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LongText Report for: 1VLQ-pdb

Name Class
1VLQ-pdb
HEADER    HYDROLASE                               09-AUG-04   1VLQ              
TITLE     CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM              
TITLE    2 THERMOTOGA MARITIMA AT 2.10 A RESOLUTION                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL XYLAN ESTERASE;                                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 EC: 3.1.1.41;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA MSB8;                       
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 GENE: TM0077;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    TM0077, ACETYL XYLAN ESTERASE, STRUCTURAL GENOMICS, JCSG,             
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS                                  
REVDAT   1   24-AUG-04 1VLQ    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS                         
JRNL        TITL   CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE                   
JRNL        TITL 2 (TM0077) FROM THERMOTOGA MARITIMA AT 2.10 A                  
JRNL        TITL 3 RESOLUTION                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.10 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 278371                         
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) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14726                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13660                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 61.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 727                          
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 33653                                   
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.71000                                             
REMARK   3    B22 (A**2) : 2.25000                                              
REMARK   3    B33 (A**2) : -1.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.82000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.195         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.128         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.076         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 32148 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 28509 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 43596 ; 1.477 ; 1.939       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 66214 ; 0.927 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3852 ; 6.308 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1585 ;30.549 ;23.073       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5085 ;14.046 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   225 ;17.373 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4439 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 36073 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  7284 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6254 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 28475 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 15311 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A): 16852 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  2055 ; 0.163 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.214 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    65 ; 0.333 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.209 ; 0.200       
REMARK   3   SYMMETRY H-BOND 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): 20879 ; 2.176 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  7800 ; 0.198 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31023 ; 2.593 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 14761 ; 4.775 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12573 ; 6.035 ;11.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H I J K L         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      4       A     320      2                      
REMARK   3           1     B      4       B     320      2                      
REMARK   3           1     C      4       C     320      2                      
REMARK   3           1     D      4       D     320      2                      
REMARK   3           1     E      4       E     320      2                      
REMARK   3           1     F      4       F     320      2                      
REMARK   3           1     G      4       G     320      2                      
REMARK   3           1     H      4       H     320      2                      
REMARK   3           1     I      4       I     320      2                      
REMARK   3           1     J      4       J     320      2                      
REMARK   3           1     K      4       K     320      2                      
REMARK   3           1     L      4       L     320      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    H    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    I    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    J    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    K    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    L    (A):   1852 ;  0.04 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2980 ;  0.26 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2980 ;  0.21 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2980 ;  0.22 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2980 ;  0.21 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   2980 ;  0.24 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   2980 ;  0.22 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   2980 ;  0.21 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    H    (A):   2980 ;  0.21 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    I    (A):   2980 ;  0.22 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    J    (A):   2980 ;  0.27 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    K    (A):   2980 ;  0.30 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    L    (A):   2980 ;  0.27 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1852 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1852 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1852 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1852 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1852 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1852 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1852 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      1    H (A**2):   1852 ;  0.19 ;  0.50           
REMARK   3   TIGHT THERMAL      1    I (A**2):   1852 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      1    J (A**2):   1852 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      1    K (A**2):   1852 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      1    L (A**2):   1852 ;  0.20 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2980 ;  0.98 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2980 ;  1.02 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2980 ;  1.05 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2980 ;  0.92 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   2980 ;  0.96 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   2980 ;  0.90 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   2980 ;  0.95 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    H (A**2):   2980 ;  1.02 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    I (A**2):   2980 ;  0.91 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    J (A**2):   2980 ;  1.01 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    K (A**2):   2980 ;  1.07 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    L (A**2):   2980 ;  1.10 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS 2. THE ACTIVE SITE TRIAD CONSISTS OF SER188,       
REMARK   3  HIS303 AND ASP274. THE ELECTRON DENSITY SUGGESTED THERE COULD       
REMARK   3  EXIST A PARTIALLY OCCUPIED ACYL INTERMEDIATE ON SER188.             
REMARK   3  HOWEVER, IT IS NOT CONCLUSIVE. AS A RESULT, WATER MOLECULES         
REMARK   3  WERE MODELLED. 3. THERE IS SOME UNEXPLAINED DENSITY NEAR N-         
REMARK   3  TERMINUS 4. RESIDUES 134,135 OF CHAIN D,H,I,J,K,L HAVE POOR         
REMARK   3  DENSITY                                                             
REMARK   4                                                                      
REMARK   4 1VLQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-2004.                
REMARK 100 THE RCSB ID CODE IS RCSB001990.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-2001                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRL ; SSRL                        
REMARK 200  BEAMLINE                       : 9-2; 9-2                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918370; 0.918370,0.979126        
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : QUANTUM-315 CCD                    
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA(CCP4 4.2)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 293140                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.560                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200   FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43300                            
REMARK 200   FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP/AUTOSHARP, SHELX, WARP                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-300, 10% GLYCEROL, 0.1M          
REMARK 280  PHOSPHATE-CITRATE PH 4.2 0.2 M (NH4)2SO4 4.5, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP,NANODROP, TEMPERATURE 293K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,1/2+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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       65.47600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 12CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L                      
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     MSE A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     LYS A    -7                                                      
REMARK 465     ILE A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     LYS A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     MSE B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     ASP B    -8                                                      
REMARK 465     LYS B    -7                                                      
REMARK 465     ILE B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     LYS B   324                                                      
REMARK 465     GLY B   325                                                      
REMARK 465     MSE C   -11                                                      
REMARK 465     GLY C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     ASP C    -8                                                      
REMARK 465     LYS C    -7                                                      
REMARK 465     ILE C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     LYS C   324                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     MSE D   -11                                                      
REMARK 465     GLY D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     ASP D    -8                                                      
REMARK 465     LYS D    -7                                                      
