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Database: PDB
Entry: 1B30
LinkDB: 1B30
Original site: 1B30 
HEADER    FAMILY 10 XYLANASE                      15-DEC-98   1B30              
TITLE     XYLANASE FROM PENICILLIUM SIMPLICISSIMUM, COMPLEX WITH 1,2-           
TITLE    2 (4-DEOXY-BETA-L-THREO-HEX-4-ENOPYRANOSYLURONIC ACID)-BETA-           
TITLE    3 1,4-XYLOTRIOSE)                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (XYLANASE);                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.8                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PENICILLIUM SIMPLICISSIMUM;                     
SOURCE   3 ORGANISM_TAXID: 69488;                                               
SOURCE   4 CELLULAR_LOCATION: SECRETED;                                         
SOURCE   5 OTHER_DETAILS: PENICILLIUM SIMPLICISSIMUM (OUDEM.) THOM.             
KEYWDS    FAMILY 10 XYLANASE, PENICILLIUM SIMPLICISSIMUM, GLYCOSYL              
KEYWDS   2 HYDROLASE, SUBSTRATE BINDING                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SCHMIDT,C.KRATKY                                                    
REVDAT   3   24-FEB-09 1B30    1       VERSN                                    
REVDAT   2   01-APR-03 1B30    1       JRNL                                     
REVDAT   1   31-MAR-99 1B30    0                                                
JRNL        AUTH   A.SCHMIDT,G.M.GUBITZ,C.KRATKY                                
JRNL        TITL   XYLAN BINDING SUBSITE MAPPING IN THE XYLANASE FROM           
JRNL        TITL 2 PENICILLIUM SIMPLICISSIMUM USING                             
JRNL        TITL 3 XYLOOLIGOSACCHARIDES AS CRYO-PROTECTANT.                     
JRNL        REF    BIOCHEMISTRY                  V.  38  2403 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10029534                                                     
JRNL        DOI    10.1021/BI982108L                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.SCHMIDT,A.SCHLACHER,W.STEINER,H.SCHWAB,C.KRATKY            
REMARK   1  TITL   STRUCTURE OF THE XYLANASE FROM PENICILLIUM                   
REMARK   1  TITL 2 SIMPLICISSIMUM                                               
REMARK   1  REF    PROTEIN SCI.                  V.   7  2081 1998              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20821                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R THROUGHOUT               
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2070                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.35                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2400                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 248                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2304                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 245                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM.PYQ                                      
REMARK   3  PARAMETER FILE  3  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  4  : PARAM3.CHO                                     
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOP.XYS_MONO                                   
REMARK   3  TOPOLOGY FILE  4   : TOP.PYQ                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PARAMETER/TOPOLOGY FILES FOR HET          
REMARK   3  GROUPS EXCEPT WATER SELF-SETUP                                      
REMARK   4                                                                      
REMARK   4 1B30 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-98.                  
REMARK 100 THE RCSB ID CODE IS RCSB000280.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : SIEMENS                            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20885                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BG4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION CONDITIONS: PROTEIN      
REMARK 280  WAS CRYSTALLIZED FROM 1.9M (NH4)2SO4, 0.1M TRISHCL PH 8.4 AT 4      
REMARK 280  C                                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.72333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       75.44667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       75.44667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.72333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  18   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  48      -23.04   -146.56                                   
REMARK 500    LEU A 177       49.08   -105.95                                   
REMARK 500    PRO A 201       74.13    -69.34                                   
REMARK 500    GLU A 238       55.30   -142.81                                   
REMARK 500    VAL A 270      -60.98   -101.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 518        DISTANCE =  6.05 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 XYLOSE UNITS 548, 549, 550 BETA-1,4 LINKED                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE.                                       
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 548                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 549                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 550                 
DBREF  1B30 A    1   302  GB     3220253  AF070417         1    302             
SEQADV 1B30 PCA A    1  GB   3220253   GLN     1 MODIFIED RESIDUE               
SEQRES   1 A  302  PCA ALA SER VAL SER ILE ASP ALA LYS PHE LYS ALA HIS          
SEQRES   2 A  302  GLY LYS LYS TYR LEU GLY THR ILE GLY ASP GLN TYR THR          
SEQRES   3 A  302  LEU THR LYS ASN THR LYS ASN PRO ALA ILE ILE LYS ALA          
SEQRES   4 A  302  ASP PHE GLY GLN LEU THR PRO GLU ASN SER MET LYS TRP          
SEQRES   5 A  302  ASP ALA THR GLU PRO ASN ARG GLY GLN PHE THR PHE SER          
