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Database: PDB
Entry: 6I7S
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Original site: 6I7S 
HEADER    LIPID TRANSPORT                         17-NOV-18   6I7S              
TITLE     MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PDI,CELLULAR THYROID HORMONE-BINDING PROTEIN,PROLYL 4-      
COMPND   5 HYDROXYLASE SUBUNIT BETA,P55;                                        
COMPND   6 EC: 5.3.4.1;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN LARGE SUBUNIT;    
COMPND  10 CHAIN: G, H;                                                         
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: P4HB, ERBA2L, PDI, PDIA1, PO4DB;                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: MTTP, MTP;                                                     
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 83333                                       
KEYWDS    LIPID TRANSFER, PROTEIN COMPLEX, PROTEIN DISULFIDE ISOMERASE, LIPID   
KEYWDS   2 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.BITEROVA,M.N.ISUPOV,R.M.KEEGAN,A.A.LEBEDEV,L.W.RUDDOCK              
REVDAT   2   04-SEP-19 6I7S    1       JRNL                                     
REVDAT   1   21-AUG-19 6I7S    0                                                
JRNL        AUTH   E.I.BITEROVA,M.N.ISUPOV,R.M.KEEGAN,A.A.LEBEDEV,A.A.SOHAIL,   
JRNL        AUTH 2 I.LIAQAT,H.I.ALANEN,L.W.RUDDOCK                              
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN MICROSOMAL TRIGLYCERIDE       
JRNL        TITL 2 TRANSFER PROTEIN.                                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 17251 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31395737                                                     
JRNL        DOI    10.1073/PNAS.1903029116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 102860                         
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5414                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7180                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 378                          
REMARK   3   BIN FREE R VALUE                    : 0.4420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20821                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 342                                     
REMARK   3   SOLVENT ATOMS            : 222                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.51000                                              
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : -1.86000                                             
REMARK   3    B12 (A**2) : 0.63000                                              
REMARK   3    B13 (A**2) : -2.06000                                             
REMARK   3    B23 (A**2) : -1.77000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.596         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.305         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21585 ; 0.006 ; 0.012       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 29000 ; 1.356 ; 1.635       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2656 ; 7.214 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1065 ;37.377 ;23.390       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3926 ;20.137 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   106 ;20.184 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2798 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15933 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 2                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    20    478       B    20    478   14142 0.100 0.050     
REMARK   3    2     G    21    884       H    21    884   26114 0.100 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: U VALUES : REFINED INDIVIDUALLY           
REMARK   4                                                                      
REMARK   4 6I7S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012952.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.966                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108279                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 1.694                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.72                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.20200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.630                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1LSH, 4EKZ                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.25, 0.2 M LI2SO4, 32%    
REMARK 280  V/V PEG 400, 2% POLYPROPYLENE GLYCOL P425, PH 7.5, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 10250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 11120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H                                  
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     MET A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     ASP A   480                                                      
REMARK 465     ASP A   481                                                      
REMARK 465     ASP A   482                                                      
REMARK 465     ASP A   483                                                      
REMARK 465     LEU A   484                                                      
REMARK 465     GLU A   485                                                      
REMARK 465     ASP A   486                                                      
REMARK 465     LEU A   487                                                      
REMARK 465     GLU A   488                                                      
REMARK 465     GLU A   489                                                      
REMARK 465     ALA A   490                                                      
REMARK 465     GLU A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     PRO A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     MET A   495                                                      
REMARK 465     GLU A   496                                                      
REMARK 465     GLU A   497                                                      
REMARK 465     ASP A   498                                                      
REMARK 465     ASP A   499                                                      
REMARK 465     ASP A   500                                                      
REMARK 465     GLN A   501                                                      
REMARK 465     LYS A   502                                                      
REMARK 465     ALA A   503                                                      
REMARK 465     VAL A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     ASP A   506                                                      
REMARK 465     GLU A   507                                                      
REMARK 465     LEU A   508                                                      
REMARK 465     MET B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ASP B   482                                                      
REMARK 465     ASP B   483                                                      
REMARK 465     LEU B   484                                                      
REMARK 465     GLU B   485                                                      
REMARK 465     ASP B   486                                                      
REMARK 465     LEU B   487                                                      
REMARK 465     GLU B   488                                                      
REMARK 465     GLU B   489                                                      
REMARK 465     ALA B   490                                                      
REMARK 465     GLU B   491                                                      
REMARK 465     GLU B   492                                                      
REMARK 465     PRO B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     MET B   495                                                      
REMARK 465     GLU B   496                                                      
REMARK 465     GLU B   497                                                      
REMARK 465     ASP B   498                                                      
REMARK 465     ASP B   499                                                      
REMARK 465     ASP B   500                                                      
REMARK 465     GLN B   501                                                      
REMARK 465     LYS B   502                                                      
REMARK 465     ALA B   503                                                      
REMARK 465     VAL B   504                                                      
REMARK 465     LYS B   505                                                      
REMARK 465     ASP B   506                                                      
REMARK 465     GLU B   507                                                      
REMARK 465     LEU B   508                                                      
REMARK 465     MET G    11                                                      
REMARK 465     HIS G    12                                                      
REMARK 465     HIS G    13                                                      
REMARK 465     HIS G    14                                                      
REMARK 465     HIS G    15                                                      
REMARK 465     HIS G    16                                                      
REMARK 465     HIS G    17                                                      
REMARK 465     MET G    18                                                      
REMARK 465     VAL G    19                                                      
REMARK 465     LEU G   718                                                      
REMARK 465     SER G   719                                                      
REMARK 465     ALA G   720                                                      
REMARK 465     PRO G   886                                                      
REMARK 465     ASP G   887                                                      
REMARK 465     SER G   888                                                      
REMARK 465     THR G   889                                                      
REMARK 465     SER G   890                                                      
REMARK 465     SER G   891                                                      
REMARK 465     GLY G   892                                                      
REMARK 465     TRP G   893                                                      
REMARK 465     PHE G   894                                                      
REMARK 465     MET H    11                                                      
REMARK 465     HIS H    12                                                      
REMARK 465     HIS H    13                                                      
REMARK 465     HIS H    14                                                      
REMARK 465     HIS H    15                                                      
REMARK 465     HIS H    16                                                      
REMARK 465     HIS H    17                                                      
REMARK 465     MET H    18                                                      
REMARK 465     VAL H    19                                                      
REMARK 465     LYS H    20                                                      
REMARK 465     LEU H   718                                                      
REMARK 465     SER H   719                                                      
REMARK 465     ALA H   720                                                      
REMARK 465     SER H   721                                                      
REMARK 465     ASP H   887                                                      
REMARK 465     SER H   888                                                      
REMARK 465     THR H   889                                                      
REMARK 465     SER H   890                                                      
REMARK 465     SER H   891                                                      
REMARK 465     GLY H   892                                                      
REMARK 465     TRP H   893                                                      
REMARK 465     PHE H   894                                                      
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    GLN G   569     O    HOH G  1001              1.99            
REMARK 500   CE   MET G   717     CB   SER G   721              2.12            
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    GLU A  22       64.10   -113.45                                   
REMARK 500    GLU A  23       88.64    -53.22                                   
REMARK 500    GLU A  73      -18.15   -159.17                                   
REMARK 500    SER A  75      -90.48   -127.17                                   
REMARK 500    GLU A  87       69.66   -101.80                                   
REMARK 500    ARG A  97      -75.91    -94.42                                   
REMARK 500    SER A 112      113.86   -163.90                                   
REMARK 500    ALA A 118     -155.79    -78.77                                   
REMARK 500    SER A 166      163.16    -40.82                                   
REMARK 500    GLN A 197       41.57     70.49                                   
REMARK 500    ASP A 210     -120.73     64.01                                   
REMARK 500    ASP A 267       49.39     72.79                                   
REMARK 500    GLU A 321     -155.81   -128.43                                   
REMARK 500    ASN A 419      -19.16   -143.29                                   
REMARK 500    ALA A 478       90.19   -173.08                                   
REMARK 500    GLU B  22       62.50   -114.05                                   
REMARK 500    GLU B  23       89.28    -53.55                                   
REMARK 500    ASP B  24       34.11     70.50                                   
REMARK 500    GLU B  87       69.61   -100.88                                   
REMARK 500    ARG B  97      -83.42    -92.09                                   
REMARK 500    ALA B 118     -155.34    -77.83                                   
REMARK 500    SER B 166      163.63    -41.44                                   
REMARK 500    ASP B 210     -120.05     63.25                                   
REMARK 500    ASP B 267       50.13     71.94                                   
REMARK 500    GLU B 321     -153.58   -127.64                                   
REMARK 500    ASN B 419      -18.85   -143.10                                   
REMARK 500    ALA B 478      179.80    178.14                                   
REMARK 500    HIS G  22      -28.75   -140.35                                   
REMARK 500    GLN G  52     -100.27   -108.90                                   
REMARK 500    ASP G  76       79.10    -62.66                                   
REMARK 500    HIS G 181     -162.09   -112.60                                   
REMARK 500    SER G 225       -8.87     82.72                                   
REMARK 500    ASP G 281      130.79   -170.59                                   
REMARK 500    HIS G 297       79.34     60.10                                   
REMARK 500    GLU G 443       15.50     55.10                                   
REMARK 500    LYS G 463       91.09    -67.86                                   
REMARK 500    GLU G 465     -139.27    -96.73                                   
REMARK 500    PHE G 707      147.48   -176.51                                   
REMARK 500    VAL G 727      -52.67   -127.61                                   
REMARK 500    SER G 795      -37.92     83.44                                   
REMARK 500    PHE G 824      136.57     77.04                                   
REMARK 500    SER G 848      -22.99     83.73                                   
REMARK 500    LEU G 870     -158.79   -108.71                                   
REMARK 500    ASP H  76       81.77    -64.27                                   
REMARK 500    HIS H 181     -162.42   -112.39                                   
REMARK 500    LYS H 271      -21.40     82.45                                   
REMARK 500    ASP H 281      133.34   -170.88                                   
REMARK 500    HIS H 297       78.51     60.37                                   
REMARK 500    GLU H 443       16.53     53.82                                   
REMARK 500    GLU H 462       42.04   -105.16                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 RAMACHANDRAN OUTLIERS.                        
