRP C 191           
SHEET    5 AB1 6 CYS B  71  PHE B  73 -1  O  ASN B  72   N  PHE B  64           
SHEET    6 AB1 6 ASP C 207  LEU C 209 -1  O  ASP C 207   N  PHE B  73           
SHEET    1 AB2 4 LEU C   7  HIS C  11  0                                        
SHEET    2 AB2 4 ARG C 105  GLU C 110 -1  O  CYS C 109   N  LEU C   8           
SHEET    3 AB2 4 LYS C  26  GLY C  38 -1  N  LEU C  27   O  VAL C 108           
SHEET    4 AB2 4 CYS C  53  LEU C  54 -1  O  LEU C  54   N  TYR C  31           
SHEET    1 AB3 5 LYS C  41  ASN C  44  0                                        
SHEET    2 AB3 5 LYS C  26  GLY C  38 -1  N  PHE C  36   O  HIS C  43           
SHEET    3 AB3 5 LYS C  79  LEU C  83 -1  O  LEU C  83   N  SER C  32           
SHEET    4 AB3 5 PHE C 171  ASN C 175 -1  O  CYS C 174   N  SER C  80           
SHEET    5 AB3 5 THR C 180  HIS C 182 -1  O  THR C 180   N  ASN C 175           
SHEET    1 AB4 4 PHE D   6  HIS D  11  0                                        
SHEET    2 AB4 4 ARG D 107  ALA D 113 -1  O  ALA D 113   N  PHE D   6           
SHEET    3 AB4 4 LYS D  25  GLY D  38 -1  N  LYS D  25   O  GLU D 112           
SHEET    4 AB4 4 CYS D  53  LEU D  54 -1  O  LEU D  54   N  TYR D  31           
SHEET    1 AB5 6 ARG D  41  GLY D  44  0                                        
SHEET    2 AB5 6 LYS D  25  GLY D  38 -1  N  VAL D  36   O  HIS D  43           
SHEET    3 AB5 6 TYR D  79  LEU D  83 -1  O  TYR D  81   N  TYR D  35           
SHEET    4 AB5 6 PHE D 173  HIS D 177 -1  O  CYS D 176   N  SER D  80           
SHEET    5 AB5 6 THR D 181  ASN D 183 -1  O  ASN D 183   N  GLU D 175           
SHEET    6 AB5 6 ILE D  96  THR D  97 -1  N  ILE D  96   O  CYS D 182           
SHEET    1 AB6 4 VAL F 117  HIS F 121  0                                        
SHEET    2 AB6 4 ARG F 221  MET F 226 -1  O  CYS F 225   N  MET F 118           
SHEET    3 AB6 4 SER F 135  THR F 147 -1  N  LEU F 137   O  VAL F 224           
SHEET    4 AB6 4 CYS F 164  LEU F 165 -1  O  LEU F 165   N  TYR F 141           
SHEET    1 AB7 7 VAL F 117  HIS F 121  0                                        
SHEET    2 AB7 7 ARG F 221  MET F 226 -1  O  CYS F 225   N  MET F 118           
SHEET    3 AB7 7 SER F 135  THR F 147 -1  N  LEU F 137   O  VAL F 224           
SHEET    4 AB7 7 TYR F 189  LEU F 193 -1  O  PHE F 191   N  MET F 145           
SHEET    5 AB7 7 PHE D  62  CYS D  65 -1  N  LEU D  63   O  TRP F 192           
SHEET    6 AB7 7 CYS D  71  PHE D  73 -1  O  ASN D  72   N  PHE D  64           
SHEET    7 AB7 7 SER F 208  LEU F 210 -1  O  LEU F 210   N  CYS D  71           
SHEET    1 AB8 4 VAL D 117  HIS D 121  0                                        
SHEET    2 AB8 4 ARG D 221  ARG D 227 -1  O  CYS D 225   N  MET D 118           
SHEET    3 AB8 4 TRP D 134  THR D 147 -1  N  SER D 135   O  MET D 226           
SHEET    4 AB8 4 CYS D 164  LEU D 165 -1  O  LEU D 165   N  TYR D 141           
SHEET    1 AB9 6 GLY D 153  GLY D 155  0                                        
SHEET    2 AB9 6 TRP D 134  THR D 147 -1  N  HIS D 146   O  SER D 154           
SHEET    3 AB9 6 TYR D 189  LEU D 193 -1  O  TYR D 189   N  THR D 147           
SHEET    4 AB9 6 PHE E  62  ASN E  66 -1  O  LEU E  63   N  TRP D 192           
SHEET    5 AB9 6 VAL E  70  TYR E  73 -1  O  TYR E  72   N  TYR E  64           
