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Database: PDB
Entry: 4ZNE
LinkDB: 4ZNE
Original site: 4ZNE 
HEADER    IMMUNE SYSTEM                           04-MAY-15   4ZNE              
TITLE     IGG1 FC-FCGAMMARI ECD COMPLEX                                         
CAVEAT     4ZNE    NAG D 2 HAS WRONG CHIRALITY AT ATOM C1 MAN F 3 HAS WRONG     
CAVEAT   2 4ZNE    CHIRALITY AT ATOM C1 MAN G 3 HAS WRONG CHIRALITY AT ATOM C1  
CAVEAT   3 4ZNE    NAG A 305 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIGH AFFINITY IMMUNOGLOBULIN GAMMA FC RECEPTOR I;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 16-282;                                       
COMPND   5 SYNONYM: IGG FC RECEPTOR I,FC-GAMMA RI,FCRI,FC-GAMMA RIA,FCGAMMARIA; 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: IG GAMMA-1 CHAIN C REGION;                                 
COMPND   9 CHAIN: E, J;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 104-330;                                      
COMPND  11 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: FCGR1A, FCG1, FCGR1, IGFR1;                                    
SOURCE   6 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR PCK146;               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 943932;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: IGHG1;                                                         
SOURCE  13 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR PBGSA;                
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 285261                                      
KEYWDS    ANTIBODY, CONSTANT REGION, RECEPTOR, HIGH AFFINITY, IMMUNE SYSTEM     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.Y.OGANESYAN,W.F.DALL'ACQUA                                          
REVDAT   3   29-JUL-20 4ZNE    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   3 2                   1       LINK   SITE   ATOM                       
REVDAT   2   18-NOV-15 4ZNE    1       JRNL                                     
REVDAT   1   11-NOV-15 4ZNE    0                                                
JRNL        AUTH   V.OGANESYAN,Y.MAZOR,C.YANG,K.E.COOK,R.M.WOODS,A.FERGUSON,    
JRNL        AUTH 2 M.A.BOWEN,T.MARTIN,J.ZHU,H.WU,W.F.DALL'ACQUA                 
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE INTERACTION OF HUMAN IGG1 WITH  
JRNL        TITL 2 FC GAMMA RI: NO DIRECT ROLE OF GLYCANS IN BINDING.           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  2354 2015              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        PMID   26527150                                                     
JRNL        DOI    10.1107/S1399004715018015                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 38042                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1950                            
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) : 2.42                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.48                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2812                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 139                          
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5311                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 321                                     
REMARK   3   SOLVENT ATOMS            : 135                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.16000                                              
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : 0.39000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.83000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.308         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.177         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.558        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5799 ; 0.011 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3900 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7929 ; 1.566 ; 2.022       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9480 ; 0.860 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   660 ; 7.115 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   242 ;33.256 ;24.421       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   917 ;14.139 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;15.877 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   941 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6078 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1084 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  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  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 4ZNE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209576.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM ZINC ACETATE DEHYDRATE AND 20%     
REMARK 280  PEG 3350, PH 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       67.36750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.37500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       67.36750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       63.37500            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, J, B, C, D, F, G                
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 416  LIES ON A SPECIAL POSITION.                          