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                              CA A 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 381   O                                                      
REMARK 620 2 ASP A 383   O    98.0                                              
REMARK 620 3 LYS A 386   O   131.3  75.9                                        
REMARK 620 4 PHE A 446   O    98.0 158.5  82.7                                  
REMARK 620 5 PRO A 447   O   138.7 108.6  86.5  67.0                            
REMARK 620 6 HOH A 713   O    74.5  78.3 145.5 120.0  80.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 381   O                                                      
REMARK 620 2 ASP B 383   O   101.6                                              
REMARK 620 3 LYS B 386   O   129.8  75.7                                        
REMARK 620 4 PHE B 446   O    94.3 156.1  80.5                                  
REMARK 620 5 PRO B 447   O   136.9 111.1  86.3  65.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE5 G 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE G 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS G 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 909                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 910                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 914                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 915                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 916                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG G 918                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE5 H 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE4 H 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE H 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE H 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE H 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 909                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 910                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG H 914                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG H 915                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG H 916                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG H 917                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG H 918                 
DBREF  6I7S A   18   508  UNP    P07237   PDIA1_HUMAN     18    508             
DBREF  6I7S B   18   508  UNP    P07237   PDIA1_HUMAN     18    508             
DBREF  6I7S G   19   894  UNP    P55157   MTP_HUMAN       19    894             
DBREF  6I7S H   19   894  UNP    P55157   MTP_HUMAN       19    894             
SEQADV 6I7S MET A   17  UNP  P07237              INITIATING METHIONINE          
SEQADV 6I7S MET B   17  UNP  P07237              INITIATING METHIONINE          
SEQADV 6I7S MET G   11  UNP  P55157              INITIATING METHIONINE          
SEQADV 6I7S HIS G   12  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS G   13  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS G   14  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS G   15  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS G   16  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS G   17  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S MET G   18  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S MET H   11  UNP  P55157              INITIATING METHIONINE          
SEQADV 6I7S HIS H   12  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS H   13  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS H   14  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS H   15  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS H   16  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S HIS H   17  UNP  P55157              EXPRESSION TAG                 
SEQADV 6I7S MET H   18  UNP  P55157              EXPRESSION TAG                 
SEQRES   1 A  492  MET ASP ALA PRO GLU GLU GLU ASP HIS VAL LEU VAL LEU          
SEQRES   2 A  492  ARG LYS SER ASN PHE ALA GLU ALA LEU ALA ALA HIS LYS          
SEQRES   3 A  492  TYR LEU LEU VAL GLU PHE TYR ALA PRO TRP CYS GLY HIS          
SEQRES   4 A  492  CYS LYS ALA LEU ALA PRO GLU TYR ALA LYS ALA ALA GLY          
SEQRES   5 A  492  LYS LEU LYS ALA GLU GLY SER GLU ILE ARG LEU ALA LYS          
SEQRES   6 A  492  VAL ASP ALA THR GLU GLU SER ASP LEU ALA GLN GLN TYR          
SEQRES   7 A  492  GLY VAL ARG GLY TYR PRO THR ILE LYS PHE PHE ARG ASN          
SEQRES   8 A  492  GLY ASP THR ALA SER PRO LYS GLU TYR THR ALA GLY ARG          
SEQRES   9 A  492  GLU ALA ASP ASP ILE VAL ASN TRP LEU LYS LYS ARG THR          
SEQRES  10 A  492  GLY PRO ALA ALA THR THR LEU PRO ASP GLY ALA ALA ALA          
SEQRES  11 A  492  GLU SER LEU VAL GLU SER SER GLU VAL ALA VAL ILE GLY          
SEQRES  12 A  492  PHE PHE LYS ASP VAL GLU SER ASP SER ALA LYS GLN PHE          
SEQRES  13 A  492  LEU GLN ALA ALA GLU ALA ILE ASP ASP ILE PRO PHE GLY          
SEQRES  14 A  492  ILE THR SER ASN SER ASP VAL PHE SER LYS TYR GLN LEU          
SEQRES  15 A  492  ASP LYS ASP GLY VAL VAL LEU PHE LYS LYS PHE ASP GLU          
SEQRES  16 A  492  GLY ARG ASN ASN PHE GLU GLY GLU VAL THR LYS GLU ASN          
SEQRES  17 A  492  LEU LEU ASP PHE ILE LYS HIS ASN GLN LEU PRO LEU VAL          
SEQRES  18 A  492  ILE GLU PHE THR GLU GLN THR ALA PRO LYS ILE PHE GLY          
SEQRES  19 A  492  GLY GLU ILE LYS THR HIS ILE LEU LEU PHE LEU PRO LYS          
SEQRES  20 A  492  SER VAL SER ASP TYR ASP GLY LYS LEU SER ASN PHE LYS          
SEQRES  21 A  492  THR ALA ALA GLU SER PHE LYS GLY LYS ILE LEU PHE ILE          
SEQRES  22 A  492  PHE ILE ASP SER ASP HIS THR ASP ASN GLN ARG ILE LEU          
SEQRES  23 A  492  GLU PHE PHE GLY LEU LYS LYS GLU GLU CYS PRO ALA VAL          
SEQRES  24 A  492  ARG LEU ILE THR LEU GLU GLU GLU MET THR LYS TYR LYS          
SEQRES  25 A  492  PRO GLU SER GLU GLU LEU THR ALA GLU ARG ILE THR GLU          
SEQRES  26 A  492  PHE CYS HIS ARG PHE LEU GLU GLY LYS ILE LYS PRO HIS          
SEQRES  27 A  492  LEU MET SER GLN GLU LEU PRO GLU ASP TRP ASP LYS GLN          
SEQRES  28 A  492  PRO VAL LYS VAL LEU VAL GLY LYS ASN PHE GLU ASP VAL          
SEQRES  29 A  492  ALA PHE ASP GLU LYS LYS ASN VAL PHE VAL GLU PHE TYR          
SEQRES  30 A  492  ALA PRO TRP CYS GLY HIS CYS LYS GLN LEU ALA PRO ILE          
SEQRES  31 A  492  TRP ASP LYS LEU GLY GLU THR TYR LYS ASP HIS GLU ASN          
SEQRES  32 A  492  ILE VAL ILE ALA LYS MET ASP SER THR ALA ASN GLU VAL          
SEQRES  33 A  492  GLU ALA VAL LYS VAL HIS SER PHE PRO THR LEU LYS PHE          
SEQRES  34 A  492  PHE PRO ALA SER ALA ASP ARG THR VAL ILE ASP TYR ASN          
SEQRES  35 A  492  GLY GLU ARG THR LEU ASP GLY PHE LYS LYS PHE LEU GLU          
SEQRES  36 A  492  SER GLY GLY GLN ASP GLY ALA GLY ASP ASP ASP ASP LEU          
SEQRES  37 A  492  GLU ASP LEU GLU GLU ALA GLU GLU PRO ASP MET GLU GLU          
SEQRES  38 A  492  ASP ASP ASP GLN LYS ALA VAL LYS ASP GLU LEU                  
SEQRES   1 B  492  MET ASP ALA PRO GLU GLU GLU ASP HIS VAL LEU VAL LEU          
SEQRES   2 B  492  ARG LYS SER ASN PHE ALA GLU ALA LEU ALA ALA HIS LYS          
SEQRES   3 B  492  TYR LEU LEU VAL GLU PHE TYR ALA PRO TRP CYS GLY HIS          