SHEET    6 AB9 6 SER D 208  LEU D 210 -1  N  SER D 208   O  TYR E  73           
SHEET    1 AC1 4 TYR E   6  HIS E  11  0                                        
SHEET    2 AC1 4 ARG E 105  ALA E 111 -1  O  ALA E 111   N  TYR E   6           
SHEET    3 AC1 4 LYS E  26  GLY E  38 -1  N  LEU E  27   O  VAL E 108           
SHEET    4 AC1 4 CYS E  53  LEU E  54 -1  O  LEU E  54   N  TYR E  31           
SHEET    1 AC2 5 LYS E  41  ASN E  44  0                                        
SHEET    2 AC2 5 LYS E  26  GLY E  38 -1  N  PHE E  36   O  HIS E  43           
SHEET    3 AC2 5 LYS E  79  LEU E  83 -1  O  LYS E  79   N  GLU E  37           
SHEET    4 AC2 5 PHE E 171  ASN E 175 -1  O  ILE E 172   N  TRP E  82           
SHEET    5 AC2 5 THR E 180  HIS E 182 -1  O  THR E 180   N  ASN E 175           
SHEET    1 AC3 4 ALA E 115  HIS E 119  0                                        
SHEET    2 AC3 4 ARG E 220  MET E 225 -1  O  CYS E 224   N  ILE E 116           
SHEET    3 AC3 4 ARG E 133  THR E 145 -1  N  LEU E 135   O  VAL E 223           
SHEET    4 AC3 4 CYS E 162  LEU E 163 -1  O  LEU E 163   N  TYR E 139           
SHEET    1 AC4 6 GLY E 151  GLY E 153  0                                        
SHEET    2 AC4 6 ARG E 133  THR E 145 -1  N  HIS E 144   O  GLY E 152           
SHEET    3 AC4 6 TYR E 188  LEU E 192 -1  O  TYR E 188   N  THR E 145           
SHEET    4 AC4 6 PHE F  62  CYS F  65 -1  O  LEU F  63   N  TRP E 191           
SHEET    5 AC4 6 CYS F  71  PHE F  73 -1  O  ASN F  72   N  PHE F  64           
SHEET    6 AC4 6 ASP E 207  LEU E 209 -1  N  LEU E 209   O  CYS F  71           
SHEET    1 AC5 4 PHE F   6  HIS F  11  0                                        
SHEET    2 AC5 4 ARG F 107  ALA F 113 -1  O  CYS F 111   N  VAL F   8           
SHEET    3 AC5 4 LYS F  25  GLY F  38 -1  N  GLY F  30   O  CYS F 108           
SHEET    4 AC5 4 CYS F  53  LEU F  54 -1  O  LEU F  54   N  TYR F  31           
SHEET    1 AC6 6 ARG F  41  GLY F  44  0                                        
SHEET    2 AC6 6 LYS F  25  GLY F  38 -1  N  VAL F  36   O  HIS F  43           
SHEET    3 AC6 6 TYR F  79  LEU F  83 -1  O  TYR F  79   N  GLN F  37           
SHEET    4 AC6 6 PHE F 173  HIS F 177 -1  O  CYS F 176   N  SER F  80           
SHEET    5 AC6 6 THR F 181  ASN F 183 -1  O  THR F 181   N  HIS F 177           
SHEET    6 AC6 6 ILE F  96  THR F  97 -1  N  ILE F  96   O  CYS F 182           
SSBOND   1 CYS A   20    CYS A  111                          1555   1555  2.05  
SSBOND   2 CYS A   53    CYS A  108                          1555   1555  2.04  
SSBOND   3 CYS A   65    CYS A   71                          1555   1555  2.04  
SSBOND   4 CYS A  130    CYS A  225                          1555   1555  2.06  
SSBOND   5 CYS A  164    CYS A  222                          1555   1555  2.04  
SSBOND   6 CYS A  176    CYS A  182                          1555   1555  2.03  
SSBOND   7 CYS B   20    CYS B  111                          1555   1555  2.05  
SSBOND   8 CYS B   53    CYS B  108                          1555   1555  2.05  
SSBOND   9 CYS B   65    CYS B   71                          1555   1555  2.06  
SSBOND  10 CYS B  130    CYS B  225                          1555   1555  2.06  
SSBOND  11 CYS B  164    CYS B  222                          1555   1555  2.04  
SSBOND  12 CYS B  176    CYS B  182                          1555   1555  2.05  
