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Database: PDB
Entry: 4YNP
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Original site: 4YNP 
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HEADER    SUGAR BINDING PROTEIN, HYDROLASE        27-FEB-12   4DXB              
TITLE     2.29A STRUCTURE OF THE ENGINEERED MBP TEM-1 FUSION PROTEIN RG13 IN    
TITLE    2 COMPLEX WITH ZINC, P1 SPACE GROUP                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN, BETA-LACTAMASE TEM    
COMPND   3 CHIMERA;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: SEE REMARK 999;                                            
COMPND   6 SYNONYM: RG13;                                                       
COMPND   7 EC: 3.5.2.6;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: MALE, BLA;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: MALE- AUXOTROPH PM9F'                      
KEYWDS    TEM, BETA-LACTAMASE, MBP, ALLOSTERIC REGULATION, ZINC BINDING,        
KEYWDS   2 MALTOSE BINDING, SUGAR BINDING PROTEIN, HYDROLASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VAN DEN AKKER,W.KE                                                  
REVDAT   2   26-JUL-17 4DXB    1       SOURCE                                   
REVDAT   1   08-AUG-12 4DXB    0                                                
JRNL        AUTH   W.KE,A.H.LAURENT,M.D.ARMSTRONG,Y.CHEN,W.E.SMITH,J.LIANG,     
JRNL        AUTH 2 C.M.WRIGHT,M.OSTERMEIER,F.VAN DEN AKKER                      
JRNL        TITL   STRUCTURE OF AN ENGINEERED BETA-LACTAMASE MALTOSE BINDING    
JRNL        TITL 2 PROTEIN FUSION PROTEIN: INSIGHTS INTO HETEROTROPIC           
JRNL        TITL 3 ALLOSTERIC REGULATION.                                       
JRNL        REF    PLOS ONE                      V.   7 39168 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22720063                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0039168                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 56130                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3008                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.29                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.35                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3659                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 201                          
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9834                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 490                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.01000                                             
REMARK   3    B23 (A**2) : 0.01000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.461         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.297         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.220         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.733         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.874                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10064 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13652 ; 0.960 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1277 ; 4.515 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   436 ;36.971 ;25.046       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1739 ;15.174 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;12.709 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1512 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7608 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4906 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6965 ; 0.293 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   563 ; 0.112 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.070 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    95 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.097 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     2 ; 0.064 ; 0.200       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6524 ; 1.605 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10160 ; 2.551 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4059 ; 1.505 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3489 ; 2.253 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4DXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070899.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08100                            