SEQRES   4 B  492  CYS LYS ALA LEU ALA PRO GLU TYR ALA LYS ALA ALA GLY          
SEQRES   5 B  492  LYS LEU LYS ALA GLU GLY SER GLU ILE ARG LEU ALA LYS          
SEQRES   6 B  492  VAL ASP ALA THR GLU GLU SER ASP LEU ALA GLN GLN TYR          
SEQRES   7 B  492  GLY VAL ARG GLY TYR PRO THR ILE LYS PHE PHE ARG ASN          
SEQRES   8 B  492  GLY ASP THR ALA SER PRO LYS GLU TYR THR ALA GLY ARG          
SEQRES   9 B  492  GLU ALA ASP ASP ILE VAL ASN TRP LEU LYS LYS ARG THR          
SEQRES  10 B  492  GLY PRO ALA ALA THR THR LEU PRO ASP GLY ALA ALA ALA          
SEQRES  11 B  492  GLU SER LEU VAL GLU SER SER GLU VAL ALA VAL ILE GLY          
SEQRES  12 B  492  PHE PHE LYS ASP VAL GLU SER ASP SER ALA LYS GLN PHE          
SEQRES  13 B  492  LEU GLN ALA ALA GLU ALA ILE ASP ASP ILE PRO PHE GLY          
SEQRES  14 B  492  ILE THR SER ASN SER ASP VAL PHE SER LYS TYR GLN LEU          
SEQRES  15 B  492  ASP LYS ASP GLY VAL VAL LEU PHE LYS LYS PHE ASP GLU          
SEQRES  16 B  492  GLY ARG ASN ASN PHE GLU GLY GLU VAL THR LYS GLU ASN          
SEQRES  17 B  492  LEU LEU ASP PHE ILE LYS HIS ASN GLN LEU PRO LEU VAL          
SEQRES  18 B  492  ILE GLU PHE THR GLU GLN THR ALA PRO LYS ILE PHE GLY          
SEQRES  19 B  492  GLY GLU ILE LYS THR HIS ILE LEU LEU PHE LEU PRO LYS          
SEQRES  20 B  492  SER VAL SER ASP TYR ASP GLY LYS LEU SER ASN PHE LYS          
SEQRES  21 B  492  THR ALA ALA GLU SER PHE LYS GLY LYS ILE LEU PHE ILE          
SEQRES  22 B  492  PHE ILE ASP SER ASP HIS THR ASP ASN GLN ARG ILE LEU          
SEQRES  23 B  492  GLU PHE PHE GLY LEU LYS LYS GLU GLU CYS PRO ALA VAL          
SEQRES  24 B  492  ARG LEU ILE THR LEU GLU GLU GLU MET THR LYS TYR LYS          
SEQRES  25 B  492  PRO GLU SER GLU GLU LEU THR ALA GLU ARG ILE THR GLU          
SEQRES  26 B  492  PHE CYS HIS ARG PHE LEU GLU GLY LYS ILE LYS PRO HIS          
SEQRES  27 B  492  LEU MET SER GLN GLU LEU PRO GLU ASP TRP ASP LYS GLN          
SEQRES  28 B  492  PRO VAL LYS VAL LEU VAL GLY LYS ASN PHE GLU ASP VAL          
SEQRES  29 B  492  ALA PHE ASP GLU LYS LYS ASN VAL PHE VAL GLU PHE TYR          
SEQRES  30 B  492  ALA PRO TRP CYS GLY HIS CYS LYS GLN LEU ALA PRO ILE          
SEQRES  31 B  492  TRP ASP LYS LEU GLY GLU THR TYR LYS ASP HIS GLU ASN          
SEQRES  32 B  492  ILE VAL ILE ALA LYS MET ASP SER THR ALA ASN GLU VAL          
SEQRES  33 B  492  GLU ALA VAL LYS VAL HIS SER PHE PRO THR LEU LYS PHE          
SEQRES  34 B  492  PHE PRO ALA SER ALA ASP ARG THR VAL ILE ASP TYR ASN          
SEQRES  35 B  492  GLY GLU ARG THR LEU ASP GLY PHE LYS LYS PHE LEU GLU          
SEQRES  36 B  492  SER GLY GLY GLN ASP GLY ALA GLY ASP ASP ASP ASP LEU          
SEQRES  37 B  492  GLU ASP LEU GLU GLU ALA GLU GLU PRO ASP MET GLU GLU          
SEQRES  38 B  492  ASP ASP ASP GLN LYS ALA VAL LYS ASP GLU LEU                  
SEQRES   1 G  884  MET HIS HIS HIS HIS HIS HIS MET VAL LYS GLY HIS THR          
SEQRES   2 G  884  THR GLY LEU SER LEU ASN ASN ASP ARG LEU TYR LYS LEU          
SEQRES   3 G  884  THR TYR SER THR GLU VAL LEU LEU ASP ARG GLY LYS GLY          
SEQRES   4 G  884  LYS LEU GLN ASP SER VAL GLY TYR ARG ILE SER SER ASN          
SEQRES   5 G  884  VAL ASP VAL ALA LEU LEU TRP ARG ASN PRO ASP GLY ASP          
SEQRES   6 G  884  ASP ASP GLN LEU ILE GLN ILE THR MET LYS ASP VAL ASN          
SEQRES   7 G  884  VAL GLU ASN VAL ASN GLN GLN ARG GLY GLU LYS SER ILE          
SEQRES   8 G  884  PHE LYS GLY LYS SER PRO SER LYS ILE MET GLY LYS GLU          
SEQRES   9 G  884  ASN LEU GLU ALA LEU GLN ARG PRO THR LEU LEU HIS LEU          
SEQRES  10 G  884  ILE HIS GLY LYS VAL LYS GLU PHE TYR SER TYR GLN ASN          
SEQRES  11 G  884  GLU ALA VAL ALA ILE GLU ASN ILE LYS ARG GLY LEU ALA          
SEQRES  12 G  884  SER LEU PHE GLN THR GLN LEU SER SER GLY THR THR ASN          
SEQRES  13 G  884  GLU VAL ASP ILE SER GLY ASN CYS LYS VAL THR TYR GLN          
SEQRES  14 G  884  ALA HIS GLN ASP LYS VAL ILE LYS ILE LYS ALA LEU ASP          
SEQRES  15 G  884  SER CYS LYS ILE ALA ARG SER GLY PHE THR THR PRO ASN          
SEQRES  16 G  884  GLN VAL LEU GLY VAL SER SER LYS ALA THR SER VAL THR          
SEQRES  17 G  884  THR TYR LYS ILE GLU ASP SER PHE VAL ILE ALA VAL LEU          
SEQRES  18 G  884  ALA GLU GLU THR HIS ASN PHE GLY LEU ASN PHE LEU GLN          
SEQRES  19 G  884  THR ILE LYS GLY LYS ILE VAL SER LYS GLN LYS LEU GLU          
SEQRES  20 G  884  LEU LYS THR THR GLU ALA GLY PRO ARG LEU MET SER GLY          
SEQRES  21 G  884  LYS GLN ALA ALA ALA ILE ILE LYS ALA VAL ASP SER LYS          
SEQRES  22 G  884  TYR THR ALA ILE PRO ILE VAL GLY GLN VAL PHE GLN SER          
SEQRES  23 G  884  HIS CYS LYS GLY CYS PRO SER LEU SER GLU LEU TRP ARG          
SEQRES  24 G  884  SER THR ARG LYS TYR LEU GLN PRO ASP ASN LEU SER LYS          
SEQRES  25 G  884  ALA GLU ALA VAL ARG ASN PHE LEU ALA PHE ILE GLN HIS          
SEQRES  26 G  884  LEU ARG THR ALA LYS LYS GLU GLU ILE LEU GLN ILE LEU          
SEQRES  27 G  884  LYS MET GLU ASN LYS GLU VAL LEU PRO GLN LEU VAL ASP          
SEQRES  28 G  884  ALA VAL THR SER ALA GLN THR SER ASP SER LEU GLU ALA          
SEQRES  29 G  884  ILE LEU ASP PHE LEU ASP PHE LYS SER ASP SER SER ILE          
SEQRES  30 G  884  ILE LEU GLN GLU ARG PHE LEU TYR ALA CYS GLY PHE ALA          
SEQRES  31 G  884  SER HIS PRO ASN GLU GLU LEU LEU ARG ALA LEU ILE SER          
SEQRES  32 G  884  LYS PHE LYS GLY SER ILE GLY SER SER ASP ILE ARG GLU          
SEQRES  33 G  884  THR VAL MET ILE ILE THR GLY THR LEU VAL ARG LYS LEU          
SEQRES  34 G  884  CYS GLN ASN GLU GLY CYS LYS LEU LYS ALA VAL VAL GLU          
SEQRES  35 G  884  ALA LYS LYS LEU ILE LEU GLY GLY LEU GLU LYS ALA GLU          
SEQRES  36 G  884  LYS LYS GLU ASP THR ARG MET TYR LEU LEU ALA LEU LYS          
SEQRES  37 G  884  ASN ALA LEU LEU PRO GLU GLY ILE PRO SER LEU LEU LYS          
SEQRES  38 G  884  TYR ALA GLU ALA GLY GLU GLY PRO ILE SER HIS LEU ALA          
SEQRES  39 G  884  THR THR ALA LEU GLN ARG TYR ASP LEU PRO PHE ILE THR          
SEQRES  40 G  884  ASP GLU VAL LYS LYS THR LEU ASN ARG ILE TYR HIS GLN          
SEQRES  41 G  884  ASN ARG LYS VAL HIS GLU LYS THR VAL ARG THR ALA ALA          
SEQRES  42 G  884  ALA ALA ILE ILE LEU ASN ASN ASN PRO SER TYR MET ASP          
SEQRES  43 G  884  VAL LYS ASN ILE LEU LEU SER ILE GLY GLU LEU PRO GLN          
SEQRES  44 G  884  GLU MET ASN LYS TYR MET LEU ALA ILE VAL GLN ASP ILE          
SEQRES  45 G  884  LEU ARG PHE GLU MET PRO ALA SER LYS ILE VAL ARG ARG          
SEQRES  46 G  884  VAL LEU LYS GLU MET VAL ALA HIS ASN TYR ASP ARG PHE          
SEQRES  47 G  884  SER ARG SER GLY SER SER SER ALA TYR THR GLY TYR ILE          
SEQRES  48 G  884  GLU ARG SER PRO ARG SER ALA SER THR TYR SER LEU ASP          
SEQRES  49 G  884  ILE LEU TYR SER GLY SER GLY ILE LEU ARG ARG SER ASN          
SEQRES  50 G  884  LEU ASN ILE PHE GLN TYR ILE GLY LYS ALA GLY LEU HIS          
SEQRES  51 G  884  GLY SER GLN VAL VAL ILE GLU ALA GLN GLY LEU GLU ALA          
SEQRES  52 G  884  LEU ILE ALA ALA THR PRO ASP GLU GLY GLU GLU ASN LEU          
SEQRES  53 G  884  ASP SER TYR ALA GLY MET SER ALA ILE LEU PHE ASP VAL          
SEQRES  54 G  884  GLN LEU ARG PRO VAL THR PHE PHE ASN GLY TYR SER ASP          
SEQRES  55 G  884  LEU MET SER LYS MET LEU SER ALA SER GLY ASP PRO ILE          
SEQRES  56 G  884  SER VAL VAL LYS GLY LEU ILE LEU LEU ILE ASP HIS SER          