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     GLN A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     VAL A    23                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     HIS A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     PRO A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     SER A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     ARG A    87                                                      
REMARK 465     GLY A    88                                                      
REMARK 465     LEU A    89                                                      
REMARK 465     SER A    90                                                      
REMARK 465     GLN A   219                                                      
REMARK 465     ARG A   220                                                      
REMARK 465     PRO A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     ASP E   221                                                      
REMARK 465     LYS E   222                                                      
REMARK 465     THR E   223                                                      
REMARK 465     HIS E   224                                                      
REMARK 465     THR E   225                                                      
REMARK 465     CYS E   226                                                      
REMARK 465     PRO E   227                                                      
REMARK 465     PRO E   228                                                      
REMARK 465     CYS E   229                                                      
REMARK 465     PRO E   230                                                      
REMARK 465     ALA E   231                                                      
REMARK 465     LYS E   447                                                      
REMARK 465     ASP J   221                                                      
REMARK 465     LYS J   222                                                      
REMARK 465     THR J   223                                                      
REMARK 465     HIS J   224                                                      
REMARK 465     THR J   225                                                      
REMARK 465     CYS J   226                                                      
REMARK 465     PRO J   227                                                      
REMARK 465     PRO J   228                                                      
REMARK 465     CYS J   229                                                      
REMARK 465     PRO J   230                                                      
REMARK 465     ALA J   231                                                      
REMARK 465     PRO J   232                                                      
REMARK 465     GLU J   233                                                      
REMARK 465     LEU J   234                                                      
REMARK 465     LEU J   235                                                      
REMARK 465     PRO J   445                                                      
REMARK 465     GLY J   446                                                      
REMARK 465     LYS J   447                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O4   NAG D     1     O5   NAG D     2              1.51            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    HIS A 148   CG    HIS A 148   CD2     0.056                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  28   C   -  N   -  CD  ANGL. DEV. = -17.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  28      112.23     31.31                                   
REMARK 500    THR A  67      149.23    -33.17                                   
REMARK 500    ARG A 239      119.93    -24.16                                   
REMARK 500    ASN E 325      146.83   -171.00                                   
REMARK 500    ASN E 434       12.86     54.84                                   
REMARK 500    ASP J 280       49.53     36.06                                   
REMARK 500    PRO J 374     -176.99    -69.81                                   