REMARK 465     ILE D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     LYS D   324                                                      
REMARK 465     GLY D   325                                                      
REMARK 465     MSE E   -11                                                      
REMARK 465     GLY E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     ASP E    -8                                                      
REMARK 465     LYS E    -7                                                      
REMARK 465     ILE E    -6                                                      
REMARK 465     HIS E    -5                                                      
REMARK 465     HIS E    -4                                                      
REMARK 465     HIS E    -3                                                      
REMARK 465     HIS E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     MSE E     1                                                      
REMARK 465     LYS E   324                                                      
REMARK 465     GLY E   325                                                      
REMARK 465     MSE F   -11                                                      
REMARK 465     GLY F   -10                                                      
REMARK 465     SER F    -9                                                      
REMARK 465     ASP F    -8                                                      
REMARK 465     LYS F    -7                                                      
REMARK 465     ILE F    -6                                                      
REMARK 465     HIS F    -5                                                      
REMARK 465     HIS F    -4                                                      
REMARK 465     HIS F    -3                                                      
REMARK 465     HIS F    -2                                                      
REMARK 465     HIS F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     MSE F     1                                                      
REMARK 465     LYS F   324                                                      
REMARK 465     GLY F   325                                                      
REMARK 465     MSE G   -11                                                      
REMARK 465     GLY G   -10                                                      
REMARK 465     SER G    -9                                                      
REMARK 465     ASP G    -8                                                      
REMARK 465     LYS G    -7                                                      
REMARK 465     ILE G    -6                                                      
REMARK 465     HIS G    -5                                                      
REMARK 465     HIS G    -4                                                      
REMARK 465     HIS G    -3                                                      
REMARK 465     HIS G    -2                                                      
REMARK 465     HIS G    -1                                                      
REMARK 465     HIS G     0                                                      
REMARK 465     MSE G     1                                                      
REMARK 465     LYS G   324                                                      
REMARK 465     GLY G   325                                                      
REMARK 465     MSE H   -11                                                      
REMARK 465     GLY H   -10                                                      
REMARK 465     SER H    -9                                                      
REMARK 465     ASP H    -8                                                      
REMARK 465     LYS H    -7                                                      
REMARK 465     ILE H    -6                                                      
REMARK 465     HIS H    -5                                                      
REMARK 465     HIS H    -4                                                      
REMARK 465     HIS H    -3                                                      
REMARK 465     HIS H    -2                                                      
REMARK 465     HIS H    -1                                                      
REMARK 465     HIS H     0                                                      
REMARK 465     MSE H     1                                                      
REMARK 465     LYS H   324                                                      
REMARK 465     GLY H   325                                                      
REMARK 465     MSE I   -11                                                      
REMARK 465     GLY I   -10                                                      
REMARK 465     SER I    -9                                                      
REMARK 465     ASP I    -8                                                      
REMARK 465     LYS I    -7                                                      
REMARK 465     ILE I    -6                                                      
REMARK 465     HIS I    -5                                                      
REMARK 465     HIS I    -4                                                      
REMARK 465     HIS I    -3                                                      
REMARK 465     HIS I    -2                                                      
REMARK 465     HIS I    -1                                                      
REMARK 465     HIS I     0                                                      
REMARK 465     MSE I     1                                                      
REMARK 465     LYS I   324                                                      
REMARK 465     GLY I   325                                                      
REMARK 465     MSE J   -11                                                      
REMARK 465     GLY J   -10                                                      
REMARK 465     SER J    -9                                                      
REMARK 465     ASP J    -8                                                      
REMARK 465     LYS J    -7                                                      
REMARK 465     ILE J    -6                                                      
REMARK 465     HIS J    -5                                                      
REMARK 465     HIS J    -4                                                      
REMARK 465     HIS J    -3                                                      
REMARK 465     HIS J    -2                                                      
REMARK 465     HIS J    -1                                                      
REMARK 465     HIS J     0                                                      
REMARK 465     MSE J     1                                                      
REMARK 465     LYS J   324                                                      
REMARK 465     GLY J   325                                                      
REMARK 465     MSE K   -11                                                      
REMARK 465     GLY K   -10                                                      
REMARK 465     SER K    -9                                                      
REMARK 465     ASP K    -8                                                      
REMARK 465     LYS K    -7                                                      
REMARK 465     ILE K    -6                                                      
REMARK 465     HIS K    -5                                                      
REMARK 465     HIS K    -4                                                      
REMARK 465     HIS K    -3                                                      
REMARK 465     HIS K    -2                                                      
REMARK 465     HIS K    -1                                                      
REMARK 465     HIS K     0                                                      
REMARK 465     MSE K     1                                                      
REMARK 465     LYS K   324                                                      
REMARK 465     GLY K   325                                                      
REMARK 465     MSE L   -11                                                      
REMARK 465     GLY L   -10                                                      
REMARK 465     SER L    -9                                                      
REMARK 465     ASP L    -8                                                      
REMARK 465     LYS L    -7                                                      
REMARK 465     ILE L    -6                                                      
REMARK 465     HIS L    -5                                                      
REMARK 465     HIS L    -4                                                      
REMARK 465     HIS L    -3                                                      
REMARK 465     HIS L    -2                                                      
REMARK 465     HIS L    -1                                                      
REMARK 465     HIS L     0                                                      
REMARK 465     MSE L     1                                                      
REMARK 465     LYS L   324                                                      
REMARK 465     GLY L   325                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   9    CG    CD    OE1   OE2                               
REMARK 470     LYS A  22    NZ                                                  
REMARK 470     GLU A  81    CD    OE1   OE2                                     
REMARK 470     GLU B   9    CD    OE1   OE2                                     
REMARK 470     GLU B  17    CD    OE1   OE2                                     
REMARK 470     LYS B  22    CD    CE    NZ                                      
REMARK 470     GLU B  79    CG    CD    OE1   OE2                               
REMARK 470     GLU B  81    CG    CD    OE1   OE2                               
REMARK 470     GLN B 222    CD    OE1   NE2                                     
REMARK 470     LYS C  22    CD    CE    NZ                                      
REMARK 470     LYS C 126    CE    NZ                                            
REMARK 470     ARG C 153    NE    CZ    NH1   NH2                               
REMARK 470     LYS D  22    CD    CE    NZ                                      
REMARK 470     GLU D  48    CD    OE1   OE2                                     
REMARK 470     GLU D  79    CB    CG    CD    OE1   OE2                         
REMARK 470     LYS D 126    CE    NZ                                            
REMARK 470     ARG D 153    NE    CZ    NH1   NH2                               
REMARK 470     GLU E   9    CD    OE1   OE2                                     
REMARK 470     LYS E  22    CD    CE    NZ                                      
REMARK 470     GLU F   9    CG    CD    OE1   OE2                               
REMARK 470     LYS F  22    CD    CE    NZ                                      
REMARK 470     GLU F  81    CG    CD    OE1   OE2                               
REMARK 470     LYS F 126    CE    NZ                                            
REMARK 470     LYS G  22    CD    CE    NZ                                      