SEQRES  57 G  884  GLN GLU LEU GLN LEU GLN SER GLY LEU LYS ALA ASN ILE          
SEQRES  58 G  884  GLU VAL GLN GLY GLY LEU ALA ILE ASP ILE SER GLY ALA          
SEQRES  59 G  884  MET GLU PHE SER LEU TRP TYR ARG GLU SER LYS THR ARG          
SEQRES  60 G  884  VAL LYS ASN ARG VAL THR VAL VAL ILE THR THR ASP ILE          
SEQRES  61 G  884  THR VAL ASP SER SER PHE VAL LYS ALA GLY LEU GLU THR          
SEQRES  62 G  884  SER THR GLU THR GLU ALA GLY LEU GLU PHE ILE SER THR          
SEQRES  63 G  884  VAL GLN PHE SER GLN TYR PRO PHE LEU VAL CYS MET GLN          
SEQRES  64 G  884  MET ASP LYS ASP GLU ALA PRO PHE ARG GLN PHE GLU LYS          
SEQRES  65 G  884  LYS TYR GLU ARG LEU SER THR GLY ARG GLY TYR VAL SER          
SEQRES  66 G  884  GLN LYS ARG LYS GLU SER VAL LEU ALA GLY CYS GLU PHE          
SEQRES  67 G  884  PRO LEU HIS GLN GLU ASN SER GLU MET CYS LYS VAL VAL          
SEQRES  68 G  884  PHE ALA PRO GLN PRO ASP SER THR SER SER GLY TRP PHE          
SEQRES   1 H  884  MET HIS HIS HIS HIS HIS HIS MET VAL LYS GLY HIS THR          
SEQRES   2 H  884  THR GLY LEU SER LEU ASN ASN ASP ARG LEU TYR LYS LEU          
SEQRES   3 H  884  THR TYR SER THR GLU VAL LEU LEU ASP ARG GLY LYS GLY          
SEQRES   4 H  884  LYS LEU GLN ASP SER VAL GLY TYR ARG ILE SER SER ASN          
SEQRES   5 H  884  VAL ASP VAL ALA LEU LEU TRP ARG ASN PRO ASP GLY ASP          
SEQRES   6 H  884  ASP ASP GLN LEU ILE GLN ILE THR MET LYS ASP VAL ASN          
SEQRES   7 H  884  VAL GLU ASN VAL ASN GLN GLN ARG GLY GLU LYS SER ILE          
SEQRES   8 H  884  PHE LYS GLY LYS SER PRO SER LYS ILE MET GLY LYS GLU          
SEQRES   9 H  884  ASN LEU GLU ALA LEU GLN ARG PRO THR LEU LEU HIS LEU          
SEQRES  10 H  884  ILE HIS GLY LYS VAL LYS GLU PHE TYR SER TYR GLN ASN          
SEQRES  11 H  884  GLU ALA VAL ALA ILE GLU ASN ILE LYS ARG GLY LEU ALA          
SEQRES  12 H  884  SER LEU PHE GLN THR GLN LEU SER SER GLY THR THR ASN          
SEQRES  13 H  884  GLU VAL ASP ILE SER GLY ASN CYS LYS VAL THR TYR GLN          
SEQRES  14 H  884  ALA HIS GLN ASP LYS VAL ILE LYS ILE LYS ALA LEU ASP          
SEQRES  15 H  884  SER CYS LYS ILE ALA ARG SER GLY PHE THR THR PRO ASN          
SEQRES  16 H  884  GLN VAL LEU GLY VAL SER SER LYS ALA THR SER VAL THR          
SEQRES  17 H  884  THR TYR LYS ILE GLU ASP SER PHE VAL ILE ALA VAL LEU          
SEQRES  18 H  884  ALA GLU GLU THR HIS ASN PHE GLY LEU ASN PHE LEU GLN          
SEQRES  19 H  884  THR ILE LYS GLY LYS ILE VAL SER LYS GLN LYS LEU GLU          
SEQRES  20 H  884  LEU LYS THR THR GLU ALA GLY PRO ARG LEU MET SER GLY          
SEQRES  21 H  884  LYS GLN ALA ALA ALA ILE ILE LYS ALA VAL ASP SER LYS          
SEQRES  22 H  884  TYR THR ALA ILE PRO ILE VAL GLY GLN VAL PHE GLN SER          
SEQRES  23 H  884  HIS CYS LYS GLY CYS PRO SER LEU SER GLU LEU TRP ARG          
SEQRES  24 H  884  SER THR ARG LYS TYR LEU GLN PRO ASP ASN LEU SER LYS          
SEQRES  25 H  884  ALA GLU ALA VAL ARG ASN PHE LEU ALA PHE ILE GLN HIS          
SEQRES  26 H  884  LEU ARG THR ALA LYS LYS GLU GLU ILE LEU GLN ILE LEU          
SEQRES  27 H  884  LYS MET GLU ASN LYS GLU VAL LEU PRO GLN LEU VAL ASP          
SEQRES  28 H  884  ALA VAL THR SER ALA GLN THR SER ASP SER LEU GLU ALA          
SEQRES  29 H  884  ILE LEU ASP PHE LEU ASP PHE LYS SER ASP SER SER ILE          
SEQRES  30 H  884  ILE LEU GLN GLU ARG PHE LEU TYR ALA CYS GLY PHE ALA          
SEQRES  31 H  884  SER HIS PRO ASN GLU GLU LEU LEU ARG ALA LEU ILE SER          
SEQRES  32 H  884  LYS PHE LYS GLY SER ILE GLY SER SER ASP ILE ARG GLU          
SEQRES  33 H  884  THR VAL MET ILE ILE THR GLY THR LEU VAL ARG LYS LEU          
SEQRES  34 H  884  CYS GLN ASN GLU GLY CYS LYS LEU LYS ALA VAL VAL GLU          
SEQRES  35 H  884  ALA LYS LYS LEU ILE LEU GLY GLY LEU GLU LYS ALA GLU          
SEQRES  36 H  884  LYS LYS GLU ASP THR ARG MET TYR LEU LEU ALA LEU LYS          
SEQRES  37 H  884  ASN ALA LEU LEU PRO GLU GLY ILE PRO SER LEU LEU LYS          
SEQRES  38 H  884  TYR ALA GLU ALA GLY GLU GLY PRO ILE SER HIS LEU ALA          
SEQRES  39 H  884  THR THR ALA LEU GLN ARG TYR ASP LEU PRO PHE ILE THR          
SEQRES  40 H  884  ASP GLU VAL LYS LYS THR LEU ASN ARG ILE TYR HIS GLN          
SEQRES  41 H  884  ASN ARG LYS VAL HIS GLU LYS THR VAL ARG THR ALA ALA          
SEQRES  42 H  884  ALA ALA ILE ILE LEU ASN ASN ASN PRO SER TYR MET ASP          
SEQRES  43 H  884  VAL LYS ASN ILE LEU LEU SER ILE GLY GLU LEU PRO GLN          
SEQRES  44 H  884  GLU MET ASN LYS TYR MET LEU ALA ILE VAL GLN ASP ILE          
SEQRES  45 H  884  LEU ARG PHE GLU MET PRO ALA SER LYS ILE VAL ARG ARG          
SEQRES  46 H  884  VAL LEU LYS GLU MET VAL ALA HIS ASN TYR ASP ARG PHE          
SEQRES  47 H  884  SER ARG SER GLY SER SER SER ALA TYR THR GLY TYR ILE          
SEQRES  48 H  884  GLU ARG SER PRO ARG SER ALA SER THR TYR SER LEU ASP          
SEQRES  49 H  884  ILE LEU TYR SER GLY SER GLY ILE LEU ARG ARG SER ASN          
SEQRES  50 H  884  LEU ASN ILE PHE GLN TYR ILE GLY LYS ALA GLY LEU HIS          
SEQRES  51 H  884  GLY SER GLN VAL VAL ILE GLU ALA GLN GLY LEU GLU ALA          
SEQRES  52 H  884  LEU ILE ALA ALA THR PRO ASP GLU GLY GLU GLU ASN LEU          
SEQRES  53 H  884  ASP SER TYR ALA GLY MET SER ALA ILE LEU PHE ASP VAL          
SEQRES  54 H  884  GLN LEU ARG PRO VAL THR PHE PHE ASN GLY TYR SER ASP          
SEQRES  55 H  884  LEU MET SER LYS MET LEU SER ALA SER GLY ASP PRO ILE          
SEQRES  56 H  884  SER VAL VAL LYS GLY LEU ILE LEU LEU ILE ASP HIS SER          
SEQRES  57 H  884  GLN GLU LEU GLN LEU GLN SER GLY LEU LYS ALA ASN ILE          
SEQRES  58 H  884  GLU VAL GLN GLY GLY LEU ALA ILE ASP ILE SER GLY ALA          
SEQRES  59 H  884  MET GLU PHE SER LEU TRP TYR ARG GLU SER LYS THR ARG          
SEQRES  60 H  884  VAL LYS ASN ARG VAL THR VAL VAL ILE THR THR ASP ILE          
SEQRES  61 H  884  THR VAL ASP SER SER PHE VAL LYS ALA GLY LEU GLU THR          
SEQRES  62 H  884  SER THR GLU THR GLU ALA GLY LEU GLU PHE ILE SER THR          
SEQRES  63 H  884  VAL GLN PHE SER GLN TYR PRO PHE LEU VAL CYS MET GLN          
SEQRES  64 H  884  MET ASP LYS ASP GLU ALA PRO PHE ARG GLN PHE GLU LYS          
SEQRES  65 H  884  LYS TYR GLU ARG LEU SER THR GLY ARG GLY TYR VAL SER          
SEQRES  66 H  884  GLN LYS ARG LYS GLU SER VAL LEU ALA GLY CYS GLU PHE          
SEQRES  67 H  884  PRO LEU HIS GLN GLU ASN SER GLU MET CYS LYS VAL VAL          
SEQRES  68 H  884  PHE ALA PRO GLN PRO ASP SER THR SER SER GLY TRP PHE          
HET     CA  A 601       1                                                       
HET    EDO  A 602       4                                                       
HET    EDO  A 603       4                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    EDO  A 606       4                                                       
HET     CA  B 601       1                                                       
HET    PGE  B 602      10                                                       
HET    PGE  B 603      10                                                       
HET    SO4  B 604       5                                                       
HET    EDO  B 605       4                                                       
HET    EDO  B 606       4                                                       
HET    EDO  B 607       4                                                       