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 GLN A   27     PRO A   28                 -120.18                    
REMARK 500 THR A  199     SER A  200                 -149.98                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 310  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 261   OE2                                                    
REMARK 620 2 HIS E 268   NE2  97.3                                              
REMARK 620 3 GLU E 294   OE2  96.8   2.0                                        
REMARK 620 4 HOH E 617   O    92.3  51.4  49.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 509  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 277   OE1                                                    
REMARK 620 2 GLU A 277   OE2  54.5                                              
REMARK 620 3 HIS J 310   NE2 104.9 102.2                                        
REMARK 620 4 HIS J 435   NE2 104.5 103.5   1.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 509  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 310   NE2                                                    
REMARK 620 2 HIS E 433   ND1 164.6                                              
REMARK 620 3 HIS E 435   NE2 113.4  58.9                                        
REMARK 620 4 HOH E 654   O   160.7  21.0  48.3                                  
REMARK 620 N                    1     2     3                                   
DBREF  4ZNE A   16   282  UNP    P12314   FCGR1_HUMAN     16    282             
DBREF  4ZNE E  221   447  UNP    P01857   IGHG1_HUMAN    104    330             
DBREF  4ZNE J  221   447  UNP    P01857   IGHG1_HUMAN    104    330             
SEQRES   1 A  267  GLN VAL ASP THR THR LYS ALA VAL ILE THR LEU GLN PRO          
SEQRES   2 A  267  PRO TRP VAL SER VAL PHE GLN GLU GLU THR VAL THR LEU          
SEQRES   3 A  267  HIS CYS GLU VAL LEU HIS LEU PRO GLY SER SER SER THR          
SEQRES   4 A  267  GLN TRP PHE LEU ASN GLY THR ALA THR GLN THR SER THR          
SEQRES   5 A  267  PRO SER TYR ARG ILE THR SER ALA SER VAL ASN ASP SER          
SEQRES   6 A  267  GLY GLU TYR ARG CYS GLN ARG GLY LEU SER GLY ARG SER          
SEQRES   7 A  267  ASP PRO ILE GLN LEU GLU ILE HIS ARG GLY TRP LEU LEU          
SEQRES   8 A  267  LEU GLN VAL SER SER ARG VAL PHE THR GLU GLY GLU PRO          
SEQRES   9 A  267  LEU ALA LEU ARG CYS HIS ALA TRP LYS ASP LYS LEU VAL          
SEQRES  10 A  267  TYR ASN VAL LEU TYR TYR ARG ASN GLY LYS ALA PHE LYS          
SEQRES  11 A  267  PHE PHE HIS TRP ASN SER ASN LEU THR ILE LEU LYS THR          
SEQRES  12 A  267  ASN ILE SER HIS ASN GLY THR TYR HIS CYS SER GLY MET          
SEQRES  13 A  267  GLY LYS HIS ARG TYR THR SER ALA GLY ILE SER VAL THR          
SEQRES  14 A  267  VAL LYS GLU LEU PHE PRO ALA PRO VAL LEU ASN ALA SER          
SEQRES  15 A  267  VAL THR SER PRO LEU LEU GLU GLY ASN LEU VAL THR LEU          
SEQRES  16 A  267  SER CYS GLU THR LYS LEU LEU LEU GLN ARG PRO GLY LEU          
SEQRES  17 A  267  GLN LEU TYR PHE SER PHE TYR MET GLY SER LYS THR LEU          
SEQRES  18 A  267  ARG GLY ARG ASN THR SER SER GLU TYR GLN ILE LEU THR          
SEQRES  19 A  267  ALA ARG ARG GLU ASP SER GLY LEU TYR TRP CYS GLU ALA          
SEQRES  20 A  267  ALA THR GLU ASP GLY ASN VAL LEU LYS ARG SER PRO GLU          
SEQRES  21 A  267  LEU GLU LEU GLN VAL LEU GLY                                  
SEQRES   1 E  227  ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU          
SEQRES   2 E  227  LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS          
SEQRES   3 E  227  PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL          
SEQRES   4 E  227  THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU          
SEQRES   5 E  227  VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS          
SEQRES   6 E  227  ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER          
SEQRES   7 E  227  THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN          
SEQRES   8 E  227  ASP TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER          
SEQRES   9 E  227  ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER          
SEQRES  10 E  227  LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR          
SEQRES  11 E  227  LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL          
