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Database: PDB
Entry: 4P5M
LinkDB: 4P5M
Original site: 4P5M 
HEADER    IMMUNE SYSTEM                           18-MAR-14   4P5M              
TITLE     STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: BRIDGING THE GAP       
TITLE    2 BETWEEN ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN; 
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 32-214;                                       
COMPND   5 SYNONYM: DP(W3),DP(W4),HLA-SB ALPHA CHAIN,MHC CLASS II DP3-ALPHA,MHC 
COMPND   6 CLASS II DPA1;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PEPTIDE,HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP BETA 1 
COMPND  10 CHAIN;                                                               
COMPND  11 CHAIN: B, D, F, H;                                                   
COMPND  12 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,DP(W2) BETA CHAIN,  
COMPND  13 MHC CLASS II ANTIGEN DPB1;                                           
COMPND  14 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: HLA-DPA1, HLA-DP1A, HLASB;                                     
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: HLA-DPB1;                                                      
SOURCE  13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    CBD, AUTOIMMUNITY, BERYLLIUM, IMMUNE SYSTEM                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.WANG,S.DAI,J.KAPPLER                                                
REVDAT   4   29-JUL-20 4P5M    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   14-OCT-15 4P5M    1       REMARK                                   
REVDAT   2   14-JAN-15 4P5M    1       LINK   ATOM                              
REVDAT   1   27-AUG-14 4P5M    0                                                
JRNL        AUTH   G.M.CLAYTON,Y.WANG,F.CRAWFORD,A.NOVIKOV,B.T.WIMBERLY,        
JRNL        AUTH 2 J.S.KIEFT,M.T.FALTA,N.A.BOWERMAN,P.MARRACK,A.P.FONTENOT,     
JRNL        AUTH 3 S.DAI,J.W.KAPPLER                                            
JRNL        TITL   STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: LINKING       
JRNL        TITL 2 ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY.                  
JRNL        REF    CELL                          V. 158   132 2014              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   24995984                                                     
JRNL        DOI    10.1016/J.CELL.2014.04.048                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 196507                         
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10563                           
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8046                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 48.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 477                          
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12284                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 290                                     
REMARK   3   SOLVENT ATOMS            : 1660                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.26000                                              
REMARK   3    B22 (A**2) : -0.55000                                             
REMARK   3    B33 (A**2) : 0.21000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.12000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.098         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.965         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13154 ; 0.023 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 11789 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17960 ; 2.222 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 27039 ; 1.046 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1528 ; 7.286 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   718 ;33.820 ;24.471       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2029 ;14.957 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    76 ;14.301 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1939 ; 0.181 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14958 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3218 ; 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 : 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 4P5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200706.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 196507                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 1.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M CITRATE PH6.5, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       65.23400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, M                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, N, O                            
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     GLN A   181                                                      
REMARK 465     GLU A   182                                                      
REMARK 465     PRO A   183                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     VAL B    -9                                                      
REMARK 465     PRO B    -8                                                      
REMARK 465     ARG B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLN C   181                                                      
REMARK 465     GLU C   182                                                      
REMARK 465     PRO C   183                                                      
REMARK 465     GLY D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     LEU D   -10                                                      
REMARK 465     VAL D    -9                                                      
REMARK 465     PRO D    -8                                                      
REMARK 465     ARG D    -7                                                      
REMARK 465     GLY D    -6                                                      
REMARK 465     SER D    -5                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     3                                                      
REMARK 465     GLN E   181                                                      