HET    PEG  B 608       7                                                       
HET    PEG  B 609       7                                                       
HET    PE5  G 901      27                                                       
HET    PGE  G 902      10                                                       
HET    TRS  G 903       8                                                       
HET    SO4  G 904       5                                                       
HET    SO4  G 905       5                                                       
HET    SO4  G 906       5                                                       
HET    SO4  G 907       5                                                       
HET    SO4  G 908       5                                                       
HET    SO4  G 909       5                                                       
HET    SO4  G 910       5                                                       
HET    EDO  G 911       4                                                       
HET    EDO  G 912       4                                                       
HET    EDO  G 913       4                                                       
HET    EDO  G 914       4                                                       
HET    EDO  G 915       4                                                       
HET    EDO  G 916       4                                                       
HET    PEG  G 917       7                                                       
HET    PEG  G 918       7                                                       
HET    PE5  H 901      27                                                       
HET    PE4  H 902      24                                                       
HET    PGE  H 903      10                                                       
HET    PGE  H 904      10                                                       
HET    PGE  H 905      10                                                       
HET    SO4  H 906       5                                                       
HET    SO4  H 907       5                                                       
HET    SO4  H 908       5                                                       
HET    EDO  H 909       4                                                       
HET    EDO  H 910       4                                                       
HET    EDO  H 911       4                                                       
HET    EDO  H 912       4                                                       
HET    EDO  H 913       4                                                       
HET    PEG  H 914       7                                                       
HET    PEG  H 915       7                                                       
HET    PEG  H 916       7                                                       
HET    PEG  H 917       7                                                       
HET    PEG  H 918       7                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL                       
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-              
HETNAM   2 PE4  ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL                                 
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     PE5 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-           
HETSYN   2 PE5  ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, POLYETHYLENE           
HETSYN   3 PE5  GLYCOL PEG400                                                   
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000                                      
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   6  EDO    19(C2 H6 O2)                                                 
FORMUL  12  PGE    6(C6 H14 O4)                                                 
FORMUL  14  SO4    11(O4 S 2-)                                                  
FORMUL  18  PEG    9(C4 H10 O3)                                                 
FORMUL  20  PE5    2(C18 H38 O9)                                                
FORMUL  22  TRS    C4 H12 N O3 1+                                               
FORMUL  39  PE4    C16 H34 O8                                                   
FORMUL  56  HOH   *222(H2 O)                                                    
HELIX    1 AA1 ASN A   33  HIS A   41  1                                   9    
HELIX    2 AA2 CYS A   53  ALA A   72  1                                  20    
HELIX    3 AA3 GLU A   87  TYR A   94  1                                   8    
HELIX    4 AA4 GLU A  121  GLY A  134  1                                  14    
HELIX    5 AA5 ASP A  142  SER A  153  1                                  12    
HELIX    6 AA6 SER A  166  ILE A  179  1                                  14    
HELIX    7 AA7 ASN A  189  TYR A  196  1                                   8    
HELIX    8 AA8 THR A  221  LEU A  234  1                                  14    
HELIX    9 AA9 THR A  244  PHE A  249  1                                   6    
HELIX   10 AB1 ASP A  267  SER A  281  1                                  15    
HELIX   11 AB2 HIS A  295  ASP A  297  5                                   3    
HELIX   12 AB3 ASN A  298  PHE A  305  1                                   8    
HELIX   13 AB4 LYS A  308  CYS A  312  5                                   5    
HELIX   14 AB5 THR A  335  GLY A  349  1                                  15    
HELIX   15 AB6 ASN A  376  PHE A  382  1                                   7    
HELIX   16 AB7 CYS A  397  LYS A  415  1                                  19    
HELIX   17 AB8 THR A  462  SER A  472  1                                  11    
HELIX   18 AB9 ASN B   33  HIS B   41  1                                   9    
HELIX   19 AC1 CYS B   53  GLU B   73  1                                  21    
HELIX   20 AC2 GLU B   87  TYR B   94  1                                   8    
HELIX   21 AC3 GLU B  121  GLY B  134  1                                  14    
HELIX   22 AC4 ASP B  142  SER B  153  1                                  12    
HELIX   23 AC5 SER B  166  ILE B  179  1                                  14    
HELIX   24 AC6 ASN B  189  TYR B  196  1                                   8    
HELIX   25 AC7 THR B  221  LEU B  234  1                                  14    
HELIX   26 AC8 THR B  244  PHE B  249  1                                   6    
HELIX   27 AC9 ASP B  267  SER B  281  1                                  15    
HELIX   28 AD1 HIS B  295  ASP B  297  5                                   3    
HELIX   29 AD2 ASN B  298  PHE B  305  1                                   8    
HELIX   30 AD3 LYS B  308  CYS B  312  5                                   5    
HELIX   31 AD4 THR B  335  GLY B  349  1                                  15    
HELIX   32 AD5 ASN B  376  PHE B  382  1                                   7    
HELIX   33 AD6 CYS B  397  LYS B  415  1                                  19    
HELIX   34 AD7 THR B  462  SER B  472  1                                  11    
HELIX   35 AD8 ARG G   96  SER G  100  5                                   5    
HELIX   36 AD9 SER G  106  GLY G  112  1                                   7    
HELIX   37 AE1 GLY G  112  ARG G  121  1                                  10    