SEQRES  12 E  227  SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP          
SEQRES  13 E  227  ILE ALA VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN          
SEQRES  14 E  227  ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY          
SEQRES  15 E  227  SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER          
SEQRES  16 E  227  ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET          
SEQRES  17 E  227  HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU          
SEQRES  18 E  227  SER LEU SER PRO GLY LYS                                      
SEQRES   1 J  227  ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU          
SEQRES   2 J  227  LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS          
SEQRES   3 J  227  PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL          
SEQRES   4 J  227  THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU          
SEQRES   5 J  227  VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS          
SEQRES   6 J  227  ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER          
SEQRES   7 J  227  THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN          
SEQRES   8 J  227  ASP TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER          
SEQRES   9 J  227  ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER          
SEQRES  10 J  227  LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR          
SEQRES  11 J  227  LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL          
SEQRES  12 J  227  SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP          
SEQRES  13 J  227  ILE ALA VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN          
SEQRES  14 J  227  ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY          
SEQRES  15 J  227  SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER          
SEQRES  16 J  227  ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET          
SEQRES  17 J  227  HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU          
SEQRES  18 J  227  SER LEU SER PRO GLY LYS                                      
MODRES 4ZNE NAG B    1  NAG  -D                                                 
MODRES 4ZNE NAG B    2  NAG  -D                                                 
MODRES 4ZNE NAG A  304  NAG  -D                                                 
MODRES 4ZNE NAG A  305  NAG  -D                                                 
MODRES 4ZNE NAG C    1  NAG  -D                                                 
MODRES 4ZNE NAG D    1  NAG  -D                                                 
MODRES 4ZNE NAG D    2  NAG  -D                                                 
MODRES 4ZNE NAG F    1  NAG  -D                                                 
MODRES 4ZNE NAG F    2  NAG  -D                                                 
MODRES 4ZNE NAG F    5  NAG  -D                                                 
MODRES 4ZNE NAG F    7  NAG  -D                                                 
MODRES 4ZNE NAG G    1  NAG  -D                                                 
MODRES 4ZNE NAG G    2  NAG  -D                                                 
MODRES 4ZNE NAG G    5  NAG  -D                                                 
MODRES 4ZNE NAG G    7  NAG  -D                                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    MAN  B   3      11                                                       
HET    NAG  C   1      14                                                       
HET    MAN  C   2      11                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    MAN  F   3      11                                                       
HET    MAN  F   4      11                                                       
HET    NAG  F   5      14                                                       
HET    MAN  F   6      11                                                       
HET    NAG  F   7      14                                                       
HET    FUL  F   8      10                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    MAN  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    NAG  G   5      14                                                       