REMARK 465     GLU E   182                                                      
REMARK 465     PRO E   183                                                      
REMARK 465     GLY F   -12                                                      
REMARK 465     SER F   -11                                                      
REMARK 465     LEU F   -10                                                      
REMARK 465     VAL F    -9                                                      
REMARK 465     PRO F    -8                                                      
REMARK 465     ARG F    -7                                                      
REMARK 465     GLY F    -6                                                      
REMARK 465     SER F    -5                                                      
REMARK 465     GLY F    -4                                                      
REMARK 465     GLY F    -3                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     GLY F    -1                                                      
REMARK 465     SER F     3                                                      
REMARK 465     LYS F   103                                                      
REMARK 465     LYS F   104                                                      
REMARK 465     GLY F   105                                                      
REMARK 465     PRO F   106                                                      
REMARK 465     LEU F   107                                                      
REMARK 465     GLN F   108                                                      
REMARK 465     HIS F   109                                                      
REMARK 465     HIS F   110                                                      
REMARK 465     GLN F   189                                                      
REMARK 465     GLN G   181                                                      
REMARK 465     GLU G   182                                                      
REMARK 465     PRO G   183                                                      
REMARK 465     GLY H   -12                                                      
REMARK 465     SER H   -11                                                      
REMARK 465     LEU H   -10                                                      
REMARK 465     VAL H    -9                                                      
REMARK 465     PRO H    -8                                                      
REMARK 465     ARG H    -7                                                      
REMARK 465     GLY H    -6                                                      
REMARK 465     SER H    -5                                                      
REMARK 465     GLY H    -4                                                      
REMARK 465     GLY H    -3                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     GLY H    -1                                                      
REMARK 465     LYS H   103                                                      
REMARK 465     LYS H   104                                                      
REMARK 465     GLY H   105                                                      
REMARK 465     PRO H   106                                                      
REMARK 465     LEU H   107                                                      
REMARK 465     GLN H   108                                                      
REMARK 465     HIS H   109                                                      
REMARK 465     HIS H   110                                                      
REMARK 465     GLN H   189                                                      
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     GLN B -25    CG   CD   OE1  NE2                                  
REMARK 470     GLN D -25    CG   CD   OE1  NE2                                  
REMARK 470     GLN F -25    CG   CD   OE1  NE2                                  
REMARK 470     GLN H -25    CG   CD   OE1  NE2                                  
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   O    HOH C   387     O    HOH C   489              1.66            
REMARK 500   O    HOH H   342     O    HOH H   381              1.80            
REMARK 500   O    HOH B   381     O    HOH B   456              1.89            
REMARK 500   OE1  GLU F    44     O    HOH F   301              1.94            
REMARK 500   OD1  ASP G    85     O    HOH G   368              1.94            
REMARK 500   OE1  GLU E    95     OD2  ASP F   119              1.95            
REMARK 500   O    HOH A   362     O    HOH A   473              1.99            
REMARK 500   O    HOH C   362     O    HOH C   493              2.00            
REMARK 500   O    HOH D   436     O    HOH D   460              2.00            
REMARK 500   OD1  ASN E   118     O    HOH E   482              2.04            
REMARK 500   OE2  GLU F    44     NH1  ARG F    46              2.04            
REMARK 500   O    HOH B   492     O    HOH H   513              2.05            
REMARK 500   O    HOH B   303     O    HOH B   310              2.05            
REMARK 500   O    HOH C   335     O    HOH C   494              2.08            
REMARK 500   OE1  GLU D   185     O    HOH D   444              2.08            
REMARK 500   O    HOH B   365     O    HOH D   347              2.10            
REMARK 500   OD1  ASP D   -22     O    HOH D   454              2.11            
REMARK 500   O    HOH D   471     O    HOH F   442              2.11            
REMARK 500   O    HOH F   486     O    HOH F   507              2.12            
REMARK 500   OD1  ASP B   -22     O    HOH B   482              2.13            
REMARK 500   OD1  ASN G   118     O    HOH G   433              2.13            
REMARK 500   NH1  ARG B    53     O    HOH B   421              2.13            
REMARK 500   OD1  ASN A   118     O    HOH A   301              2.13            
REMARK 500   O    HOH G   431     O    HOH G   465              2.14            
REMARK 500   O    HOH H   438     O    HOH H   488              2.14            
REMARK 500   O    HOH B   360     O    HOH B   423              2.15            
REMARK 500   O    ALA E   180     O    HOH E   515              2.15            
REMARK 500   O    HOH E   403     O    HOH E   442              2.15            