REMARK 470     GLU G  79    CD    OE1   OE2                                     
REMARK 470     LYS G 126    CE    NZ                                            
REMARK 470     GLU H   9    CD    OE1   OE2                                     
REMARK 470     LYS H  22    CD    CE    NZ                                      
REMARK 470     GLU I  30    CD    OE1   OE2                                     
REMARK 470     GLU I  48    CD    OE1   OE2                                     
REMARK 470     GLU I  79    CD    OE1   OE2                                     
REMARK 470     LYS J  22    CG    CD    CE    NZ                                
REMARK 470     GLU J  30    CD    OE1   OE2                                     
REMARK 470     GLU J  79    CG    CD    OE1   OE2                               
REMARK 470     ARG J 153    NE    CZ    NH1   NH2                               
REMARK 470     GLU K   9    CG    CD    OE1   OE2                               
REMARK 470     LYS K  22    NZ                                                  
REMARK 470     GLU K  79    CD    OE1   OE2                                     
REMARK 470     LYS K 202    CE    NZ                                            
REMARK 470     LYS L 126    CE    NZ                                            
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                             
REMARK 500   OH   TYR H    19     OE2  GLU H    21              2.13            
REMARK 500   OE1  GLN H   176     O    HOH    2005              2.16            
REMARK 500   O    HOH     604     O    HOH    1162              2.16            
REMARK 500   O    HOH    2256     O    HOH    2304              2.18            
REMARK 500   OE1  GLU A    34     O    HOH    2381              2.19            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ALA A 164   CA    ALA A 164   CB    -0.109                        
REMARK 500    ASN E 302   CB    ASN E 302   CG     0.099                        
REMARK 500    VAL E 315   CB    VAL E 315   CG1    0.135                        
REMARK 500    LEU G  51   CG    LEU G  51   CD2    0.097                        
REMARK 500    ALA G 164   CA    ALA G 164   CB    -0.110                        
REMARK 500    ASN L 302   CB    ASN L 302   CG     0.099                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY D 135   N   -  CA  -  C   ANGL. DEV. =  9.8 DEGREES           
REMARK 500    LYS J 237   CD  -  CE  -  NZ  ANGL. DEV. = 10.7 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 188     -119.51     56.91                                   
REMARK 500    SER B 188     -117.62     57.15                                   
REMARK 500    SER C 188     -116.39     58.87                                   
REMARK 500    SER D 188     -119.48     60.26                                   
REMARK 500    SER E 188     -116.21     56.34                                   
REMARK 500    SER F 188     -117.96     58.20                                   
REMARK 500    SER G 188     -119.03     62.47                                   
REMARK 500    SER H 188     -118.45     56.48                                   
REMARK 500    SER J 188     -116.46     59.73                                   
REMARK 500    SER K 188     -118.08     56.72                                   
REMARK 500    SER L 188     -119.57     56.64                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA C    2    PHE C    3                  149.36                     
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH  1555        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH  1910        DISTANCE =  6.08 ANGSTROMS                       
DBREF  1VLQ A    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ B    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ C    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ D    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ E    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ F    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ G    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ H    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ I    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ J    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ K    1   325  GB     15642852 NP_227893        1    325             
DBREF  1VLQ L    1   325  GB     15642852 NP_227893        1    325             
SEQADV 1VLQ MSE A  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY A  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER A   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP A   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS A   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE A   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS A   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS A   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS A   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS A   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS A   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS A    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE A    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE A   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE A  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE A  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE A  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE A  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE B  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY B  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER B   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP B   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS B   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE B   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS B   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS B   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS B   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS B   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS B   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS B    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE B    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE B   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE B  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE B  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE B  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE B  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE C  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY C  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER C   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP C   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS C   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE C   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS C   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS C   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS C   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS C   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS C   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS C    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE C    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE C   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE C  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE C  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE C  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE C  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE D  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY D  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER D   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP D   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS D   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE D   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS D   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS D   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS D   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS D   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS D   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS D    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE D    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE D   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE D  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE D  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE D  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE D  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE E  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY E  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER E   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP E   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS E   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE E   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS E   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS E   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS E   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS E   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS E   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS E    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE E    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE E   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE E  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE E  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE E  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE E  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE F  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY F  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER F   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP F   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS F   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE F   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS F   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS F   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS F   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS F   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS F   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS F    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE F    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE F   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE F  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE F  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE F  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE F  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE G  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY G  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER G   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP G   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS G   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE G   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS G   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS G   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS G   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS G   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS G   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS G    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE G    