HET    MAN  G   6      11                                                       
HET    NAG  G   7      14                                                       
HET    FUL  G   8      10                                                       
HET    NAG  A 304      14                                                       
HET    NAG  A 305      14                                                       
HET     ZN  A 310       1                                                       
HET     ZN  E 509       1                                                       
HET     ZN  J 509       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     FUL BETA-L-FUCOPYRANOSE                                              
HETNAM      ZN ZINC ION                                                         
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   4  NAG    15(C8 H15 N O6)                                              
FORMUL   4  MAN    8(C6 H12 O6)                                                 
FORMUL   7  FUL    2(C6 H12 O5)                                                 
FORMUL  11   ZN    3(ZN 2+)                                                     
FORMUL  14  HOH   *135(H2 O)                                                    
HELIX    1 AA1 SER A   76  SER A   80  5                                   5    
HELIX    2 AA2 LYS A  128  LYS A  130  5                                   3    
HELIX    3 AA3 ASN A  159  ASN A  163  5                                   5    
HELIX    4 AA4 ARG A  251  SER A  255  5                                   5    
HELIX    5 AA5 LYS E  246  MET E  252  1                                   7    
HELIX    6 AA6 LEU E  309  ASN E  315  1                                   7    
HELIX    7 AA7 SER E  354  LYS E  360  5                                   7    
HELIX    8 AA8 LYS E  414  GLN E  419  1                                   6    
HELIX    9 AA9 LEU E  432  TYR E  436  5                                   5    
HELIX   10 AB1 LYS J  246  MET J  252  1                                   7    
HELIX   11 AB2 LEU J  309  ASN J  315  1                                   7    
HELIX   12 AB3 SER J  354  LYS J  360  5                                   7    
HELIX   13 AB4 LYS J  414  GLN J  419  1                                   6    
HELIX   14 AB5 LEU J  432  ASN J  434  5                                   3    
SHEET    1 AA1 3 THR A  25  GLN A  27  0                                        
SHEET    2 AA1 3 VAL A  39  HIS A  42 -1  O  HIS A  42   N  THR A  25           
SHEET    3 AA1 3 SER A  69  ILE A  72 -1  O  TYR A  70   N  LEU A  41           
SHEET    1 AA2 5 SER A  32  PHE A  34  0                                        
SHEET    2 AA2 5 ILE A  96  HIS A 101  1  O  HIS A 101   N  VAL A  33           
SHEET    3 AA2 5 GLY A  81  CYS A  85 -1  N  TYR A  83   O  ILE A  96           
SHEET    4 AA2 5 TRP A  56  LEU A  58 -1  N  PHE A  57   O  ARG A  84           
SHEET    5 AA2 5 THR A  61  ALA A  62 -1  O  THR A  61   N  LEU A  58           
SHEET    1 AA3 3 LEU A 105  VAL A 109  0                                        
SHEET    2 AA3 3 LEU A 120  ALA A 126 -1  O  ARG A 123   N  GLN A 108           
SHEET    3 AA3 3 LEU A 153  ILE A 155 -1  O  LEU A 153   N  LEU A 122           
SHEET    1 AA4 5 VAL A 113  THR A 115  0                                        
SHEET    2 AA4 5 ILE A 181  LYS A 186  1  O  THR A 184   N  PHE A 114           
SHEET    3 AA4 5 GLY A 164  MET A 171 -1  N  TYR A 166   O  ILE A 181           
SHEET    4 AA4 5 TYR A 133  ARG A 139 -1  N  TYR A 138   O  HIS A 167           
SHEET    5 AA4 5 LYS A 142  TRP A 149 -1  O  PHE A 144   N  TYR A 137           
SHEET    1 AA5 4 VAL A 113  THR A 115  0                                        
SHEET    2 AA5 4 ILE A 181  LYS A 186  1  O  THR A 184   N  PHE A 114           
SHEET    3 AA5 4 GLY A 164  MET A 171 -1  N  TYR A 166   O  ILE A 181           
SHEET    4 AA5 4 ARG A 175  THR A 177 -1  O  TYR A 176   N  GLY A 170           
SHEET    1 AA6 3 VAL A 193  ALA A 196  0                                        
SHEET    2 AA6 3 VAL A 208  GLU A 213 -1  O  SER A 211   N  ASN A 195           
SHEET    3 AA6 3 GLU A 244  ILE A 247 -1  O  ILE A 247   N  VAL A 208           