REMARK 500   O    LEU E   170     O    HOH E   331              2.16            
REMARK 500   O    HOH F   301     O    HOH F   320              2.16            
REMARK 500   O    HOH A   342     O    HOH A   487              2.16            
REMARK 500   O    HOH C   443     O    HOH C   478              2.17            
REMARK 500   O    HOH E   390     O    HOH E   498              2.17            
REMARK 500   O    HOH B   366     O    HOH D   438              2.17            
REMARK 500   OE1  GLU H    57     O    HOH H   301              2.19            
REMARK 500   O    HOH A   336     O    HOH A   337              2.19            
REMARK 500   O    HOH E   386     O    HOH E   520              2.19            
REMARK 500   O    HOH E   414     O    HOH E   507              2.19            
REMARK 500   O    ALA H   188     O    HOH H   507              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   301     O    HOH G   313     2645     2.01            
REMARK 500   NZ   LYS A    39     OD2  ASP F    64     2545     2.19            
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    GLU C  40   CD    GLU C  40   OE1     0.076                       
REMARK 500    TYR C 150   CG    TYR C 150   CD1     0.087                       
REMARK 500    GLU E  55   CD    GLU E  55   OE1     0.077                       
REMARK 500    GLU E  55   CD    GLU E  55   OE2     0.089                       
REMARK 500    GLU E  95   CD    GLU E  95   OE2     0.085                       
REMARK 500    GLU F  69   CD    GLU F  69   OE2     0.070                       
REMARK 500    GLU F  82   CD    GLU F  82   OE2     0.086                       
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    LEU A  60   CA  -  CB  -  CG  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU A  73   CA  -  CB  -  CG  ANGL. DEV. = -17.6 DEGREES          
REMARK 500    ARG A  76   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A  76   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    LEU A 117   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG B  78   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG B  78   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ASP C 110   CB  -  CG  -  OD1 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP D  39   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP D  39   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ARG D  75   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    GLU E  21   OE1 -  CD  -  OE2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG F  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP F  39   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG G 140   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG H  12   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG H  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 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    ASP A  27       46.94     38.83                                   
REMARK 500    ASN B  31     -112.30     59.19                                   
REMARK 500    ARG B  75      -97.74   -100.17                                   
REMARK 500    TRP B 151       31.04     71.72                                   
REMARK 500    ASP C  27       50.13     38.02                                   
REMARK 500    ASN D  31     -111.12     59.94                                   
REMARK 500    ARG D  75      -95.92   -103.07                                   
REMARK 500    TRP D 151       31.66     70.60                                   
REMARK 500    ASN F  31     -110.45     52.37                                   
REMARK 500    ARG F  75      -97.60   -106.02                                   
REMARK 500    THR F  88      -70.78   -134.59                                   
REMARK 500    ASN H  31     -109.21     53.80                                   
REMARK 500    ARG H  75      -98.13   -108.65                                   
REMARK 500    THR H  88      -79.79   -122.09                                   
REMARK 500    ASP H 119       35.21     70.74                                   
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 A 478        DISTANCE =  8.06 ANGSTROMS                       
REMARK 525    HOH B 472        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH C 518        DISTANCE =  7.56 ANGSTROMS                       
REMARK 525    HOH C 525        DISTANCE =  6.33 ANGSTROMS                       
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                              NA A 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 313   O                                                      
REMARK 620 2 HOH A 326   O    47.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  98   OE2                                                    
REMARK 620 2 HOH C 352   O   100.1                                              
REMARK 620 3 HOH C 474   O    56.0 152.9                                        
REMARK 620 4 GLU H 135   OE2 107.3 113.0  88.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P4K   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P4R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P57   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P5K   RELATED DB: PDB                                   
DBREF  4P5M A    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P5M B  -25   -14  PDB    4P5M     4P5M           -25    -14             
DBREF  4P5M B    3   189  UNP    Q5EP54   Q5EP54_HUMAN    32    218             
DBREF  4P5M C    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P5M D  -25   -14  PDB    4P5M     4P5M           -25    -14             
DBREF  4P5M D    3   189  UNP    Q5EP54   Q5EP54_HUMAN    32    218             
DBREF  4P5M E    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P5M F  -25   -14  PDB    4P5M     4P5M           -25    -14             
DBREF  4P5M F    3   189  UNP    Q5EP54   Q5EP54_HUMAN    32    218             
DBREF  4P5M G    1   183  UNP    P20036   DPA1_HUMAN      32    214             
DBREF  4P5M H  -25   -14  PDB    4P5M     4P5M           -25    -14             
DBREF  4P5M H    3   189  UNP    Q5EP54   Q5EP54_HUMAN    32    218             
SEQADV 4P5M GLY B  -13  PDB                      LINKER                         