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE G   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE G  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE G  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE G  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE G  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE H  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY H  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER H   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP H   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS H   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE H   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS H   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS H   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS H   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS H   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS H   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS H    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE H    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE H   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE H  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE H  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE H  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE H  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE I  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY I  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER I   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP I   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS I   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE I   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS I   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS I   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS I   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS I   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS I   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS I    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE I    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE I   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE I  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE I  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE I  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE I  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE J  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY J  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER J   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP J   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS J   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE J   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS J   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS J   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS J   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS J   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS J   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS J    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE J    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE J   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE J  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE J  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE J  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE J  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE K  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY K  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER K   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP K   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS K   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE K   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS K   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS K   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS K   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS K   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS K   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS K    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE K    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE K   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE K  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE K  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE K  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE K  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQADV 1VLQ MSE L  -11  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ GLY L  -10  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ SER L   -9  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ASP L   -8  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ LYS L   -7  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ ILE L   -6  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS L   -5  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS L   -4  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS L   -3  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS L   -2  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS L   -1  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ HIS L    0  GB   15642852            LEADER SEQUENCE                
SEQADV 1VLQ MSE L    1  GB   15642852  MET     1 MODIFIED RESIDUE               
SEQADV 1VLQ MSE L   47  GB   15642852  MET    47 MODIFIED RESIDUE               
SEQADV 1VLQ MSE L  108  GB   15642852  MET   108 MODIFIED RESIDUE               
SEQADV 1VLQ MSE L  115  GB   15642852  MET   115 MODIFIED RESIDUE               
SEQADV 1VLQ MSE L  145  GB   15642852  MET   145 MODIFIED RESIDUE               
SEQADV 1VLQ MSE L  273  GB   15642852  MET   273 MODIFIED RESIDUE               
SEQRES   1 A  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 A  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 A  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 A  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 A  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 A  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 A  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 A  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 A  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 A  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 A  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 A  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 A  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 A  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 A  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 A  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 A  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 A  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 A  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 A  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 A  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 A  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 A  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 A  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 A  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 A  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 B  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 B  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 B  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 B  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 B  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 B  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 B  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 B  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 B  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 B  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 B  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 B  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 B  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 B  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 B  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 B  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 B  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 B  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 B  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 B  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 B  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 B  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 B  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 B  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 B  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 B  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 C  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 C  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 C  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 C  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 C  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 C  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 C  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 C  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 C  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 C  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 C  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 C  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 C  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 C  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 C  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 C  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 C  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 C  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 C  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 C  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 C  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 C  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 C  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 C  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 C  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 C  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 D  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 D  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 D  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 D  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 D  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 D  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 D  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 D  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 D  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 D  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 D  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 D  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 D  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 D  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 D  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 D  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 D  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 D  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 D  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 D  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 D  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 D  