SHEET    1 AA7 5 PRO A 201  LEU A 203  0                                        
SHEET    2 AA7 5 LEU A 276  LEU A 281  1  O  LEU A 281   N  LEU A 202           
SHEET    3 AA7 5 GLY A 256  THR A 264 -1  N  TYR A 258   O  LEU A 276           
SHEET    4 AA7 5 LEU A 225  MET A 231 -1  N  TYR A 226   O  ALA A 263           
SHEET    5 AA7 5 LYS A 234  ASN A 240 -1  O  ASN A 240   N  PHE A 227           
SHEET    1 AA8 4 PRO A 201  LEU A 203  0                                        
SHEET    2 AA8 4 LEU A 276  LEU A 281  1  O  LEU A 281   N  LEU A 202           
SHEET    3 AA8 4 GLY A 256  THR A 264 -1  N  TYR A 258   O  LEU A 276           
SHEET    4 AA8 4 LEU A 270  ARG A 272 -1  O  LYS A 271   N  ALA A 262           
SHEET    1 AA9 4 SER E 239  PHE E 243  0                                        
SHEET    2 AA9 4 GLU E 258  VAL E 266 -1  O  VAL E 262   N  PHE E 241           
SHEET    3 AA9 4 TYR E 300  THR E 307 -1  O  TYR E 300   N  VAL E 266           
SHEET    4 AA9 4 LYS E 288  THR E 289 -1  N  LYS E 288   O  VAL E 305           
SHEET    1 AB1 4 SER E 239  PHE E 243  0                                        
SHEET    2 AB1 4 GLU E 258  VAL E 266 -1  O  VAL E 262   N  PHE E 241           
SHEET    3 AB1 4 TYR E 300  THR E 307 -1  O  TYR E 300   N  VAL E 266           
SHEET    4 AB1 4 GLU E 293  GLU E 294 -1  N  GLU E 293   O  ARG E 301           
SHEET    1 AB2 4 VAL E 282  VAL E 284  0                                        
SHEET    2 AB2 4 LYS E 274  VAL E 279 -1  N  VAL E 279   O  VAL E 282           
SHEET    3 AB2 4 TYR E 319  SER E 324 -1  O  LYS E 322   N  ASN E 276           
SHEET    4 AB2 4 ILE E 332  ILE E 336 -1  O  ILE E 336   N  TYR E 319           
SHEET    1 AB3 4 GLN E 347  LEU E 351  0                                        
SHEET    2 AB3 4 GLN E 362  PHE E 372 -1  O  LYS E 370   N  GLN E 347           
SHEET    3 AB3 4 PHE E 404  ASP E 413 -1  O  LEU E 410   N  LEU E 365           
SHEET    4 AB3 4 TYR E 391  THR E 393 -1  N  LYS E 392   O  LYS E 409           
SHEET    1 AB4 4 GLN E 347  LEU E 351  0                                        
SHEET    2 AB4 4 GLN E 362  PHE E 372 -1  O  LYS E 370   N  GLN E 347           
SHEET    3 AB4 4 PHE E 404  ASP E 413 -1  O  LEU E 410   N  LEU E 365           
SHEET    4 AB4 4 VAL E 397  LEU E 398 -1  N  VAL E 397   O  PHE E 405           
SHEET    1 AB5 4 GLN E 386  GLU E 388  0                                        
SHEET    2 AB5 4 ALA E 378  SER E 383 -1  N  TRP E 381   O  GLU E 388           
SHEET    3 AB5 4 PHE E 423  MET E 428 -1  O  SER E 426   N  GLU E 380           
SHEET    4 AB5 4 THR E 437  LEU E 441 -1  O  LYS E 439   N  CYS E 425           
SHEET    1 AB6 4 SER J 239  PHE J 243  0                                        
SHEET    2 AB6 4 GLU J 258  VAL J 266 -1  O  VAL J 262   N  PHE J 241           
SHEET    3 AB6 4 TYR J 300  THR J 307 -1  O  SER J 304   N  CYS J 261           
SHEET    4 AB6 4 LYS J 288  THR J 289 -1  N  LYS J 288   O  VAL J 305           
SHEET    1 AB7 4 SER J 239  PHE J 243  0                                        
SHEET    2 AB7 4 GLU J 258  VAL J 266 -1  O  VAL J 262   N  PHE J 241           
SHEET    3 AB7 4 TYR J 300  THR J 307 -1  O  SER J 304   N  CYS J 261           
SHEET    4 AB7 4 GLU J 293  GLU J 294 -1  N  GLU J 293   O  ARG J 301           
SHEET    1 AB8 4 VAL J 282  VAL J 284  0                                        
SHEET    2 AB8 4 LYS J 274  VAL J 279 -1  N  VAL J 279   O  VAL J 282           
SHEET    3 AB8 4 TYR J 319  SER J 324 -1  O  LYS J 322   N  ASN J 276           
SHEET    4 AB8 4 ILE J 332  ILE J 336 -1  O  ILE J 336   N  TYR J 319           
SHEET    1 AB9 4 GLN J 347  LEU J 351  0                                        
SHEET    2 AB9 4 GLN J 362  PHE J 372 -1  O  LEU J 368   N  TYR J 349           
SHEET    3 AB9 4 PHE J 404  ASP J 413 -1  O  PHE J 404   N  PHE J 372           
SHEET    4 AB9 4 TYR J 391  THR J 393 -1  N  LYS J 392   O  LYS J 409           
SHEET    1 AC1 4 GLN J 347  LEU J 351  0                                        
SHEET    2 AC1 4 GLN J 362  PHE J 372 -1  O  LEU J 368   N  TYR J 349           
SHEET    3 AC1 4 PHE J 404  ASP J 413 -1  O  PHE J 404   N  PHE J 372           
SHEET    4 AC1 4 VAL J 397  LEU J 398 -1  N  VAL J 397   O  PHE J 405           