SEQADV 4P5M GLY B  -12  PDB                      LINKER                         
SEQADV 4P5M SER B  -11  PDB                      LINKER                         
SEQADV 4P5M LEU B  -10  PDB                      LINKER                         
SEQADV 4P5M VAL B   -9  PDB                      LINKER                         
SEQADV 4P5M PRO B   -8  PDB                      LINKER                         
SEQADV 4P5M ARG B   -7  PDB                      LINKER                         
SEQADV 4P5M GLY B   -6  PDB                      LINKER                         
SEQADV 4P5M SER B   -5  PDB                      LINKER                         
SEQADV 4P5M GLY B   -4  PDB                      LINKER                         
SEQADV 4P5M GLY B   -3  PDB                      LINKER                         
SEQADV 4P5M GLY B   -2  PDB                      LINKER                         
SEQADV 4P5M GLY B   -1  PDB                      LINKER                         
SEQADV 4P5M SER B    3  UNP  Q5EP54    THR    32 VARIANT                        
SEQADV 4P5M GLY D  -13  PDB                      LINKER                         
SEQADV 4P5M GLY D  -12  PDB                      LINKER                         
SEQADV 4P5M SER D  -11  PDB                      LINKER                         
SEQADV 4P5M LEU D  -10  PDB                      LINKER                         
SEQADV 4P5M VAL D   -9  PDB                      LINKER                         
SEQADV 4P5M PRO D   -8  PDB                      LINKER                         
SEQADV 4P5M ARG D   -7  PDB                      LINKER                         
SEQADV 4P5M GLY D   -6  PDB                      LINKER                         
SEQADV 4P5M SER D   -5  PDB                      LINKER                         
SEQADV 4P5M GLY D   -4  PDB                      LINKER                         
SEQADV 4P5M GLY D   -3  PDB                      LINKER                         
SEQADV 4P5M GLY D   -2  PDB                      LINKER                         
SEQADV 4P5M GLY D   -1  PDB                      LINKER                         
SEQADV 4P5M SER D    3  UNP  Q5EP54    THR    32 VARIANT                        
SEQADV 4P5M GLY F  -13  PDB                      LINKER                         
SEQADV 4P5M GLY F  -12  PDB                      LINKER                         
SEQADV 4P5M SER F  -11  PDB                      LINKER                         
SEQADV 4P5M LEU F  -10  PDB                      LINKER                         
SEQADV 4P5M VAL F   -9  PDB                      LINKER                         
SEQADV 4P5M PRO F   -8  PDB                      LINKER                         
SEQADV 4P5M ARG F   -7  PDB                      LINKER                         
SEQADV 4P5M GLY F   -6  PDB                      LINKER                         
SEQADV 4P5M SER F   -5  PDB                      LINKER                         
SEQADV 4P5M GLY F   -4  PDB                      LINKER                         
SEQADV 4P5M GLY F   -3  PDB                      LINKER                         
SEQADV 4P5M GLY F   -2  PDB                      LINKER                         
SEQADV 4P5M GLY F   -1  PDB                      LINKER                         
SEQADV 4P5M SER F    3  UNP  Q5EP54    THR    32 VARIANT                        
SEQADV 4P5M GLY H  -13  PDB                      LINKER                         
SEQADV 4P5M GLY H  -12  PDB                      LINKER                         
SEQADV 4P5M SER H  -11  PDB                      LINKER                         
SEQADV 4P5M LEU H  -10  PDB                      LINKER                         
SEQADV 4P5M VAL H   -9  PDB                      LINKER                         
SEQADV 4P5M PRO H   -8  PDB                      LINKER                         
SEQADV 4P5M ARG H   -7  PDB                      LINKER                         
SEQADV 4P5M GLY H   -6  PDB                      LINKER                         
SEQADV 4P5M SER H   -5  PDB                      LINKER                         
SEQADV 4P5M GLY H   -4  PDB                      LINKER                         
SEQADV 4P5M GLY H   -3  PDB                      LINKER                         
SEQADV 4P5M GLY H   -2  PDB                      LINKER                         
SEQADV 4P5M GLY H   -1  PDB                      LINKER                         
SEQADV 4P5M SER H    3  UNP  Q5EP54    THR    32 VARIANT                        
SEQRES   1 A  183  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 A  183  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 A  183  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 A  183  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 A  183  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 A  183  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 A  183  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 A  183  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 A  183  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 A  183  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 A  183  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 A  183  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 A  183  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  183  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU          
SEQRES  15 A  183  PRO                                                          
SEQRES   1 B  212  GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY          
SEQRES   2 B  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 B  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 B  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 B  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 B  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 B  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 B  212  GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 B  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 B  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 B  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 B  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 B  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 B  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 B  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 B  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 B  212  TRP LYS ALA GLN                                              