HELIX   38 AE2 ALA G  142  LEU G  155  1                                  14    
HELIX   39 AE3 LEU G  191  CYS G  194  5                                   4    
HELIX   40 AE4 GLN G  272  ASP G  281  1                                  10    
HELIX   41 AE5 SER G  303  ARG G  312  1                                  10    
HELIX   42 AE6 GLN G  316  LEU G  320  5                                   5    
HELIX   43 AE7 LYS G  322  ARG G  337  1                                  16    
HELIX   44 AE8 LYS G  340  MET G  350  1                                  11    
HELIX   45 AE9 VAL G  355  GLN G  367  1                                  13    
HELIX   46 AF1 THR G  368  LEU G  379  1                                  12    
HELIX   47 AF2 SER G  386  PHE G  399  1                                  14    
HELIX   48 AF3 ASN G  404  GLY G  417  1                                  14    
HELIX   49 AF4 SER G  421  ASN G  442  1                                  22    
HELIX   50 AF5 LEU G  447  LYS G  463  1                                  17    
HELIX   51 AF6 LYS G  466  LEU G  481  1                                  16    
HELIX   52 AF7 LEU G  482  GLU G  484  5                                   3    
HELIX   53 AF8 GLY G  485  ALA G  495  1                                  11    
HELIX   54 AF9 GLY G  498  GLN G  509  1                                  12    
HELIX   55 AG1 ARG G  510  TYR G  511  5                                   2    
HELIX   56 AG2 ASP G  512  ILE G  516  5                                   5    
HELIX   57 AG3 THR G  517  GLN G  530  1                                  14    
HELIX   58 AG4 GLU G  536  ASN G  549  1                                  14    
HELIX   59 AG5 SER G  553  ILE G  564  1                                  12    
HELIX   60 AG6 PRO G  568  GLU G  586  1                                  19    
HELIX   61 AG7 ALA G  589  LYS G  598  1                                  10    
HELIX   62 AG8 LEU G  671  ILE G  675  5                                   5    
HELIX   63 AG9 GLY G  682  LEU G  686  5                                   5    
HELIX   64 AH1 GLY G  709  MET G  717  1                                   9    
HELIX   65 AH2 HIS G  871  PHE G  882  1                                  12    
HELIX   66 AH3 ARG H   96  SER H  100  5                                   5    
HELIX   67 AH4 SER H  106  GLY H  112  1                                   7    
HELIX   68 AH5 GLY H  112  ARG H  121  1                                  10    
HELIX   69 AH6 ALA H  142  LEU H  155  1                                  14    
HELIX   70 AH7 LEU H  191  CYS H  194  5                                   4    
HELIX   71 AH8 GLN H  272  ASP H  281  1                                  10    
HELIX   72 AH9 SER H  303  ARG H  312  1                                  10    
HELIX   73 AI1 GLN H  316  LEU H  320  5                                   5    
HELIX   74 AI2 LYS H  322  ARG H  337  1                                  16    
HELIX   75 AI3 LYS H  340  MET H  350  1                                  11    
HELIX   76 AI4 VAL H  355  GLN H  367  1                                  13    
HELIX   77 AI5 THR H  368  LEU H  379  1                                  12    
HELIX   78 AI6 SER H  386  PHE H  399  1                                  14    
HELIX   79 AI7 ASN H  404  GLY H  417  1                                  14    
HELIX   80 AI8 SER H  421  GLN H  441  1                                  21    
HELIX   81 AI9 LEU H  447  GLU H  462  1                                  16    
HELIX   82 AJ1 LYS H  466  LEU H  481  1                                  16    
HELIX   83 AJ2 LEU H  482  GLU H  484  5                                   3    
HELIX   84 AJ3 GLY H  485  ALA H  495  1                                  11    
HELIX   85 AJ4 GLY H  498  GLN H  509  1                                  12    
HELIX   86 AJ5 ARG H  510  TYR H  511  5                                   2    
HELIX   87 AJ6 ASP H  512  ILE H  516  5                                   5    
HELIX   88 AJ7 THR H  517  GLN H  530  1                                  14    
HELIX   89 AJ8 GLU H  536  ASN H  549  1                                  14    
HELIX   90 AJ9 SER H  553  ILE H  564  1                                  12    
HELIX   91 AK1 PRO H  568  GLU H  586  1                                  19    
HELIX   92 AK2 ALA H  589  LEU H  597  1                                   9    
HELIX   93 AK3 LEU H  671  ILE H  675  5                                   5    
HELIX   94 AK4 GLY H  682  LEU H  686  5                                   5    
HELIX   95 AK5 GLY H  709  MET H  717  1                                   9    
HELIX   96 AK6 HIS H  871  PHE H  882  1                                  12    
SHEET    1 AA1 5 LEU A  27  VAL A  28  0                                        
SHEET    2 AA1 5 ILE A  77  ASP A  83  1  O  LEU A  79   N  LEU A  27           
SHEET    3 AA1 5 TYR A  43  TYR A  49  1  N  LEU A  45   O  ALA A  80           
SHEET    4 AA1 5 THR A 101  PHE A 105 -1  O  THR A 101   N  PHE A  48           
SHEET    5 AA1 5 LYS A 114  GLU A 115 -1  O  LYS A 114   N  PHE A 104           
SHEET    1 AA2 5 ALA A 137  THR A 139  0                                        
SHEET    2 AA2 5 PHE A 184  THR A 187  1  O  ILE A 186   N  THR A 138           
SHEET    3 AA2 5 VAL A 155  PHE A 160  1  N  GLY A 159   O  GLY A 185           
SHEET    4 AA2 5 GLY A 202  LYS A 207 -1  O  PHE A 206   N  ALA A 156           
SHEET    5 AA2 5 ARG A 213  ASN A 215 -1  O  ASN A 214   N  LEU A 205           
SHEET    1 AA3 5 VAL A 237  GLU A 239  0                                        
SHEET    2 AA3 5 LEU A 287  ILE A 291  1  O  PHE A 290   N  ILE A 238           
SHEET    3 AA3 5 THR A 255  PHE A 260  1  N  ILE A 257   O  ILE A 289           
SHEET    4 AA3 5 ALA A 314  LEU A 320 -1  O  ARG A 316   N  LEU A 258           
SHEET    5 AA3 5 MET A 324  TYR A 327 -1  O  TYR A 327   N  LEU A 317           
SHEET    1 AA4 5 LYS A 370  VAL A 371  0                                        
SHEET    2 AA4 5 ILE A 420  ASP A 426  1  O  ILE A 422   N  LYS A 370           
SHEET    3 AA4 5 ASN A 387  TYR A 393  1  N  PHE A 389   O  ALA A 423           
SHEET    4 AA4 5 THR A 442  PHE A 446 -1  O  THR A 442   N  PHE A 392           
SHEET    5 AA4 5 ILE A 455  ASP A 456 -1  O  ILE A 455   N  PHE A 445           
SHEET    1 AA5 5 LEU B  27  VAL B  28  0                                        
SHEET    2 AA5 5 ILE B  77  ASP B  83  1  O  LEU B  79   N  LEU B  27           
SHEET    3 AA5 5 TYR B  43  TYR B  49  1  N  LEU B  45   O  ALA B  80           
SHEET    4 AA5 5 THR B 101  ARG B 106 -1  O  THR B 101   N  PHE B  48           
SHEET    5 AA5 5 LYS B 114  GLU B 115 -1  O  LYS B 114   N  PHE B 104           
SHEET    1 AA6 5 THR B 138  THR B 139  0                                        
SHEET    2 AA6 5 PHE B 184  THR B 187  1  O  ILE B 186   N  THR B 138           
SHEET    3 AA6 5 VAL B 155  PHE B 160  1  N  GLY B 159   O  GLY B 185           
SHEET    4 AA6 5 GLY B 202  LYS B 207 -1  O  PHE B 206   N  ALA B 156           
SHEET    5 AA6 5 ARG B 213  ASN B 215 -1  O  ASN B 214   N  LEU B 205           
SHEET    1 AA7 5 VAL B 237  GLU B 239  0                                        
SHEET    2 AA7 5 LEU B 287  ILE B 291  1  O  PHE B 290   N  ILE B 238           