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 D  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 D  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 D  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 D  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 E  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 E  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 E  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 E  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 E  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 E  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 E  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 E  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 E  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 E  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 E  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 E  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 E  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 E  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 E  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 E  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 E  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 E  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 E  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 E  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 E  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 E  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 E  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 E  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 E  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 E  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 F  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 F  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 F  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 F  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 F  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 F  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 F  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 F  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 F  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 F  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 F  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 F  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 F  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 F  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 F  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 F  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 F  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 F  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 F  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 F  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 F  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 F  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 F  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 F  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 F  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 F  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 G  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 G  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 G  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 G  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 G  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 G  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 G  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 G  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 G  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 G  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 G  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 G  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 G  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 G  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 G  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 G  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 G  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 G  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 G  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 G  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 G  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 G  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 G  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 G  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 G  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 G  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 H  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 H  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 H  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 H  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 H  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 H  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 H  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 H  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 H  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 H  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 H  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 H  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 H  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 H  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 H  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 H  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 H  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 H  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 H  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 H  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 H  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 H  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 H  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 H  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 H  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 H  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 I  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 I  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 I  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 I  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 I  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 I  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 I  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 I  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 I  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 I  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 I  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 I  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 I  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 I  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 I  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 I  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 I  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 I  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 I  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 I  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 I  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 I  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 I  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 I  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 I  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 I  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 J  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 J  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 J  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 J  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 J  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 J  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 J  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 J  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 J  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 J  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 J  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 J  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 J  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 J  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 J  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 J  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 J  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 J  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 J  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 J  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 J  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 J  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 J  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 J  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 J  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 J  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 K  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 K  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 K  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 K  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 K  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 K  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 K  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 K  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 K  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 K  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 K  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 K  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 K  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 K  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 K  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 K  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 K  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 K  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 K  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 K  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 K  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 K  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 K  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 K  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 K  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 K  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
SEQRES   1 L  337  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 L  337  ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR          
SEQRES   3 L  337  ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE          
SEQRES   4 L  337  TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU          
SEQRES   5 L  337  ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR          
SEQRES   6 L  337  VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY          
SEQRES   7 L  337  GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU          
SEQRES   8 L  337  GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR          
SEQRES   9 L  337  ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP          
SEQRES  10 L  337  PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG          
SEQRES  11 L  337  GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP          