SEQRES   6 A  302  GLY SER ASP TYR LEU VAL ASN PHE ALA GLN SER ASN GLY          
SEQRES   7 A  302  LYS LEU ILE ARG GLY HIS THR LEU VAL TRP HIS SER GLN          
SEQRES   8 A  302  LEU PRO GLY TRP VAL SER SER ILE THR ASP LYS ASN THR          
SEQRES   9 A  302  LEU ILE SER VAL LEU LYS ASN HIS ILE THR THR VAL MET          
SEQRES  10 A  302  THR ARG TYR LYS GLY LYS ILE TYR ALA TRP ASP VAL LEU          
SEQRES  11 A  302  ASN GLU ILE PHE ASN GLU ASP GLY SER LEU ARG ASN SER          
SEQRES  12 A  302  VAL PHE TYR ASN VAL ILE GLY GLU ASP TYR VAL ARG ILE          
SEQRES  13 A  302  ALA PHE GLU THR ALA ARG SER VAL ASP PRO ASN ALA LYS          
SEQRES  14 A  302  LEU TYR ILE ASN ASP TYR ASN LEU ASP SER ALA GLY TYR          
SEQRES  15 A  302  SER LYS VAL ASN GLY MET VAL SER HIS VAL LYS LYS TRP          
SEQRES  16 A  302  LEU ALA ALA GLY ILE PRO ILE ASP GLY ILE GLY SER GLN          
SEQRES  17 A  302  THR HIS LEU GLY ALA GLY ALA GLY SER ALA VAL ALA GLY          
SEQRES  18 A  302  ALA LEU ASN ALA LEU ALA SER ALA GLY THR LYS GLU ILE          
SEQRES  19 A  302  ALA ILE THR GLU LEU ASP ILE ALA GLY ALA SER SER THR          
SEQRES  20 A  302  ASP TYR VAL ASN VAL VAL ASN ALA CYS LEU ASN GLN ALA          
SEQRES  21 A  302  LYS CYS VAL GLY ILE THR VAL TRP GLY VAL ALA ASP PRO          
SEQRES  22 A  302  ASP SER TRP ARG SER SER SER SER PRO LEU LEU PHE ASP          
SEQRES  23 A  302  GLY ASN TYR ASN PRO LYS ALA ALA TYR ASN ALA ILE ALA          
SEQRES  24 A  302  ASN ALA LEU                                                  
MODRES 1B30 PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    XYP  A 548       9                                                       
HET    XYP  A 549       9                                                       
HET    XYP  A 550      10                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  XYP    3(C5 H10 O5)                                                 
FORMUL   3  HOH   *245(H2 O)                                                    
HELIX    1 A12 SER A    5  ALA A   12  1SEE REMARK 650                     8    
HELIX    2  B1 GLN A   24  LYS A   29  1                                   6    
HELIX    3   B LYS A   32  ASP A   40  1                                   9    
HELIX    4  C1 TRP A   52  GLU A   56  1                                   5    
HELIX    5   C SER A   65  SER A   76  1                                  12    
HELIX    6  D1 GLY A   94  SER A   97  1                                   4    
HELIX    7   D LYS A  102  ARG A  119  1                                  18    
HELIX    8  E1 SER A  143  GLU A  151  1                                   9    
HELIX    9   E ASP A  152  VAL A  164  1                                  13    
HELIX   10   F TYR A  182  ALA A  197  1                                  16    
HELIX   11   G VAL A  219  ALA A  225  1                                   7    
HELIX   12   H SER A  246  LEU A  257  1                                  12    
HELIX   13  A1 ASP A  272  ASP A  274  5                                   3    
HELIX   14  A2 SER A  278  SER A  280  5                                   3    
HELIX   15 A11 ALA A  293  LEU A  302  1                                  10    
SHEET    1   1 8 TYR A  17  GLY A  22  0                                        
SHEET    2   1 8 GLN A  43  GLU A  47  1                                        
SHEET    3   1 8 LEU A  80  GLN A  91  1                                        
SHEET    4   1 8 ALA A 126  GLU A 132  1                                        
SHEET    5   1 8 LYS A 169  ASP A 174  1                                        
SHEET    6   1 8 GLY A 204  LEU A 211  1                                        
SHEET    7   1 8 GLU A 233  ILE A 241  1                                        
SHEET    8   1 8 CYS A 262  VAL A 267  1                                        
SSBOND   1 CYS A  256    CYS A  262                          1555   1555  2.02  
LINK         C1B XYP A 548                 O4B XYP A 549     1555   1555  1.40  
LINK         C1B XYP A 549                 O4B XYP A 550     1555   1555  1.39  
LINK         C   PCA A   1                 N   ALA A   2     1555   1555  1.33  
CISPEP   1 HIS A   84    THR A   85          0        -0.97                     
SITE     1 ACT  2 GLU A 132  GLU A 238                                          
SITE     1 AC1  4 ASN A  48  LYS A 261  HOH A 473  XYP A 549                    
SITE     1 AC2  8 GLU A  47  ASN A  48  LYS A  51  GLN A  91                    
SITE     2 AC2  8 TRP A 268  TRP A 276  XYP A 548  XYP A 550                    
SITE     1 AC3 10 LYS A  51  HIS A  84  TRP A  88  ASN A 131                    
SITE     2 AC3 10 GLU A 132  GLN A 208  GLU A 238  TRP A 268                    
SITE     3 AC3 10 TRP A 276  XYP A 549                                          
CRYST1   81.300   81.300  113.170  90.00  90.00 120.00 P 31 2 1      6          
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      0.012300  0.007101  0.000000        0.00000                         
SCALE2      0.000000  0.014203  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008836        0.00000                         
HETATM    1  N   PCA A   1      62.668  62.203  21.309  1.00 18.58           N  
HETATM    2  CA  PCA A   1      63.088  62.571  22.657  1.00 18.88           C  
HETATM    3  CB  PCA A   1      63.715  63.964  22.513  1.00 17.28           C  
HETATM    4  CG  PCA A   1      63.535  64.343  21.056  1.00 18.73           C  
HETATM    5  CD  PCA A   1      62.895  63.139  20.399  1.00 19.64           C  
HETATM    6  OE  PCA A   1      62.622  63.048  19.203  1.00 22.45           O  
HETATM    7  C   PCA A   1      61.917  62.622  23.634  1.00 19.25           C  
HETATM    8  O   PCA A   1      60.871  63.199  23.333  1.00 20.24           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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