SHEET    1 AC2 4 GLN J 386  PRO J 387  0                                        
SHEET    2 AC2 4 ALA J 378  SER J 383 -1  N  SER J 383   O  GLN J 386           
SHEET    3 AC2 4 PHE J 423  MET J 428 -1  O  MET J 428   N  ALA J 378           
SHEET    4 AC2 4 TYR J 436  LEU J 441 -1  O  LYS J 439   N  CYS J 425           
SSBOND   1 CYS A   43    CYS A   85                          1555   1555  2.04  
SSBOND   2 CYS A  124    CYS A  168                          1555   1555  2.09  
SSBOND   3 CYS A  212    CYS A  260                          1555   1555  2.07  
SSBOND   4 CYS E  261    CYS E  321                          1555   1555  2.03  
SSBOND   5 CYS E  367    CYS E  425                          1555   1555  2.03  
SSBOND   6 CYS J  261    CYS J  321                          1555   1555  2.03  
SSBOND   7 CYS J  367    CYS J  425                          1555   1555  2.05  
LINK         ND2 ASN A  59                 C1  NAG B   1     1555   1555  1.44  
LINK         ND2 ASN A  78                 C1  NAG A 304     1555   1555  1.46  
LINK         ND2 ASN A 152                 C1  NAG A 305     1555   1555  1.27  
LINK         ND2 ASN A 159                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN A 163                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN E 297                 C1  NAG F   1     1555   1555  1.44  
LINK         ND2 ASN J 297                 C1  NAG G   1     1555   1555  1.44  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.46  
LINK         O3  NAG B   2                 C1  MAN B   3     1555   1555  1.47  
LINK         O4  NAG C   1                 C1  MAN C   2     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.30  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O6  NAG F   1                 C1  FUL F   8     1555   1555  1.45  
LINK         O4  NAG F   2                 C1  MAN F   3     1555   1555  1.45  
LINK         O3  MAN F   3                 C1  MAN F   4     1555   1555  1.43  
LINK         O6  MAN F   3                 C1  MAN F   6     1555   1555  1.43  
LINK         O2  MAN F   4                 C1  NAG F   5     1555   1555  1.43  
LINK         O2  MAN F   6                 C1  NAG F   7     1555   1555  1.42  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.42  
LINK         O6  NAG G   1                 C1  FUL G   8     1555   1555  1.44  
LINK         O4  NAG G   2                 C1  MAN G   3     1555   1555  1.43  
LINK         O3  MAN G   3                 C1  MAN G   4     1555   1555  1.44  
LINK         O6  MAN G   3                 C1  MAN G   6     1555   1555  1.44  
LINK         O2  MAN G   4                 C1  NAG G   5     1555   1555  1.44  
LINK         O2  MAN G   6                 C1  NAG G   7     1555   1555  1.44  
LINK         OE2 GLU A 261                ZN    ZN A 310     1555   1555  1.86  
LINK         OE1 GLU A 277                ZN    ZN J 509     1555   4455  2.17  
LINK         OE2 GLU A 277                ZN    ZN J 509     1555   4455  2.55  
LINK        ZN    ZN A 310                 NE2 HIS E 268     4444   1555  2.13  
LINK        ZN    ZN A 310                 OE2 GLU E 294     4444   1555  1.86  
LINK        ZN    ZN A 310                 O   HOH E 617     1555   4454  2.24  
LINK         NE2 HIS E 310                ZN    ZN E 509     1555   2555  2.05  
LINK         ND1 HIS E 433                ZN    ZN E 509     1555   1555  1.92  
LINK         NE2 HIS E 435                ZN    ZN E 509     1555   2555  2.30  
LINK        ZN    ZN E 509                 O   HOH E 654     1555   2555  2.00  
LINK         NE2 HIS J 310                ZN    ZN J 509     1555   1555  1.89  
LINK         NE2 HIS J 435                ZN    ZN J 509     1555   1555  2.02  
CISPEP   1 TYR E  373    PRO E  374          0        -7.61                     
CISPEP   2 TYR J  373    PRO J  374          0        -8.92                     
CRYST1  134.735  126.750   71.844  90.00 118.44  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007422  0.000000  0.004019        0.00000                         
SCALE2      0.000000  0.007890  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015829        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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