SEQRES   1 C  183  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 C  183  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 C  183  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 C  183  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 C  183  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 C  183  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 C  183  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 C  183  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 C  183  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 C  183  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 C  183  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 C  183  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 C  183  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 C  183  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU          
SEQRES  15 C  183  PRO                                                          
SEQRES   1 D  212  GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY          
SEQRES   2 D  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 D  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 D  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 D  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 D  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 D  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 D  212  GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 D  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 D  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 D  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 D  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 D  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 D  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 D  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 D  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 D  212  TRP LYS ALA GLN                                              
SEQRES   1 E  183  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 E  183  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 E  183  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 E  183  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 E  183  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 E  183  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 E  183  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 E  183  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 E  183  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 E  183  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 E  183  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 E  183  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 E  183  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 E  183  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU          
SEQRES  15 E  183  PRO                                                          
SEQRES   1 F  212  GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY          
SEQRES   2 F  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 F  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 F  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 F  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 F  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 F  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 F  212  GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 F  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 F  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 F  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 F  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 F  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 F  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 F  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 F  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 F  212  TRP LYS ALA GLN                                              
SEQRES   1 G  183  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 G  183  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 G  183  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 G  183  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 G  183  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 G  183  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 G  183  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 G  183  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 G  183  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 G  183  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 G  183  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 G  183  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 G  183  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 G  183  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU          
SEQRES  15 G  183  PRO                                                          
SEQRES   1 H  212  GLN ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLY          
SEQRES   2 H  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 H  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 H  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 H  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 H  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 H  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 H  212  GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 H  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 H  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 H  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 H  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 H  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 H  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 H  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 H  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 H  212  TRP LYS ALA GLN                                              
MODRES 4P5M ASN A  118  ASN  GLYCOSYLATION SITE                                 
MODRES 4P5M ASN B   19  ASN  GLYCOSYLATION SITE                                 
MODRES 4P5M ASN C  118  ASN  GLYCOSYLATION SITE                                 