SEQRES  12 L  337  TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE          
SEQRES  13 L  337  MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR          
SEQRES  14 L  337  ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA          
SEQRES  15 L  337  ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL          
SEQRES  16 L  337  ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA          
SEQRES  17 L  337  VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS          
SEQRES  18 L  337  ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN          
SEQRES  19 L  337  LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE          
SEQRES  20 L  337  LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG          
SEQRES  21 L  337  THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG          
SEQRES  22 L  337  ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP          
SEQRES  23 L  337  ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN          
SEQRES  24 L  337  TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR          
SEQRES  25 L  337  ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU          
SEQRES  26 L  337  GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY              
MODRES 1VLQ MSE A   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE A  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE A  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE A  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE A  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE B   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE B  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE B  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE B  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE B  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE C   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE C  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE C  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE C  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE C  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE D   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE D  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE D  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE D  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE D  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE E   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE E  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE E  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE E  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE E  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE F   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE F  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE F  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE F  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE F  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE G   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE G  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE G  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE G  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE G  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE H   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE H  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE H  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE H  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE H  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE I   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE I  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE I  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE I  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE I  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE J   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE J  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE J  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE J  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE J  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE K   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE K  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE K  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE K  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE K  273  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE L   47  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE L  108  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE L  115  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE L  145  MET  SELENOMETHIONINE                                   
MODRES 1VLQ MSE L  273  MET  SELENOMETHIONINE                                   
HET    MSE  A  47       8                                                       
HET    MSE  A 108       8                                                       
HET    MSE  A 115       8                                                       
HET    MSE  A 145       8                                                       
HET    MSE  A 273       8                                                       
HET    MSE  B  47       8                                                       
HET    MSE  B 108       8                                                       
HET    MSE  B 115       8                                                       
HET    MSE  B 145       8                                                       
HET    MSE  B 273       8                                                       
HET    MSE  C  47       8                                                       
HET    MSE  C 108       8                                                       
HET    MSE  C 115       8                                                       
HET    MSE  C 145       8                                                       
HET    MSE  C 273       8                                                       
HET    MSE  D  47       8                                                       
HET    MSE  D 108       8                                                       
HET    MSE  D 115       8                                                       
HET    MSE  D 145       8                                                       
HET    MSE  D 273       8                                                       
HET    MSE  E  47       8                                                       
HET    MSE  E 108       8                                                       
HET    MSE  E 115       8                                                       
HET    MSE  E 145       8                                                       
HET    MSE  E 273       8                                                       
HET    MSE  F  47       8                                                       
HET    MSE  F 108       8                                                       
HET    MSE  F 115       8                                                       
HET    MSE  F 145       8                                                       
HET    MSE  F 273       8                                                       
HET    MSE  G  47       8                                                       
HET    MSE  G 108       8                                                       
HET    MSE  G 115       8                                                       
HET    MSE  G 145       8                                                       
HET    MSE  G 273       8                                                       
HET    MSE  H  47       8                                                       
HET    MSE  H 108       8                                                       
HET    MSE  H 115       8                                                       
HET    MSE  H 145       8                                                       
HET    MSE  H 273       8                                                       
HET    MSE  I  47       8                                                       
HET    MSE  I 108       8                                                       
HET    MSE  I 115       8                                                       
HET    MSE  I 145       8                                                       
HET    MSE  I 273       8                                                       
HET    MSE  J  47       8                                                       
HET    MSE  J 108       8                                                       
HET    MSE  J 115       8                                                       
HET    MSE  J 145       8                                                       
HET    MSE  J 273       8                                                       
HET    MSE  K  47       8                                                       
HET    MSE  K 108       8                                                       
HET    MSE  K 115       8                                                       
HET    MSE  K 145       8                                                       
HET    MSE  K 273       8                                                       
HET    MSE  L  47       8                                                       
HET    MSE  L 108       8                                                       
HET    MSE  L 115       8                                                       
HET    MSE  L 145       8                                                       
HET    MSE  L 273       8                                                       
HET    GOL      1       6                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
FORMUL   1  MSE    60(C5 H11 N1 O2 SE1)                                         
FORMUL  13  GOL    C3 H8 O3                                                     
FORMUL  14  HOH   *2464(H2 O1)                                                  
HELIX    1   1 PRO A    7  LYS A   12  1                                   6    
HELIX    2   2 ASP A   23  LYS A   37  1                                  15    
HELIX    3   3 TYR A   64  GLY A   66  5                                   3    
HELIX    4   4 PHE A   98  TRP A  102  5                                   5    
HELIX    5   5 LEU A  103  MSE A  108  1                                   6    
HELIX    6   6 TYR A  155  SER A  173  1                                  19    
HELIX    7   7 SER A  188  SER A  201  1                                  14    
HELIX    8   8 HIS A  216  VAL A  224  1                                   9    
HELIX    9   9 PRO A  228  HIS A  239  1                                  12    
HELIX   10  10 LYS A  242  TYR A  252  1                                  11    
HELIX   11  11 ASP A  254  ALA A  260  1                                   7    
HELIX   12  12 PRO A  278  TYR A  289  1                                  12    
HELIX   13  13 GLY A  306  GLU A  323  1                                  18    
HELIX   14  14 PRO B    7  LYS B   12  1                                   6    
HELIX   15  15 ASP B   23  LYS B   37  1                                  15    
HELIX   16  16 TYR B   64  GLY B   66  5                                   3    
HELIX   17  17 PHE B   98  TRP B  102  5                                   5    
HELIX   18  18 LEU B  103  MSE B  108  1                                   6    
HELIX   19  19 ASP B  151  THR B  154  5                                   4    