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SAGITTAL FOCUSING                  
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59138                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 56.8                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1ZG4 AND 1OMP                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: A 1.0 UL DROP WAS PREPARED USING 0.5     
REMARK 280  UL PROTEIN MIXTURE (13.8 MG/ML RG13, 2.5 MM ZINC CHLORIDE) AND      
REMARK 280  0.5 UL RESERVOIR SOLUTION (0.2 M AMMONIUM ACETATE, 0.1 M TRIS,      
REMARK 280  PH 8.5-9.5, 15-30% PEG3350) AND EQUILIBRATED OVER A 1 ML            
REMARK 280  RESERVOIR SOLUTION, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  293.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS B   637                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  55     -169.30   -108.63                                   
REMARK 500    LEU A 122       86.01   -152.88                                   
REMARK 500    LYS A 144     -160.97   -125.87                                   
REMARK 500    ALA A 168      -72.99    -79.88                                   
REMARK 500    ASN A 173       23.95     43.24                                   
REMARK 500    TYR A 283      -55.05   -121.06                                   
REMARK 500    ASP A 340       13.71     58.90                                   
REMARK 500    SER A 344       -5.38   -141.61                                   
REMARK 500    ASP A 394      -72.76    -57.57                                   
REMARK 500    MET A 425     -130.15     57.34                                   
REMARK 500    LEU A 525       -9.19    -56.81                                   
REMARK 500    LEU A 581       77.99   -115.30                                   
REMARK 500    ASN A 599       30.44    -95.42                                   
REMARK 500    ASP B  55     -164.54   -103.88                                   
REMARK 500    ASP B  65       34.01    -74.20                                   
REMARK 500    ARG B  66      -22.79   -151.83                                   
REMARK 500    VAL B  97       49.76    -97.80                                   
REMARK 500    ILE B 108      -60.68   -105.52                                   
REMARK 500    LYS B 144     -164.99   -106.55                                   
REMARK 500    TYR B 283      -54.48   -121.63                                   
REMARK 500    TRP B 376     -172.79    -66.56                                   
REMARK 500    ASP B 394      -70.18    -54.82                                   
REMARK 500    MET B 425     -128.66     59.38                                   
REMARK 500    PRO B 530      -58.68    -26.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  39   NE2                                                    
REMARK 620 2 TYR B  17   OH  116.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 514   ND1                                                    
REMARK 620 2 HIS A 509   ND1 117.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 468   NE2                                                    
REMARK 620 2 ASP B 164   OD1 102.4                                              
REMARK 620 3 ASP B 164   OD2 118.6  51.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 468   NE2                                                    
REMARK 620 2 ASP A 164   OD1 107.8                                              
REMARK 620 3 HOH A 861   O   126.9 104.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 702                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DXC   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RG13 IS A CHIMERA COMPRISING THE N-TERMINAL DOMAIN OF MALTOSE-       
REMARK 999 BINDING PERIPLASMIC PROTEIN (UNP RESIDUES 27-342), THE C-TERMINAL    
REMARK 999 DOMAIN OF BETA-LACTAMASE TEM (UNP RESIDUES 227-286), AN ENGINEERED   
REMARK 999 LINKER (GSGGG), THE N-TERMINAL DOMAIN OF BETA-LACTAMASE TEM (UNP     
REMARK 999 RESIDUES 24-226), AN ENGINEERED LINKER (S), AND THE C-TERMINAL       
REMARK 999 DOMAIN OF MALTOSE-BINDING PERIPLASMIC PROTEIN (UNP RESIDUES 345-396) 
REMARK 999 .                                                                    
DBREF  4DXB A    1   316  UNP    P0AEX9   MALE_ECOLI      27    342             