MODRES 4P5M ASN D   19  ASN  GLYCOSYLATION SITE                                 
MODRES 4P5M ASN E  118  ASN  GLYCOSYLATION SITE                                 
MODRES 4P5M ASN F   19  ASN  GLYCOSYLATION SITE                                 
MODRES 4P5M ASN G  118  ASN  GLYCOSYLATION SITE                                 
MODRES 4P5M ASN H   19  ASN  GLYCOSYLATION SITE                                 
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    NAG  J   3      14                                                       
HET    NAG  J   4      14                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    NAG  L   3      14                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    NAG  M   3      14                                                       
HET    BMA  M   4      11                                                       
HET    NAG  N   1      14                                                       
HET    NAG  N   2      14                                                       
HET    NAG  O   1      14                                                       
HET    BMA  O   2      11                                                       
HET    NAG  O   3      14                                                       
HET     NA  A 201       1                                                       
HET     NA  C 201       1                                                       
HET    NAG  E 201      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM      NA SODIUM ION                                                       
FORMUL   9  NAG    19(C8 H15 N O6)                                              
FORMUL  13  BMA    2(C6 H12 O6)                                                 
FORMUL  16   NA    2(NA 1+)                                                     
FORMUL  19  HOH   *1660(H2 O)                                                   
HELIX    1 AA1 LEU A   45  PHE A   52  1                                   8    
HELIX    2 AA2 GLU A   55  SER A   77  1                                  23    
HELIX    3 AA3 THR B   49  LEU B   51  5                                   3    
HELIX    4 AA4 GLY B   52  SER B   61  1                                  10    
HELIX    5 AA5 GLN B   62  ALA B   71  1                                  10    
HELIX    6 AA6 ARG B   75  GLY B   84  1                                  10    
HELIX    7 AA7 GLY B   84  GLN B   90  1                                   7    
HELIX    8 AA8 LYS B  104  HIS B  109  1                                   6    
HELIX    9 AA9 LEU C   45  PHE C   52  1                                   8    
HELIX   10 AB1 GLU C   55  SER C   77  1                                  23    
HELIX   11 AB2 THR D   49  LEU D   51  5                                   3    
HELIX   12 AB3 GLY D   52  SER D   61  1                                  10    
HELIX   13 AB4 GLN D   62  ALA D   71  1                                  10    
HELIX   14 AB5 ARG D   75  GLY D   84  1                                  10    
HELIX   15 AB6 GLY D   84  GLN D   90  1                                   7    
HELIX   16 AB7 LYS D  104  HIS D  109  1                                   6    
HELIX   17 AB8 LEU E   45  PHE E   52  1                                   8    
HELIX   18 AB9 GLU E   55  SER E   77  1                                  23    
HELIX   19 AC1 THR F   49  LEU F   51  5                                   3    
HELIX   20 AC2 GLY F   52  SER F   61  1                                  10    
HELIX   21 AC3 GLN F   62  ALA F   71  1                                  10    
HELIX   22 AC4 ARG F   75  GLY F   85  1                                  11    
HELIX   23 AC5 PRO F   86  THR F   88  5                                   3    
HELIX   24 AC6 LEU G   45  PHE G   52  1                                   8    
HELIX   25 AC7 GLU G   55  SER G   77  1                                  23    
HELIX   26 AC8 THR H   49  LEU H   51  5                                   3    
HELIX   27 AC9 GLY H   52  SER H   61  1                                  10    
HELIX   28 AD1 GLN H   62  ALA H   71  1                                  10    
HELIX   29 AD2 ARG H   75  GLY H   85  1                                  11    
HELIX   30 AD3 PRO H   86  THR H   88  5                                   3    
SHEET    1 AA1 8 GLU A  40  TRP A  43  0                                        
SHEET    2 AA1 8 ASP A  29  ASP A  35 -1  N  ASP A  35   O  GLU A  40           
SHEET    3 AA1 8 GLY A  20  PHE A  26 -1  N  PHE A  24   O  MET A  31           
SHEET    4 AA1 8 HIS A   5  GLN A  14 -1  N  THR A   8   O  GLU A  25           
SHEET    5 AA1 8 LEU B   8  PHE B  18 -1  O  CYS B  15   N  SER A   7           
SHEET    6 AA1 8 THR B  21  TYR B  30 -1  O  LEU B  25   N  GLU B  14           
SHEET    7 AA1 8 GLU B  33  ASP B  39 -1  O  GLU B  33   N  TYR B  30           
SHEET    8 AA1 8 PHE B  45  ALA B  47 -1  O  ARG B  46   N  ARG B  37           
SHEET    1 AA2 4 GLU A  88  PRO A  93  0                                        
SHEET    2 AA2 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3 AA2 4 PHE A 145  PHE A 153 -1  O  HIS A 149   N  CYS A 107           
SHEET    4 AA2 4 VAL A 132  GLU A 134 -1  N  ALA A 133   O  TYR A 150           
SHEET    1 AA3 4 GLU A  88  PRO A  93  0                                        
SHEET    2 AA3 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3 AA3 4 PHE A 145  PHE A 153 -1  O  HIS A 149   N  CYS A 107           
SHEET    4 AA3 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  HIS A 146           
SHEET    1 AA4 4 GLU A 126  VAL A 128  0                                        
SHEET    2 AA4 4 ASN A 118  CYS A 123 -1  N  CYS A 123   O  GLU A 126           
SHEET    3 AA4 4 PHE A 160  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4 AA4 4 LEU A 174  GLU A 179 -1  O  LEU A 174   N  VAL A 165           
SHEET    1 AA5 4 ARG B  96  PRO B 101  0                                        
SHEET    2 AA5 4 LEU B 112  PHE B 120 -1  O  HIS B 116   N  ASN B  98           
SHEET    3 AA5 4 PHE B 153  GLU B 160 -1  O  VAL B 157   N  CYS B 115           
SHEET    4 AA5 4 VAL B 140  SER B 142 -1  N  VAL B 141   O  MET B 158           
SHEET    1 AA6 4 ARG B  96  PRO B 101  0                                        
SHEET    2 AA6 4 LEU B 112  PHE B 120 -1  O  HIS B 116   N  ASN B  98           