HELIX   20  20 TYR B  155  SER B  173  1                                  19    
HELIX   21  21 SER B  188  SER B  201  1                                  14    
HELIX   22  22 HIS B  216  VAL B  224  1                                   9    
HELIX   23  23 PRO B  228  HIS B  239  1                                  12    
HELIX   24  24 LYS B  242  TYR B  252  1                                  11    
HELIX   25  25 ASP B  254  ALA B  260  1                                   7    
HELIX   26  26 PRO B  278  TYR B  289  1                                  12    
HELIX   27  27 GLY B  306  PHE B  322  1                                  17    
HELIX   28  28 PRO C    7  LYS C   12  1                                   6    
HELIX   29  29 ASP C   23  LYS C   37  1                                  15    
HELIX   30  30 TYR C   64  GLY C   66  5                                   3    
HELIX   31  31 PHE C   98  TRP C  102  5                                   5    
HELIX   32  32 LEU C  103  MSE C  108  1                                   6    
HELIX   33  33 ASP C  151  THR C  154  5                                   4    
HELIX   34  34 TYR C  155  SER C  173  1                                  19    
HELIX   35  35 SER C  188  SER C  201  1                                  14    
HELIX   36  36 HIS C  216  VAL C  224  1                                   9    
HELIX   37  37 TYR C  229  HIS C  239  1                                  11    
HELIX   38  38 LYS C  242  TYR C  252  1                                  11    
HELIX   39  39 ASP C  254  ALA C  260  1                                   7    
HELIX   40  40 PRO C  278  TYR C  289  1                                  12    
HELIX   41  41 GLY C  306  PHE C  322  1                                  17    
HELIX   42  42 PRO D    7  LYS D   12  1                                   6    
HELIX   43  43 ASP D   23  LYS D   37  1                                  15    
HELIX   44  44 TYR D   64  GLY D   66  5                                   3    
HELIX   45  45 PHE D   98  TRP D  102  5                                   5    
HELIX   46  46 LEU D  103  MSE D  108  1                                   6    
HELIX   47  47 TYR D  155  SER D  173  1                                  19    
HELIX   48  48 SER D  188  SER D  201  1                                  14    
HELIX   49  49 HIS D  216  VAL D  224  1                                   9    
HELIX   50  50 PRO D  228  HIS D  239  1                                  12    
HELIX   51  51 LYS D  242  TYR D  252  1                                  11    
HELIX   52  52 ASP D  254  ALA D  260  1                                   7    
HELIX   53  53 PRO D  278  TYR D  289  1                                  12    
HELIX   54  54 GLY D  306  GLU D  323  1                                  18    
HELIX   55  55 PRO E    7  LYS E   12  1                                   6    
HELIX   56  56 ASP E   23  LYS E   37  1                                  15    
HELIX   57  57 TYR E   64  GLY E   66  5                                   3    
HELIX   58  58 PHE E   98  TRP E  102  5                                   5    
HELIX   59  59 LEU E  103  MSE E  108  1                                   6    
HELIX   60  60 ASP E  151  THR E  154  5                                   4    
HELIX   61  61 TYR E  155  SER E  173  1                                  19    
HELIX   62  62 SER E  188  SER E  201  1                                  14    
HELIX   63  63 HIS E  216  VAL E  224  1                                   9    
HELIX   64  64 PRO E  228  HIS E  239  1                                  12    
HELIX   65  65 LYS E  242  TYR E  252  1                                  11    
HELIX   66  66 ASP E  254  ALA E  260  1                                   7    
HELIX   67  67 PRO E  278  TYR E  289  1                                  12    
HELIX   68  68 GLY E  306  GLU E  323  1                                  18    
HELIX   69  69 PRO F    7  LYS F   12  1                                   6    
HELIX   70  70 ASP F   23  LYS F   37  1                                  15    
HELIX   71  71 TYR F   64  GLY F   66  5                                   3    
HELIX   72  72 PHE F   98  TRP F  102  5                                   5    
HELIX   73  73 LEU F  103  MSE F  108  1                                   6    
HELIX   74  74 ASP F  151  THR F  154  5                                   4    
HELIX   75  75 TYR F  155  SER F  173  1                                  19    
HELIX   76  76 SER F  188  SER F  201  1                                  14    
HELIX   77  77 HIS F  216  VAL F  224  1                                   9    
HELIX   78  78 PRO F  228  HIS F  239  1                                  12    
HELIX   79  79 LYS F  242  TYR F  252  1                                  11    
HELIX   80  80 ASP F  254  ALA F  260  1                                   7    
HELIX   81  81 PRO F  278  TYR F  289  1                                  12    
HELIX   82  82 GLY F  306  PHE F  322  1                                  17    
HELIX   83  83 PRO G    7  LYS G   12  1                                   6    
HELIX   84  84 ASP G   23  LYS G   37  1                                  15    
HELIX   85  85 TYR G   64  GLY G   66  5                                   3    
HELIX   86  86 PHE G   98  TRP G  102  5                                   5    
HELIX   87  87 LEU G  103  MSE G  108  1                                   6    
HELIX   88  88 ASP G  151  THR G  154  5                                   4    
HELIX   89  89 TYR G  155  SER G  173  1                                  19    
HELIX   90  90 SER G  188  SER G  201  1                                  14    
HELIX   91  91 HIS G  216  VAL G  224  1                                   9    
HELIX   92  92 TYR G  229  HIS G  239  1                                  11    
HELIX   93  93 LYS G  242  TYR G  252  1                                  11    
HELIX   94  94 ASP G  254  ALA G  260  1                                   7    
HELIX   95  95 PRO G  278  TYR G  289  1                                  12    
HELIX   96  96 GLY G  306  GLU G  323  1                                  18    
HELIX   97  97 PRO H    7  LYS H   12  1                                   6    
HELIX   98  98 ASP H   23  LYS H   37  1                                  15    
HELIX   99  99 TYR H   64  GLY H   66  5                                   3    
HELIX  100 100 PHE H   98  TRP H  102  5                                   5    
HELIX  101 101 LEU H  103  MSE H  108  1                                   6    
HELIX  102 102 ASP H  151  THR H  154  5                                   4    
HELIX  103 103 TYR H  155  SER H  173  1                                  19    
HELIX  104 104 SER H  188  SER H  201  1                                  14    
HELIX  105 105 HIS H  216  VAL H  224  1                                   9    
HELIX  106 106 PRO H  228  HIS H  239  1                                  12    
HELIX  107 107 LYS H  242  TYR H  252  1                                  11    
HELIX  108 108 ASP H  254  ALA H  260  1                                   7    
HELIX  109 109 PRO H  278  TYR H  289  1                                  12    
HELIX  110 110 GLY H  306  GLU H  323  1                                  18    
HELIX  111 111 PRO I    7  LYS I   12  1                                   6    
HELIX  112 112 ASP I   23  LYS I   37  1                                  15    
HELIX  113 113 TYR I   64  GLY I   66  5                                   3    
HELIX  114 114 PHE I   98  TRP I  102  5                                   5    
HELIX  115 115 LEU I  103  MSE I  108  1                                   6    
HELIX  116 116 TYR I  155  SER I  173  1                                  19    
HELIX  117 117 SER I  188  SER I  201  1                                  14    
HELIX  118 118 HIS I  216  VAL I  224  1                                   9    
HELIX  119 119 PRO I  228  HIS I  239  1                                  12    
HELIX  120 120 LYS I  242  TYR I  252  1                                  11    
HELIX  121 121 ASP I  254  ALA I  260  1                                   7    
HELIX  122 122 PRO I  278  TYR I  289  1                                  12    
HELIX  123 123 GLY I  306  PHE I  322  1                                  17    
HELIX  124 124 PRO J    7  LYS J   12  1                                   6    
HELIX  125 125 ASP J   23  LYS J   37  1                                  15    
HELIX  126 126 TYR J   64  GLY J   66  5                                   3    
HELIX  127 127 PHE J   98  TRP J  102  5                                   5    
HELIX  128 128 LEU J  103  MSE J  108  1                                   6    
HELIX  129 129 ASP J  151  THR J  154  5                                   4    
HELIX  130 130 TYR J  155  SER J  173  1                                  19    
HELIX  131 131 SER J  188  SER J  201  1                                  14    
HELIX  132 132 HIS J  216  VAL J  224  1                                   9    
HELIX  133 133 PRO J  228  HIS J  239  1                                  12    
HELIX  134 134 LYS J  242  TYR J  252  1                                  11    
HELIX  135 135 ASP J  254  ALA J  260  1                                   7    
HELIX  136 136 PRO J  278  TYR J  289  1                                  12    
HELIX  137 137 GLY J  306  PHE J  322  1                                  17    
HELIX  138 138 PRO K    7  LYS K   12  1                                   6    
HELIX  139 139 ASP K   23  LYS K   37  1                                  15    
HELIX  140 140 TYR K   64  GLY K   66  5                                   3    
HELIX  141 141 PHE K   98  TRP K  102  5                                   5    
HELIX  142 142 LEU K  103  MSE K  108  1                                   6    
HELIX  143 143 ASP K  151  THR K  154  5                                   4    
HELIX  144 144 TYR K  155  SER K  173  1                                  19    
HELIX  145 145 SER K  188  SER K  201  1                                  14    
HELIX  146 146 HIS K  216  VAL K  224  1                                   9    
HELIX  147 147 PRO K  228  HIS K  239  1                                  12    
HELIX  148 148 LYS K  242  TYR K  252  1                                  11    
HELIX  149 149 ASP K  254  ALA K  260  1                                   7    
HELIX  150 150 PRO K  278  TYR K  289  1                                  12    
HELIX  151 151 GLY K  306  GLU K  323  1                                  18    
HELIX  152 152 PRO L    7  LYS L   12  1                                   6    
HELIX  153 153 ASP L   23  LYS L   37  1                                  15    
HELIX  154 154 TYR L   64  GLY L   66  5                                   3    
HELIX  155 155 PHE L   98  TRP L  102  5                                   5    
HELIX  156 156 LEU L  103  MSE L  108  1                                   6    
HELIX  157 157 ASP L  151  THR L  154  5                                   4    
HELIX  158 158 TYR L  155  SER L  173  1                                  19    
HELIX  159 159 SER L  188  SER L  201  1                                  14    
HELIX  160 160 HIS L  216  VAL L  224  1                                   9    
HELIX  161 161 PRO L  228  HIS L  239  1                                  12    