SSBOND  13 CYS C   20    CYS C  109                          1555   1555  2.04  
SSBOND  14 CYS C   53    CYS C  106                          1555   1555  2.05  
SSBOND  15 CYS C   65    CYS C   71                          1555   1555  2.04  
SSBOND  16 CYS C  128    CYS C  224                          1555   1555  2.05  
SSBOND  17 CYS C  162    CYS C  221                          1555   1555  2.06  
SSBOND  18 CYS C  174    CYS C  181                          1555   1555  2.03  
SSBOND  19 CYS D   20    CYS D  111                          1555   1555  2.05  
SSBOND  20 CYS D   53    CYS D  108                          1555   1555  2.04  
SSBOND  21 CYS D   65    CYS D   71                          1555   1555  2.03  
SSBOND  22 CYS D  130    CYS D  225                          1555   1555  2.05  
SSBOND  23 CYS D  164    CYS D  222                          1555   1555  2.02  
SSBOND  24 CYS D  176    CYS D  182                          1555   1555  2.04  
SSBOND  25 CYS E   20    CYS E  109                          1555   1555  2.04  
SSBOND  26 CYS E   53    CYS E  106                          1555   1555  2.05  
SSBOND  27 CYS E   65    CYS E   71                          1555   1555  2.06  
SSBOND  28 CYS E  128    CYS E  224                          1555   1555  2.05  
SSBOND  29 CYS E  162    CYS E  221                          1555   1555  2.04  
SSBOND  30 CYS E  174    CYS E  181                          1555   1555  2.04  
SSBOND  31 CYS F   20    CYS F  111                          1555   1555  2.04  
SSBOND  32 CYS F   53    CYS F  108                          1555   1555  2.03  
SSBOND  33 CYS F   65    CYS F   71                          1555   1555  2.06  
SSBOND  34 CYS F  130    CYS F  225                          1555   1555  2.06  
SSBOND  35 CYS F  164    CYS F  222                          1555   1555  2.05  
SSBOND  36 CYS F  176    CYS F  182                          1555   1555  2.05  
SITE     1 AC1  4 ALA A  74  ARG A  76  ASP A  78  GLY A 178                    
SITE     1 AC2  3 ASN A  66  TYR B 189  ALA D 186                               
SITE     1 AC3  3 ALA B  74  ARG B  76  ASP B  78                               
SITE     1 AC4  3 ASN B  66  TYR C 188  ALA E 185                               
SITE     1 AC5  3 ALA C  74  ARG C  76  ASP C  78                               
SITE     1 AC6  4 TYR C 184  ALA C 185  TYR E 188  ASN F  66                    
SITE     1 AC7  4 ARG A 179  ALA D  74  ARG D  76  ASP D  78                    
SITE     1 AC8  5 ALA B 186  TYR D 189  TYR E  64  ASN E  66                    
SITE     2 AC8  5 TYR E  72                                                     
SITE     1 AC9  3 ALA E  74  ARG E  76  ASP E  78                               
SITE     1 AD1  3 ALA F  74  ARG F  76  ASP F  78                               
SITE     1 AD2  3 ALA A 186  ASN D  66  TYR F 189                               
CRYST1  126.148  126.148  216.211  90.00  90.00 120.00 P 31 2 1     24          
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      0.007927  0.004577  0.000000        0.00000                         
SCALE2      0.000000  0.009154  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004625        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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