SHEET    3 AA6 4 PHE B 153  GLU B 160 -1  O  VAL B 157   N  CYS B 115           
SHEET    4 AA6 4 ILE B 146  ARG B 147 -1  N  ILE B 146   O  GLN B 154           
SHEET    1 AA7 4 GLN B 134  GLU B 136  0                                        
SHEET    2 AA7 4 GLN B 126  LEU B 131 -1  N  TRP B 129   O  GLU B 136           
SHEET    3 AA7 4 VAL B 168  GLU B 174 -1  O  GLN B 172   N  ARG B 128           
SHEET    4 AA7 4 VAL B 182  LYS B 187 -1  O  TRP B 186   N  TYR B 169           
SHEET    1 AA8 8 GLU C  40  TRP C  43  0                                        
SHEET    2 AA8 8 ASP C  29  ASP C  35 -1  N  TYR C  33   O  VAL C  42           
SHEET    3 AA8 8 GLY C  20  PHE C  26 -1  N  PHE C  24   O  PHE C  32           
SHEET    4 AA8 8 HIS C   5  GLN C  14 -1  N  THR C   8   O  GLU C  25           
SHEET    5 AA8 8 LEU D   8  PHE D  18 -1  O  CYS D  15   N  SER C   7           
SHEET    6 AA8 8 THR D  21  TYR D  30 -1  O  LEU D  25   N  GLU D  14           
SHEET    7 AA8 8 GLU D  33  ASP D  39 -1  O  GLU D  33   N  TYR D  30           
SHEET    8 AA8 8 PHE D  45  ALA D  47 -1  O  ARG D  46   N  ARG D  37           
SHEET    1 AA9 4 GLU C  88  PRO C  93  0                                        
SHEET    2 AA9 4 ASN C 103  PHE C 112 -1  O  HIS C 108   N  THR C  90           
SHEET    3 AA9 4 PHE C 145  PHE C 153 -1  O  HIS C 149   N  CYS C 107           
SHEET    4 AA9 4 VAL C 132  GLU C 134 -1  N  ALA C 133   O  TYR C 150           
SHEET    1 AB1 4 GLU C  88  PRO C  93  0                                        
SHEET    2 AB1 4 ASN C 103  PHE C 112 -1  O  HIS C 108   N  THR C  90           
SHEET    3 AB1 4 PHE C 145  PHE C 153 -1  O  HIS C 149   N  CYS C 107           
SHEET    4 AB1 4 LEU C 138  PRO C 139 -1  N  LEU C 138   O  HIS C 146           
SHEET    1 AB2 4 GLU C 126  VAL C 128  0                                        
SHEET    2 AB2 4 ASN C 118  CYS C 123 -1  N  TRP C 121   O  VAL C 128           
SHEET    3 AB2 4 PHE C 160  GLU C 166 -1  O  ARG C 164   N  THR C 120           
SHEET    4 AB2 4 LEU C 174  GLU C 179 -1  O  TRP C 178   N  TYR C 161           
SHEET    1 AB3 4 ARG D  96  PRO D 101  0                                        
SHEET    2 AB3 4 LEU D 112  PHE D 120 -1  O  HIS D 116   N  ASN D  98           
SHEET    3 AB3 4 PHE D 153  GLU D 160 -1  O  ILE D 155   N  VAL D 117           
SHEET    4 AB3 4 VAL D 140  SER D 142 -1  N  VAL D 141   O  MET D 158           
SHEET    1 AB4 4 ARG D  96  PRO D 101  0                                        
SHEET    2 AB4 4 LEU D 112  PHE D 120 -1  O  HIS D 116   N  ASN D  98           
SHEET    3 AB4 4 PHE D 153  GLU D 160 -1  O  ILE D 155   N  VAL D 117           
SHEET    4 AB4 4 ILE D 146  ARG D 147 -1  N  ILE D 146   O  GLN D 154           
SHEET    1 AB5 4 GLN D 134  GLU D 136  0                                        
SHEET    2 AB5 4 GLN D 126  LEU D 131 -1  N  TRP D 129   O  GLU D 136           
SHEET    3 AB5 4 VAL D 168  GLU D 174 -1  O  GLN D 172   N  ARG D 128           
SHEET    4 AB5 4 VAL D 182  LYS D 187 -1  O  VAL D 182   N  VAL D 173           
SHEET    1 AB6 8 GLU E  40  TRP E  43  0                                        
SHEET    2 AB6 8 ASP E  29  ASP E  35 -1  N  TYR E  33   O  VAL E  42           
SHEET    3 AB6 8 GLY E  20  PHE E  26 -1  N  PHE E  24   O  MET E  31           
SHEET    4 AB6 8 HIS E   5  GLN E  14 -1  N  THR E   8   O  GLU E  25           
SHEET    5 AB6 8 LEU F   8  PHE F  18 -1  O  CYS F  15   N  SER E   7           
SHEET    6 AB6 8 THR F  21  TYR F  30 -1  O  LEU F  25   N  GLU F  14           
SHEET    7 AB6 8 GLU F  33  ASP F  39 -1  O  GLU F  33   N  TYR F  30           
SHEET    8 AB6 8 PHE F  45  ALA F  47 -1  O  ARG F  46   N  ARG F  37           
SHEET    1 AB7 4 GLU E  88  PRO E  93  0                                        
SHEET    2 AB7 4 ASN E 103  PHE E 112 -1  O  HIS E 108   N  THR E  90           
SHEET    3 AB7 4 PHE E 145  PHE E 153 -1  O  LYS E 147   N  ILE E 109           
SHEET    4 AB7 4 VAL E 132  GLU E 134 -1  N  ALA E 133   O  TYR E 150           
SHEET    1 AB8 4 GLU E  88  PRO E  93  0                                        
SHEET    2 AB8 4 ASN E 103  PHE E 112 -1  O  HIS E 108   N  THR E  90           
SHEET    3 AB8 4 PHE E 145  PHE E 153 -1  O  LYS E 147   N  ILE E 109           
SHEET    4 AB8 4 LEU E 138  PRO E 139 -1  N  LEU E 138   O  HIS E 146           
SHEET    1 AB9 4 GLU E 126  VAL E 128  0                                        
SHEET    2 AB9 4 ASN E 118  CYS E 123 -1  N  CYS E 123   O  GLU E 126           
SHEET    3 AB9 4 PHE E 160  GLU E 166 -1  O  GLU E 166   N  ASN E 118           
SHEET    4 AB9 4 LEU E 174  GLU E 179 -1  O  TRP E 178   N  TYR E 161           
SHEET    1 AC1 4 ARG F  96  PRO F 101  0                                        
SHEET    2 AC1 4 LEU F 112  PHE F 120 -1  O  HIS F 116   N  ASN F  98           
SHEET    3 AC1 4 PHE F 153  GLU F 160 -1  O  VAL F 157   N  CYS F 115           
SHEET    4 AC1 4 VAL F 140  SER F 142 -1  N  VAL F 141   O  MET F 158           
SHEET    1 AC2 4 ARG F  96  PRO F 101  0                                        
SHEET    2 AC2 4 LEU F 112  PHE F 120 -1  O  HIS F 116   N  ASN F  98           
SHEET    3 AC2 4 PHE F 153  GLU F 160 -1  O  VAL F 157   N  CYS F 115           
SHEET    4 AC2 4 ILE F 146  ARG F 147 -1  N  ILE F 146   O  GLN F 154           
SHEET    1 AC3 4 GLN F 134  GLU F 136  0                                        
SHEET    2 AC3 4 GLN F 126  LEU F 131 -1  N  LEU F 131   O  GLN F 134           
SHEET    3 AC3 4 VAL F 168  GLU F 174 -1  O  GLN F 172   N  ARG F 128           
SHEET    4 AC3 4 VAL F 182  LYS F 187 -1  O  VAL F 182   N  VAL F 173           
SHEET    1 AC4 8 GLU G  40  TRP G  43  0                                        
SHEET    2 AC4 8 ASP G  29  ASP G  35 -1  N  TYR G  33   O  VAL G  42           
SHEET    3 AC4 8 GLY G  20  PHE G  26 -1  N  PHE G  24   O  MET G  31           
SHEET    4 AC4 8 HIS G   5  GLN G  14 -1  N  THR G   8   O  GLU G  25           
SHEET    5 AC4 8 LEU H   8  PHE H  18 -1  O  CYS H  15   N  SER G   7           
SHEET    6 AC4 8 THR H  21  TYR H  30 -1  O  LEU H  25   N  GLU H  14           
SHEET    7 AC4 8 GLU H  33  ASP H  39 -1  O  GLU H  33   N  TYR H  30           
SHEET    8 AC4 8 PHE H  45  ALA H  47 -1  O  ARG H  46   N  ARG H  37           