DBREF  4DXB A  317   376  UNP    P62593   BLAT_ECOLX     227    286             
DBREF  4DXB A  382   584  UNP    P62593   BLAT_ECOLX      24    226             
DBREF  4DXB A  586   637  UNP    P0AEX9   MALE_ECOLI     345    396             
DBREF  4DXB B    1   316  UNP    P0AEX9   MALE_ECOLI      27    342             
DBREF  4DXB B  317   376  UNP    P62593   BLAT_ECOLX     227    286             
DBREF  4DXB B  382   584  UNP    P62593   BLAT_ECOLX      24    226             
DBREF  4DXB B  586   637  UNP    P0AEX9   MALE_ECOLI     345    396             
SEQADV 4DXB GLY A  377  UNP  P62593              LINKER                         
SEQADV 4DXB SER A  378  UNP  P62593              LINKER                         
SEQADV 4DXB GLY A  379  UNP  P62593              LINKER                         
SEQADV 4DXB GLY A  380  UNP  P62593              LINKER                         
SEQADV 4DXB GLY A  381  UNP  P62593              LINKER                         
SEQADV 4DXB SER A  585  UNP  P0AEX9              LINKER                         
SEQADV 4DXB GLY B  377  UNP  P62593              LINKER                         
SEQADV 4DXB SER B  378  UNP  P62593              LINKER                         
SEQADV 4DXB GLY B  379  UNP  P62593              LINKER                         
SEQADV 4DXB GLY B  380  UNP  P62593              LINKER                         
SEQADV 4DXB GLY B  381  UNP  P62593              LINKER                         
SEQADV 4DXB SER B  585  UNP  P0AEX9              LINKER                         
SEQRES   1 A  637  LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN GLY          
SEQRES   2 A  637  ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS LYS          
SEQRES   3 A  637  PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU HIS          
SEQRES   4 A  637  PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA ALA          
SEQRES   5 A  637  THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS ASP          
SEQRES   6 A  637  ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA GLU          
SEQRES   7 A  637  ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR PRO          
SEQRES   8 A  637  PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU ILE          
SEQRES   9 A  637  ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE TYR          
SEQRES  10 A  637  ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP GLU          
SEQRES  11 A  637  GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS GLY          
SEQRES  12 A  637  LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR PHE          
SEQRES  13 A  637  THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA PHE          
SEQRES  14 A  637  LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL GLY          
SEQRES  15 A  637  VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE LEU          
SEQRES  16 A  637  VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP THR          
SEQRES  17 A  637  ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY GLU          
SEQRES  18 A  637  THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER ASN          
SEQRES  19 A  637  ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL LEU          
SEQRES  20 A  637  PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL GLY          
SEQRES  21 A  637  VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN LYS          
SEQRES  22 A  637  GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU THR          
SEQRES  23 A  637  ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO LEU          
SEQRES  24 A  637  GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU ALA          
SEQRES  25 A  637  LYS ASP PRO ARG TRP PHE ILE ALA ASP LYS SER GLY ALA          
SEQRES  26 A  637  GLY GLU ARG GLY SER ARG GLY ILE ILE ALA ALA LEU GLY          
SEQRES  27 A  637  PRO ASP GLY LYS PRO SER ARG ILE VAL VAL ILE TYR THR          
SEQRES  28 A  637  THR GLY SER GLN ALA THR MET ASP GLU ARG ASN ARG GLN          
SEQRES  29 A  637  ILE ALA GLU ILE GLY ALA SER LEU ILE LYS HIS TRP GLY          
SEQRES  30 A  637  SER GLY GLY GLY HIS PRO GLU THR LEU VAL LYS VAL LYS          
SEQRES  31 A  637  ASP ALA GLU ASP GLN LEU GLY ALA ARG VAL GLY TYR ILE          
SEQRES  32 A  637  GLU LEU ASP LEU ASN SER GLY LYS ILE LEU GLU SER PHE          
SEQRES  33 A  637  ARG PRO GLU GLU ARG PHE PRO MET MET SER THR PHE LYS          