SHEET    3 AA7 5 THR B 255  PHE B 260  1  N  LEU B 259   O  ILE B 289           
SHEET    4 AA7 5 ALA B 314  LEU B 320 -1  O  ARG B 316   N  LEU B 258           
SHEET    5 AA7 5 MET B 324  TYR B 327 -1  O  TYR B 327   N  LEU B 317           
SHEET    1 AA8 5 VAL B 369  VAL B 371  0                                        
SHEET    2 AA8 5 ILE B 420  ASP B 426  1  O  ILE B 422   N  LYS B 370           
SHEET    3 AA8 5 ASN B 387  TYR B 393  1  N  PHE B 389   O  ALA B 423           
SHEET    4 AA8 5 THR B 442  PHE B 446 -1  O  THR B 442   N  PHE B 392           
SHEET    5 AA8 5 ILE B 455  ASP B 456 -1  O  ILE B 455   N  PHE B 445           
SHEET    1 AA912 GLY G 163  ASP G 169  0                                        
SHEET    2 AA912 GLY G 172  ALA G 180 -1  O  TYR G 178   N  GLY G 163           
SHEET    3 AA912 LYS G 184  LYS G 189 -1  O  ILE G 188   N  THR G 177           
SHEET    4 AA912 VAL G 210  GLU G 223 -1  O  THR G 218   N  LYS G 187           
SHEET    5 AA912 PHE G 226  LEU G 240 -1  O  LEU G 231   N  THR G 219           
SHEET    6 AA912 LYS G 247  ALA G 263 -1  O  SER G 252   N  GLU G 234           
SHEET    7 AA912 ARG G  32  ASP G  45 -1  N  LYS G  35   O  LYS G 259           
SHEET    8 AA912 VAL G  55  ARG G  70 -1  O  VAL G  65   N  TYR G  34           
SHEET    9 AA912 ASP G  77  ASN G  91 -1  O  LYS G  85   N  ASN G  62           
SHEET   10 AA912 THR G 123  ILE G 128 -1  O  LEU G 125   N  ILE G  80           
SHEET   11 AA912 LYS G 131  TYR G 138 -1  O  LYS G 133   N  HIS G 126           
SHEET   12 AA912 TYR G 284  ILE G 287 -1  O  THR G 285   N  SER G 137           
SHEET    1 AB1 7 GLY G 200  PHE G 201  0                                        
SHEET    2 AB1 7 ILE G 725  GLN G 742 -1  O  SER G 738   N  PHE G 201           
SHEET    3 AB1 7 LYS G 748  SER G 768 -1  O  GLY G 755   N  ILE G 735           
SHEET    4 AB1 7 GLU G 773  ASP G 793 -1  O  LYS G 779   N  SER G 762           
SHEET    5 AB1 7 LYS G 798  GLN G 818 -1  O  LEU G 811   N  ASN G 780           
SHEET    6 AB1 7 ALA G 835  ARG G 846 -1  O  LYS G 842   N  GLU G 802           
SHEET    7 AB1 7 TYR G 853  LEU G 863 -1  O  LEU G 863   N  ALA G 835           
SHEET    1 AB2 7 GLY G 200  PHE G 201  0                                        
SHEET    2 AB2 7 ILE G 725  GLN G 742 -1  O  SER G 738   N  PHE G 201           
SHEET    3 AB2 7 LYS G 748  SER G 768 -1  O  GLY G 755   N  ILE G 735           
SHEET    4 AB2 7 GLU G 773  ASP G 793 -1  O  LYS G 779   N  SER G 762           
SHEET    5 AB2 7 LYS G 798  GLN G 818 -1  O  LEU G 811   N  ASN G 780           
SHEET    6 AB2 7 LEU G 825  LYS G 832 -1  O  ASP G 831   N  GLU G 812           
SHEET    7 AB2 7 CYS G 866  PHE G 868 -1  O  CYS G 866   N  LYS G 832           
SHEET    1 AB3 6 SER G 615  ARG G 623  0                                        
SHEET    2 AB3 6 SER G 627  TYR G 637 -1  O  SER G 629   N  ILE G 621           
SHEET    3 AB3 6 LEU G 643  ILE G 654 -1  O  ARG G 645   N  LEU G 636           
SHEET    4 AB3 6 ALA G 657  GLN G 669 -1  O  ALA G 657   N  ILE G 654           
SHEET    5 AB3 6 TYR G 689  LEU G 696 -1  O  SER G 693   N  VAL G 665           
SHEET    6 AB3 6 VAL G 699  GLN G 700 -1  O  VAL G 699   N  LEU G 696           
SHEET    1 AB4 6 SER G 615  ARG G 623  0                                        
SHEET    2 AB4 6 SER G 627  TYR G 637 -1  O  SER G 629   N  ILE G 621           
SHEET    3 AB4 6 LEU G 643  ILE G 654 -1  O  ARG G 645   N  LEU G 636           
SHEET    4 AB4 6 ALA G 657  GLN G 669 -1  O  ALA G 657   N  ILE G 654           
SHEET    5 AB4 6 TYR G 689  LEU G 696 -1  O  SER G 693   N  VAL G 665           
SHEET    6 AB4 6 VAL G 704  ASN G 708 -1  O  PHE G 706   N  ALA G 690           
SHEET    1 AB512 GLY H 163  ASP H 169  0                                        
SHEET    2 AB512 GLY H 172  ALA H 180 -1  O  TYR H 178   N  GLY H 163           
SHEET    3 AB512 LYS H 184  LYS H 189 -1  O  ILE H 188   N  THR H 177           
SHEET    4 AB512 VAL H 210  GLU H 223 -1  O  THR H 218   N  LYS H 187           
SHEET    5 AB512 PHE H 226  LEU H 240 -1  O  LEU H 231   N  THR H 219           
SHEET    6 AB512 LYS H 247  ALA H 263 -1  O  GLN H 254   N  ALA H 232           
SHEET    7 AB512 ARG H  32  ASP H  45 -1  N  LEU H  43   O  VAL H 251           
SHEET    8 AB512 VAL H  55  ARG H  70 -1  O  ILE H  59   N  THR H  40           
SHEET    9 AB512 ASP H  77  ASN H  91 -1  O  LYS H  85   N  ASN H  62           
SHEET   10 AB512 THR H 123  ILE H 128 -1  O  LEU H 125   N  ILE H  80           
SHEET   11 AB512 LYS H 131  TYR H 138 -1  O  LYS H 133   N  HIS H 126           
SHEET   12 AB512 TYR H 284  ILE H 287 -1  O  THR H 285   N  SER H 137           
SHEET    1 AB6 7 GLY H 200  THR H 202  0                                        
SHEET    2 AB6 7 SER H 726  GLN H 742 -1  O  SER H 738   N  PHE H 201           
SHEET    3 AB6 7 LYS H 748  SER H 768 -1  O  GLY H 755   N  ILE H 735           
SHEET    4 AB6 7 GLU H 773  ASP H 793 -1  O  LYS H 779   N  SER H 762           
SHEET    5 AB6 7 LYS H 798  GLN H 818 -1  O  LEU H 811   N  ASN H 780           
SHEET    6 AB6 7 ALA H 835  ARG H 846 -1  O  ARG H 838   N  GLU H 806           
SHEET    7 AB6 7 GLY H 852  LEU H 863 -1  O  LEU H 863   N  ALA H 835           
SHEET    1 AB7 7 GLY H 200  THR H 202  0                                        
SHEET    2 AB7 7 SER H 726  GLN H 742 -1  O  SER H 738   N  PHE H 201           
SHEET    3 AB7 7 LYS H 748  SER H 768 -1  O  GLY H 755   N  ILE H 735           
SHEET    4 AB7 7 GLU H 773  ASP H 793 -1  O  LYS H 779   N  SER H 762           
SHEET    5 AB7 7 LYS H 798  GLN H 818 -1  O  LEU H 811   N  ASN H 780           
SHEET    6 AB7 7 LEU H 825  LYS H 832 -1  O  ASP H 831   N  GLU H 812           
SHEET    7 AB7 7 CYS H 866  PHE H 868 -1  O  CYS H 866   N  LYS H 832           
SHEET    1 AB8 6 SER H 615  ARG H 623  0                                        
SHEET    2 AB8 6 SER H 627  TYR H 637 -1  O  SER H 629   N  ILE H 621           
SHEET    3 AB8 6 LEU H 643  ILE H 654 -1  O  ARG H 645   N  LEU H 636           
SHEET    4 AB8 6 ALA H 657  GLN H 669 -1  O  VAL H 664   N  LEU H 648           
SHEET    5 AB8 6 TYR H 689  LEU H 696 -1  O  SER H 693   N  VAL H 665           
SHEET    6 AB8 6 VAL H 699  GLN H 700 -1  O  VAL H 699   N  LEU H 696           
SHEET    1 AB9 6 SER H 615  ARG H 623  0                                        
SHEET    2 AB9 6 SER H 627  TYR H 637 -1  O  SER H 629   N  ILE H 621           
SHEET    3 AB9 6 LEU H 643  ILE H 654 -1  O  ARG H 645   N  LEU H 636           
SHEET    4 AB9 6 ALA H 657  GLN H 669 -1  O  VAL H 664   N  LEU H 648           
SHEET    5 AB9 6 TYR H 689  LEU H 696 -1  O  SER H 693   N  VAL H 665           
SHEET    6 AB9 6 VAL H 704  ASN H 708 -1  O  PHE H 706   N  ALA H 690           
SSBOND   1 CYS G  174    CYS G  194                          1555   1555  2.07  
SSBOND   2 CYS G  298    CYS G  301                          1555   1555  2.05  
SSBOND   3 CYS G  440    CYS G  445                          1555   1555  2.12  
SSBOND   4 CYS G  827    CYS G  878                          1555   1555  2.10  
SSBOND   5 CYS H  174    CYS H  194                          1555   1555  2.10  
SSBOND   6 CYS H  298    CYS H  301                          1555   1555  2.03  
SSBOND   7 CYS H  440    CYS H  445                          1555   1555  2.12  