SHEET    1 AC5 4 GLU G  88  PRO G  93  0                                        
SHEET    2 AC5 4 ASN G 103  PHE G 112 -1  O  ASP G 110   N  GLU G  88           
SHEET    3 AC5 4 PHE G 145  PHE G 153 -1  O  LEU G 151   N  LEU G 105           
SHEET    4 AC5 4 VAL G 132  GLU G 134 -1  N  ALA G 133   O  TYR G 150           
SHEET    1 AC6 4 GLU G  88  PRO G  93  0                                        
SHEET    2 AC6 4 ASN G 103  PHE G 112 -1  O  ASP G 110   N  GLU G  88           
SHEET    3 AC6 4 PHE G 145  PHE G 153 -1  O  LEU G 151   N  LEU G 105           
SHEET    4 AC6 4 LEU G 138  PRO G 139 -1  N  LEU G 138   O  HIS G 146           
SHEET    1 AC7 4 GLU G 126  LEU G 127  0                                        
SHEET    2 AC7 4 ASN G 118  CYS G 123 -1  N  CYS G 123   O  GLU G 126           
SHEET    3 AC7 4 PHE G 160  GLU G 166 -1  O  GLU G 166   N  ASN G 118           
SHEET    4 AC7 4 LEU G 174  GLU G 179 -1  O  LEU G 174   N  VAL G 165           
SHEET    1 AC8 4 ARG H  96  PRO H 101  0                                        
SHEET    2 AC8 4 LEU H 112  PHE H 120 -1  O  HIS H 116   N  ASN H  98           
SHEET    3 AC8 4 PHE H 153  GLU H 160 -1  O  VAL H 157   N  CYS H 115           
SHEET    4 AC8 4 VAL H 140  SER H 142 -1  N  VAL H 141   O  MET H 158           
SHEET    1 AC9 4 ARG H  96  PRO H 101  0                                        
SHEET    2 AC9 4 LEU H 112  PHE H 120 -1  O  HIS H 116   N  ASN H  98           
SHEET    3 AC9 4 PHE H 153  GLU H 160 -1  O  VAL H 157   N  CYS H 115           
SHEET    4 AC9 4 ILE H 146  ARG H 147 -1  N  ILE H 146   O  GLN H 154           
SHEET    1 AD1 4 GLN H 134  GLU H 136  0                                        
SHEET    2 AD1 4 GLN H 126  LEU H 131 -1  N  TRP H 129   O  GLU H 136           
SHEET    3 AD1 4 VAL H 168  GLU H 174 -1  O  GLN H 172   N  ARG H 128           
SHEET    4 AD1 4 VAL H 182  LYS H 187 -1  O  TRP H 186   N  TYR H 169           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.13  
SSBOND   2 CYS B   15    CYS B   77                          1555   1555  2.15  
SSBOND   3 CYS B  115    CYS B  171                          1555   1555  2.00  
SSBOND   4 CYS C  107    CYS C  163                          1555   1555  2.10  
SSBOND   5 CYS D   15    CYS D   77                          1555   1555  2.15  
SSBOND   6 CYS D  115    CYS D  171                          1555   1555  2.15  
SSBOND   7 CYS E  107    CYS E  163                          1555   1555  2.15  
SSBOND   8 CYS F   15    CYS F   77                          1555   1555  2.12  
SSBOND   9 CYS F  115    CYS F  171                          1555   1555  2.06  
SSBOND  10 CYS G  107    CYS G  163                          1555   1555  2.20  
SSBOND  11 CYS H   15    CYS H   77                          1555   1555  2.11  
SSBOND  12 CYS H  115    CYS H  171                          1555   1555  2.04  
LINK         ND2 ASN A 118                 C1  NAG I   1     1555   1555  1.47  
LINK         ND2 ASN B  19                 C1  NAG J   1     1555   1555  1.43  
LINK         ND2 ASN C 118                 C1  NAG K   1     1555   1555  1.44  
LINK         ND2 ASN D  19                 C1  NAG L   1     1555   1555  1.45  
LINK         ND2 ASN E 118                 C1  NAG E 201     1555   1555  1.46  
LINK         ND2 ASN F  19                 C1  NAG M   1     1555   1555  1.45  
LINK         ND2 ASN G 118                 C1  NAG N   1     1555   1555  1.46  
LINK         ND2 ASN H  19                 C1  NAG O   1     1555   1555  1.43  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.46  
LINK         O3  NAG J   1                 C1  NAG J   2     1555   1555  1.44  
LINK         O4  NAG J   1                 C1  NAG J   3     1555   1555  1.47  
LINK         O6  NAG J   1                 C1  NAG J   4     1555   1555  1.45  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.47  
LINK         O3  NAG L   1                 C1  NAG L   2     1555   1555  1.44  
LINK         O4  NAG L   1                 C1  NAG L   3     1555   1555  1.47  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.43  
LINK         O3  NAG M   1                 C1  BMA M   4     1555   1555  1.45  
LINK         O4  NAG M   2                 C1  NAG M   3     1555   1555  1.46  
LINK         O4  NAG N   1                 C1  NAG N   2     1555   1555  1.44  
LINK         O3  NAG O   1                 C1  BMA O   2     1555   1555  1.36  
LINK         O4  NAG O   1                 C1  NAG O   3     1555   1555  1.45  
LINK        NA    NA A 201                 O   HOH A 313     1555   1555  3.08  
LINK        NA    NA A 201                 O   HOH A 326     1555   1555  2.60  
LINK         OE2AGLU C  98                NA    NA C 201     1555   1555  3.13  
LINK        NA    NA C 201                 O   HOH C 352     1555   1555  2.78  
LINK        NA    NA C 201                 O   HOH C 474     1555   1555  3.04  
LINK        NA    NA C 201                 OE2 GLU H 135     1555   1555  2.79  
CISPEP   1 ARG A   17    PRO A   18          0        -2.98                     
CISPEP   2 PHE A  113    PRO A  114          0         6.29                     
CISPEP   3 TYR B  121    PRO B  122          0         0.31                     
CISPEP   4 ARG C   17    PRO C   18          0         6.14                     
CISPEP   5 PHE C  113    PRO C  114          0         3.81                     
CISPEP   6 TYR D  121    PRO D  122          0         2.82                     
CISPEP   7 ARG E   17    PRO E   18          0        -5.40                     
CISPEP   8 PHE E  113    PRO E  114          0         1.17                     
CISPEP   9 TYR F  121    PRO F  122          0        -2.51                     
CISPEP  10 ARG G   17    PRO G   18          0         1.36                     
CISPEP  11 PHE G  113    PRO G  114          0         6.15                     
CISPEP  12 TYR H  121    PRO H  122          0        -3.46                     
CRYST1   81.631  130.468  107.994  90.00 107.16  90.00 P 1 21 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      0.012250  0.000000  0.003782        0.00000                         
SCALE2      0.000000  0.007665  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009691        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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