SEQRES  34 A  637  VAL LEU LEU CYS GLY ALA VAL LEU SER ARG ILE ASP ALA          
SEQRES  35 A  637  GLY GLN GLU GLN LEU GLY ARG ARG ILE HIS TYR SER GLN          
SEQRES  36 A  637  ASN ASP LEU VAL GLU TYR SER PRO VAL THR GLU LYS HIS          
SEQRES  37 A  637  LEU THR ASP GLY MET THR VAL ARG GLU LEU CYS SER ALA          
SEQRES  38 A  637  ALA ILE THR MET SER ASP ASN THR ALA ALA ASN LEU LEU          
SEQRES  39 A  637  LEU THR THR ILE GLY GLY PRO LYS GLU LEU THR ALA PHE          
SEQRES  40 A  637  LEU HIS ASN MET GLY ASP HIS VAL THR ARG LEU ASP ARG          
SEQRES  41 A  637  TRP GLU PRO GLU LEU ASN GLU ALA ILE PRO ASN ASP GLU          
SEQRES  42 A  637  ARG ASP THR THR MET PRO VAL ALA MET ALA THR THR LEU          
SEQRES  43 A  637  ARG LYS LEU LEU THR GLY GLU LEU LEU THR LEU ALA SER          
SEQRES  44 A  637  ARG GLN GLN LEU ILE ASP TRP MET GLU ALA ASP LYS VAL          
SEQRES  45 A  637  ALA GLY PRO LEU LEU ARG SER ALA LEU PRO ALA GLY SER          
SEQRES  46 A  637  ALA THR MET GLU ASN ALA GLN LYS GLY GLU ILE MET PRO          
SEQRES  47 A  637  ASN ILE PRO GLN MET SER ALA PHE TRP TYR ALA VAL ARG          
SEQRES  48 A  637  THR ALA VAL ILE ASN ALA ALA SER GLY ARG GLN THR VAL          
SEQRES  49 A  637  ASP GLU ALA LEU LYS ASP ALA GLN THR ARG ILE THR LYS          
SEQRES   1 B  637  LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN GLY          
SEQRES   2 B  637  ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS LYS          
SEQRES   3 B  637  PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU HIS          
SEQRES   4 B  637  PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA ALA          
SEQRES   5 B  637  THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS ASP          
SEQRES   6 B  637  ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA GLU          
SEQRES   7 B  637  ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR PRO          
SEQRES   8 B  637  PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU ILE          
SEQRES   9 B  637  ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE TYR          
SEQRES  10 B  637  ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP GLU          
SEQRES  11 B  637  GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS GLY          
SEQRES  12 B  637  LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR PHE          
SEQRES  13 B  637  THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA PHE          
SEQRES  14 B  637  LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL GLY          
SEQRES  15 B  637  VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE LEU          
SEQRES  16 B  637  VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP THR          
SEQRES  17 B  637  ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY GLU          
SEQRES  18 B  637  THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER ASN          
SEQRES  19 B  637  ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL LEU          
SEQRES  20 B  637  PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL GLY          
SEQRES  21 B  637  VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN LYS          
SEQRES  22 B  637  GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU THR          
SEQRES  23 B  637  ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO LEU          
SEQRES  24 B  637  GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU ALA          
SEQRES  25 B  637  LYS ASP PRO ARG TRP PHE ILE ALA ASP LYS SER GLY ALA          
SEQRES  26 B  637  GLY GLU ARG GLY SER ARG GLY ILE ILE ALA ALA LEU GLY          
SEQRES  27 B  637  PRO ASP GLY LYS PRO SER ARG ILE VAL VAL ILE TYR THR          
SEQRES  28 B  637  THR GLY SER GLN ALA THR MET ASP GLU ARG ASN ARG GLN          
SEQRES  29 B  637  ILE ALA GLU ILE GLY ALA SER LEU ILE LYS HIS TRP GLY          
SEQRES  30 B  637  SER GLY GLY GLY HIS PRO GLU THR LEU VAL LYS VAL LYS          
SEQRES  31 B  637  ASP ALA GLU ASP GLN LEU GLY ALA ARG VAL GLY TYR ILE          
SEQRES  32 B  637  GLU LEU ASP LEU ASN SER GLY LYS ILE LEU GLU SER PHE          
SEQRES  33 B  637  ARG PRO GLU GLU ARG PHE PRO MET MET SER THR PHE LYS          
SEQRES  34 B  637  VAL LEU LEU CYS GLY ALA VAL LEU SER ARG ILE ASP ALA          
SEQRES  35 B  637  GLY GLN GLU GLN LEU GLY ARG ARG ILE HIS TYR SER GLN          
SEQRES  36 B  637  ASN ASP LEU VAL GLU TYR SER PRO VAL THR GLU LYS HIS          