SSBOND   8 CYS H  827    CYS H  878                          1555   1555  2.09  
LINK         O   ALA A 381                CA    CA A 601     1555   1555  2.80  
LINK         O   ASP A 383                CA    CA A 601     1555   1555  2.58  
LINK         O   LYS A 386                CA    CA A 601     1555   1555  2.50  
LINK         O   PHE A 446                CA    CA A 601     1555   1555  2.59  
LINK         O   PRO A 447                CA    CA A 601     1555   1555  2.56  
LINK         O   ALA B 381                CA    CA B 601     1555   1555  2.80  
LINK         O   ASP B 383                CA    CA B 601     1555   1555  2.56  
LINK         O   LYS B 386                CA    CA B 601     1555   1555  2.54  
LINK         O   PHE B 446                CA    CA B 601     1555   1555  2.65  
LINK         O   PRO B 447                CA    CA B 601     1555   1555  2.57  
LINK        CA    CA A 601                 O   HOH A 713     1555   1555  3.13  
CISPEP   1 TYR A   99    PRO A  100          0         0.03                     
CISPEP   2 CYS A  312    PRO A  313          0         8.20                     
CISPEP   3 PHE A  440    PRO A  441          0        -0.45                     
CISPEP   4 TYR B   99    PRO B  100          0         0.62                     
CISPEP   5 CYS B  312    PRO B  313          0         4.89                     
CISPEP   6 PHE B  440    PRO B  441          0        -3.79                     
CISPEP   7 TYR G  822    PRO G  823          0        -5.59                     
CISPEP   8 TYR G  822    PRO G  823          0        26.65                     
CISPEP   9 TYR H  822    PRO H  823          0        -6.48                     
SITE     1 AC1  5 ALA A 381  ASP A 383  LYS A 386  PHE A 446                    
SITE     2 AC1  5 PRO A 447                                                     
SITE     1 AC2  3 LYS A 162  SER A 190  ASP A 199                               
SITE     1 AC3  6 VAL A 150  SER A 153  GLU A 154  PHE A 206                    
SITE     2 AC3  6 LYS A 207  LYS A 208                                          
SITE     1 AC4  1 LYS A 276                                                     
SITE     1 AC5  3 LYS A 415  HOH A 714  LYS G 195                               
SITE     1 AC6  1 GLY A 349                                                     
SITE     1 AC7  5 ALA B 381  ASP B 383  LYS B 386  PHE B 446                    
SITE     2 AC7  5 PRO B 447                                                     
SITE     1 AC8  2 ALA B 118  ARG B 120                                          
SITE     1 AC9  5 TYR B 327  GLY B 349  LYS G 103  LYS G 105                    
SITE     2 AC9  5 LYS G 109                                                     
SITE     1 AD1  6 GLU B 322  GLU B 323  MET B 324  HOH B 708                    
SITE     2 AD1  6 ARG H 594  HIS H 603                                          
SITE     1 AD2  2 VAL B 237  LYS B 276                                          
SITE     1 AD3  3 TYR B  49  CYS B  56  LYS B  81                               
SITE     1 AD4  2 ASN B 419  LYS G 278                                          
SITE     1 AD5  3 GLU B 177  ALA B 178  LYS B 222                               
SITE     1 AD6  3 HIS B 438  GLN G  95  HOH H1039                               
SITE     1 AD7  5 SER G 646  SER G 662  ASN G 780  ALA G 809                    
SITE     2 AD7  5 PHE G 813                                                     
SITE     1 AD8  4 GLU G 391  TYR G 395  VAL G 728  HOH G1003                    
SITE     1 AD9  1 VAL G 227                                                     
SITE     1 AE1  3 GLY G 850  ARG G 851  GLY G 852                               
SITE     1 AE2  5 GLU G  90  ASN G  91  PHE G 102  HOH G1006                    
SITE     2 AE2  5 HOH G1012                                                     
SITE     1 AE3  4 GLU G 536  LYS G 537  THR G 538  ARG G 644                    
SITE     1 AE4  4 SER G  39  ARG G  58  LYS G 255  HOH G1016                    
SITE     1 AE5  6 SER G 768  LEU G 769  TRP G 770  ILE H 196                    
SITE     2 AE5  6 ALA H 197  ARG H 198                                          
SITE     1 AE6  4 ARG A 300  GLN G 569  ARG G 610  SER G 611                    
SITE     1 AE7  2 ILE G 188  ALA G 190                                          
SITE     1 AE8  1 ARG G 623                                                     
SITE     1 AE9  1 ARG G 121                                                     
SITE     1 AF1  2 ASN G 140  GLU G 141                                          
SITE     1 AF2  2 SER G 296  LYS G 748                                          
SITE     1 AF3  2 ARG G 312  ASN G 352                                          
SITE     1 AF4  9 SER G 365  GLN G 367  ALA G 396  PHE G 399                    
SITE     2 AF4  9 ALA G 400  SER G 401  ILE G 732  LEU G 733                    
SITE     3 AF4  9 HOH G1011                                                     
SITE     1 AF5  4 GLN G 509  ASN G 549  HIS G 660  GLN G 663                    
SITE     1 AF6  4 SER H 646  SER H 662  ASN H 780  PHE H 813                    
SITE     1 AF7  8 LYS H  99  THR H 849  GLY H 850  ARG H 851                    
SITE     2 AF7  8 GLY H 852  VAL H 854  GLN H 856  HOH H1055                    
SITE     1 AF8  5 GLN H 509  ARG H 510  TYR H 511  ASP H 512                    
SITE     2 AF8  5 PHE H 651                                                     
SITE     1 AF9  1 TYR H 554                                                     
SITE     1 AG1  3 SER H  27  PHE H 226  VAL H 227                               
SITE     1 AG2  4 ARG G  32  ALA G 263  THR H 517  ASP H 518                    
SITE     1 AG3  4 GLN H 569  ARG H 610  SER H 611  HOH H1005                    
SITE     1 AG4  3 GLN H 530  ARG H 540  PRO H 568                               
SITE     1 AG5  2 THR H 705  HOH H1040                                          
SITE     1 AG6  2 ARG H 312  ASN H 352                                          
SITE     1 AG7  3 PRO H 204  ASN H 205  GLN H 441                               
SITE     1 AG8  1 TYR H 314                                                     
SITE     1 AG9  2 THR H 165  ASN H 166                                          
SITE     1 AH1  5 TYR H 395  PHE H 399  LEU H 701  VAL H 728                    
SITE     2 AH1  5 GLY H 730                                                     
SITE     1 AH2  1 MET H 692                                                     
SITE     1 AH3  2 SER G 269  LYS H 859                                          
SITE     1 AH4  5 THR H  37  TYR H  38  SER H  39  SER H  61                    
SITE     2 AH4  5 LYS H 255                                                     
SITE     1 AH5  1 GLY H 200                                                     
CRYST1   77.537  105.595  112.269  89.81  76.95  74.24 P 1           2          
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      0.012897 -0.003640 -0.003220        0.00000                         
SCALE2      0.000000  0.009840  0.000609        0.00000                         
SCALE3      0.000000  0.000000  0.009161        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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