HELIX  162 162 LYS L  242  TYR L  252  1                                  11    
HELIX  163 163 ASP L  254  ALA L  260  1                                   7    
HELIX  164 164 PRO L  278  TYR L  289  1                                  12    
HELIX  165 165 GLY L  306  GLU L  323  1                                  18    
SHEET    1   A 9 VAL A  43  ARG A  46  0                                        
SHEET    2   A 9 VAL A  54  SER A  62 -1  O  THR A  60   N  VAL A  43           
SHEET    3   A 9 ARG A  68  PRO A  76 -1  O  VAL A  75   N  GLU A  55           
SHEET    4   A 9 ILE A 111  MSE A 115 -1  O  VAL A 114   N  TRP A  72           
SHEET    5   A 9 LEU A  83  GLN A  88  1  N  VAL A  86   O  ILE A 111           
SHEET    6   A 9 VAL A 177  GLY A 187  1  O  VAL A 183   N  VAL A  87           
SHEET    7   A 9 ALA A 206  ASP A 210  1  O  ALA A 206   N  ILE A 184           
SHEET    8   A 9 ALA A 266  GLY A 271  1  O  LEU A 267   N  LEU A 207           
SHEET    9   A 9 LYS A 293  TYR A 298  1  O  GLU A 294   N  PHE A 268           
SHEET    1   B 9 VAL B  43  ARG B  46  0                                        
SHEET    2   B 9 VAL B  54  SER B  62 -1  O  THR B  60   N  VAL B  43           
SHEET    3   B 9 ARG B  68  PRO B  76 -1  O  VAL B  75   N  GLU B  55           
SHEET    4   B 9 ILE B 111  MSE B 115 -1  O  VAL B 114   N  TRP B  72           
SHEET    5   B 9 LEU B  83  GLN B  88  1  N  GLN B  88   O  PHE B 113           
SHEET    6   B 9 VAL B 177  GLY B 187  1  O  VAL B 183   N  CYS B  85           
SHEET    7   B 9 ALA B 206  ASP B 210  1  O  ALA B 206   N  ILE B 184           
SHEET    8   B 9 ALA B 266  GLY B 271  1  O  LEU B 267   N  CYS B 209           
SHEET    9   B 9 LYS B 293  TYR B 298  1  O  GLU B 294   N  PHE B 268           
SHEET    1   C 9 VAL C  43  ARG C  46  0                                        
SHEET    2   C 9 VAL C  54  SER C  62 -1  O  THR C  60   N  VAL C  43           
SHEET    3   C 9 ARG C  68  PRO C  76 -1  O  VAL C  75   N  GLU C  55           
SHEET    4   C 9 ILE C 111  MSE C 115 -1  O  VAL C 114   N  TRP C  72           
SHEET    5   C 9 LEU C  83  GLN C  88  1  N  VAL C  86   O  ILE C 111           
SHEET    6   C 9 VAL C 177  GLY C 187  1  O  VAL C 183   N  VAL C  87           
SHEET    7   C 9 ALA C 206  ASP C 210  1  O  ALA C 206   N  ILE C 184           
SHEET    8   C 9 ALA C 266  GLY C 271  1  O  LEU C 267   N  LEU C 207           
SHEET    9   C 9 LYS C 293  TYR C 298  1  O  GLU C 294   N  PHE C 268           
SHEET    1   D 9 VAL D  43  ARG D  46  0                                        
SHEET    2   D 9 VAL D  54  SER D  62 -1  O  THR D  60   N  VAL D  43           
SHEET    3   D 9 ARG D  68  PRO D  76 -1  O  ILE D  69   N  PHE D  61           
SHEET    4   D 9 ILE D 111  MSE D 115 -1  O  VAL D 114   N  TRP D  72           
SHEET    5   D 9 LEU D  83  GLN D  88  1  N  VAL D  86   O  ILE D 111           
SHEET    6   D 9 VAL D 177  GLY D 187  1  O  VAL D 183   N  VAL D  87           
SHEET    7   D 9 ALA D 206  ASP D 210  1  O  ALA D 206   N  ILE D 184           
SHEET    8   D 9 ALA D 266  GLY D 271  1  O  LEU D 267   N  LEU D 207           
SHEET    9   D 9 LYS D 293  TYR D 298  1  O  GLU D 294   N  PHE D 268           
SHEET    1   E 9 VAL E  43  ARG E  46  0                                        
SHEET    2   E 9 VAL E  54  SER E  62 -1  O  THR E  60   N  VAL E  43           
SHEET    3   E 9 ARG E  68  PRO E  76 -1  O  VAL E  75   N  GLU E  55           
SHEET    4   E 9 ILE E 111  MSE E 115 -1  O  VAL E 114   N  TRP E  72           
SHEET    5   E 9 LEU E  83  GLN E  88  1  N  GLN E  88   O  PHE E 113           
SHEET    6   E 9 VAL E 177  GLY E 187  1  O  VAL E 183   N  CYS E  85           
SHEET    7   E 9 ALA E 206  ASP E 210  1  O  LEU E 208   N  ILE E 184           
SHEET    8   E 9 ALA E 266  GLY E 271  1  O  LEU E 267   N  CYS E 209           
SHEET    9   E 9 LYS E 293  TYR E 298  1  O  GLU E 294   N  PHE E 268           
SHEET    1   F 9 VAL F  43  ARG F  46  0                                        
SHEET    2   F 9 VAL F  54  SER F  62 -1  O  THR F  60   N  VAL F  43           
SHEET    3   F 9 ARG F  68  PRO F  76 -1  O  ILE F  69   N  PHE F  61           
SHEET    4   F 9 ILE F 111  MSE F 115 -1  O  VAL F 114   N  TRP F  72           
SHEET    5   F 9 LEU F  83  GLN F  88  1  N  GLN F  88   O  PHE F 113           
SHEET    6   F 9 VAL F 177  GLY F 187  1  O  VAL F 183   N  CYS F  85           
SHEET    7   F 9 ALA F 206  ASP F 210  1  O  LEU F 208   N  ILE F 184           
SHEET    8   F 9 ALA F 266  GLY F 271  1  O  LEU F 267   N  CYS F 209           
SHEET    9   F 9 LYS F 293  TYR F 298  1  O  GLU F 294   N  PHE F 268           
SHEET    1   G 9 VAL G  43  ARG G  46  0                                        
SHEET    2   G 9 VAL G  54  SER G  62 -1  O  THR G  60   N  VAL G  43           
SHEET    3   G 9 ARG G  68  PRO G  76 -1  O  VAL G  75   N  GLU G  55           
SHEET    4   G 9 ILE G 111  MSE G 115 -1  O  VAL G 114   N  TRP G  72           
SHEET    5   G 9 LEU G  83  GLN G  88  1  N  VAL G  86   O  ILE G 111           
SHEET    6   G 9 VAL G 177  GLY G 187  1  O  VAL G 183   N  VAL G  87           
SHEET    7   G 9 ALA G 206  ASP G 210  1  O  ALA G 206   N  ILE G 184           
SHEET    8   G 9 ALA G 266  GLY G 271  1  O  LEU G 267   N  LEU G 207           
SHEET    9   G 9 LYS G 293  TYR G 298  1  O  GLU G 294   N  PHE G 268           
SHEET    1   H 9 VAL H  43  ARG H  46  0                                        
SHEET    2   H 9 VAL H  54  SER H  62 -1  O  THR H  60   N  VAL H  43           
SHEET    3   H 9 ARG H  68  PRO H  76 -1  O  VAL H  75   N  GLU H  55           
SHEET    4   H 9 ILE H 111  MSE H 115 -1  O  VAL H 114   N  TRP H  72           
SHEET    5   H 9 LEU H  83  GLN H  88  1  N  GLN H  88   O  PHE H 113           
SHEET    6   H 9 VAL H 177  GLY H 187  1  O  VAL H 183   N  VAL H  87           
SHEET    7   H 9 ALA H 206  ASP H 210  1  O  ALA H 206   N  ILE H 184           
SHEET    8   H 9 ALA H 266  GLY H 271  1  O  LEU H 267   N  CYS H 209           
SHEET    9   H 9 LYS H 293  TYR H 298  1  O  GLU H 294   N  PHE H 268           
SHEET    1   I 9 VAL I  43  ARG I  46  0                                        
SHEET    2   I 9 VAL I  54  SER I  62 -1  O  THR I  60   N  VAL I  43           
SHEET    3   I 9 ARG I  68  PRO I  76 -1  O  VAL I  75   N  GLU I  55           
SHEET    4   I 9 ILE I 111  MSE I 115 -1  O  VAL I 114   N  TRP I  72           
SHEET    5   I 9 LEU I  83  GLN I  88  1  N  GLN I  88   O  PHE I 113           
SHEET    6   I 9 VAL I 177  GLY I 187  1  O  VAL I 183   N  VAL I  87           
SHEET    7   I 9 ALA I 206  ASP I 210  1  O  ALA I 206   N  ILE I 184           
SHEET    8   I 9 ALA I 266  GLY I 271  1  O  LEU I 267   N  LEU I 207           
SHEET    9   I 9 LYS I 293  TYR I 298  1  O  GLU I 294   N  PHE I 268           
SHEET    1   J 9 VAL J  43  ARG J  46  0                                        
SHEET    2   J 9 VAL J  54  SER J  62 -1  O  THR J  60   N  VAL J  43           
SHEET    3   J 9 ARG J  68  PRO J  76 -1  O  VAL J  75   N  GLU J  55           
SHEET    4   J 9 ILE J 111  MSE J 115 -1  O  VAL J 114   N  TRP J  72           
SHEET    5   J 9 LEU J  83  GLN J  88  1  N  VAL J  86   O  ILE J 111           
SHEET    6   J 9 VAL J 177  GLY J 187  1  O  VAL J 183   N  CYS J  85           
SHEET    7   J 9 ALA J 206  ASP J 210  1  O  ALA J 206   N  ILE J 184           
SHEET    8   J 9 ALA J 266  GLY J 271  1  O  LEU J 267   N  CYS J 209           
SHEET    9   J 9 LYS J 293  TYR J 298  1  O  GLU J 294   N  PHE J 268           
SHEET    1   K 9 VAL K  43  ARG K  46  0                                        
SHEET    2   K 9 VAL K  54  SER K  62 -1  O  THR K  60   N  VAL K  43           
SHEET    3   K 9 ARG K  68  PRO K  76 -1  O  VAL K  75   N  GLU K  55           
SHEET    4   K 9 ILE K 111  MSE K 115 -1  O  VAL K 114   N  TRP K  72           
SHEET    5   K 9 LEU K  83  GLN K  88  1  N  VAL K  86   O  ILE K 111           
SHEET    6   K 9 VAL K 177  GLY K 187  1  O  VAL K 183   N  VAL K  87           
SHEET    7   K 9 ALA K 206  ASP K 210  1  O  ALA K 206   N  ILE K 184           
SHEET    8   K 9 ALA K 266  GLY K 271  1  O  LEU K 267   N  CYS K 209           
SHEET    9   K 9 LYS K 293  TYR K 298  1  O  GLU K 294   N  PHE K 268           
SHEET    1   L 9 VAL L  43  ARG L  46  0                                        
SHEET    2   L 9 VAL L  54  SER L  62 -1  O  THR L  60   N  VAL L  43           
SHEET    3   L 9 ARG L  68  PRO L  76 -1  O  VAL L  75   N  GLU L  55           
SHEET    4   L 9 ILE L 111  MSE L 115 -1  O  VAL L 114   N  TRP L  72           
SHEET    5   L 9 LEU L  83  TYR L  89  1  N  GLN L  88   O  PHE L 113           
SHEET    6   L 9 VAL L 177  GLY L 187  1  O  VAL L 183   N  CYS L  85           
SHEET    7   L 9 ALA L 206  ASP L 210  1  O  ALA L 206   N  ILE L 184           
SHEET    8   L 9 ALA L 266  GLY L 271  1  O  LEU L 267   N  LEU L 207           
SHEET    9   L 9 LYS L 293  TYR L 298  1  O  GLU L 294   N  PHE L 268           
CISPEP   1 HIS A  227    PRO A  228          0         4.70                     
CISPEP   2 HIS B  227    PRO B  228          0         4.27                     
CISPEP   3 HIS C  227    PRO C  228          0         2.79                     
CISPEP   4 HIS D  227    PRO D  228          0         2.25                     
CISPEP   5 HIS E  227    PRO E  228          0         1.81                     
CISPEP   6 HIS F  227    PRO F  228          0         4.95                     
CISPEP   7 HIS G  227    PRO G  228          0        -1.51                     
CISPEP   8 HIS H  227    PRO H  228          0         1.92                     
CISPEP   9 HIS I  227    PRO I  228          0         6.91                     
CISPEP  10 HIS J  227    PRO J  228          0         4.47                     
CISPEP  11 HIS K  227    PRO K  228          0        -2.10                     
CISPEP  12 HIS L  227    PRO L  228          0         1.88                     
CRYST1  152.640  130.952  157.815  90.00 118.93  90.00 P 1 21 1     24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006551  0.000000  0.003621        0.00000                         
SCALE2      0.000000  0.007636  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007240        0.00000                         
TER    2605      GLU A 323                                                      
TER    5194      GLU B 323                                                      
TER    7794      GLU C 323                                                      
TER   10386      GLU D 323                                                      
TER   12989      GLU E 323                                                      
TER   15585      GLU F 323                                                      
TER   18186      GLU G 323                                                      
TER   20789      GLU H 323                                                      
TER   23389      GLU I 323                                                      
TER   25986      GLU J 323                                                      
TER   28585      GLU K 323                                                      
TER   31195      GLU L 323                                                      
MASTER      619    0   61  165  108    0    0    633653   12  486  312          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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