SEQRES  37 B  637  LEU THR ASP GLY MET THR VAL ARG GLU LEU CYS SER ALA          
SEQRES  38 B  637  ALA ILE THR MET SER ASP ASN THR ALA ALA ASN LEU LEU          
SEQRES  39 B  637  LEU THR THR ILE GLY GLY PRO LYS GLU LEU THR ALA PHE          
SEQRES  40 B  637  LEU HIS ASN MET GLY ASP HIS VAL THR ARG LEU ASP ARG          
SEQRES  41 B  637  TRP GLU PRO GLU LEU ASN GLU ALA ILE PRO ASN ASP GLU          
SEQRES  42 B  637  ARG ASP THR THR MET PRO VAL ALA MET ALA THR THR LEU          
SEQRES  43 B  637  ARG LYS LEU LEU THR GLY GLU LEU LEU THR LEU ALA SER          
SEQRES  44 B  637  ARG GLN GLN LEU ILE ASP TRP MET GLU ALA ASP LYS VAL          
SEQRES  45 B  637  ALA GLY PRO LEU LEU ARG SER ALA LEU PRO ALA GLY SER          
SEQRES  46 B  637  ALA THR MET GLU ASN ALA GLN LYS GLY GLU ILE MET PRO          
SEQRES  47 B  637  ASN ILE PRO GLN MET SER ALA PHE TRP TYR ALA VAL ARG          
SEQRES  48 B  637  THR ALA VAL ILE ASN ALA ALA SER GLY ARG GLN THR VAL          
SEQRES  49 B  637  ASP GLU ALA LEU LYS ASP ALA GLN THR ARG ILE THR LYS          
HET     ZN  A 701       1                                                       
HET     ZN  A 702       1                                                       
HET     ZN  B 701       1                                                       
HET     ZN  B 702       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   7  HOH   *490(H2 O)                                                    
HELIX    1   1 GLY A   16  GLY A   32  1                                  17    
HELIX    2   2 LYS A   42  GLY A   54  1                                  13    
HELIX    3   3 ARG A   66  SER A   73  1                                   8    
HELIX    4   4 ASP A   82  ASP A   87  1                                   6    
HELIX    5   5 TYR A   90  VAL A   97  1                                   8    
HELIX    6   6 GLU A  131  ALA A  141  1                                  11    
HELIX    7   7 GLU A  153  ASP A  164  1                                  12    
HELIX    8   8 ASN A  185  ASN A  201  1                                  17    
HELIX    9   9 ASP A  209  LYS A  219  1                                  11    
HELIX   10  10 GLY A  228  TRP A  230  5                                   3    
HELIX   11  11 ALA A  231  LYS A  239  1                                   9    
HELIX   12  12 ASN A  272  TYR A  283  1                                  12    
HELIX   13  13 THR A  286  LYS A  297  1                                  12    
HELIX   14  14 LEU A  304  ALA A  312  1                                   9    
HELIX   15  15 LYS A  313  PHE A  318  5                                   6    
HELIX   16  16 GLY A  324  ARG A  328  5                                   5    
HELIX   17  17 THR A  357  HIS A  375  1                                  19    
HELIX   18  18 HIS A  382  GLY A  397  1                                  16    
HELIX   19  19 MET A  425  THR A  427  5                                   3    
HELIX   20  20 PHE A  428  ALA A  442  1                                  15    
HELIX   21  21 SER A  454  LEU A  458  5                                   5    
HELIX   22  22 VAL A  464  HIS A  468  5                                   5    
HELIX   23  23 VAL A  475  MET A  485  1                                  11    
HELIX   24  24 ASP A  487  GLY A  499  1                                  13    
HELIX   25  25 GLY A  500  MET A  511  1                                  12    
HELIX   26  26 PRO A  523  GLU A  527  5                                   5    
HELIX   27  27 MET A  538  LEU A  550  1                                  13    
HELIX   28  28 THR A  556  GLY A  574  1                                  19    
HELIX   29  29 SER A  585  GLY A  594  1                                  10    
HELIX   30  30 GLN A  602  GLY A  620  1                                  19    
HELIX   31  31 THR A  623  THR A  636  1                                  14    
HELIX   32  32 GLY B   16  GLY B   32  1                                  17    
HELIX   33  33 LYS B   42  THR B   53  1                                  12    
HELIX   34  34 ARG B   66  SER B   73  1                                   8    
HELIX   35  35 ASP B   82  ASP B   87  1                                   6    
HELIX   36  36 TYR B   90  VAL B   97  1                                   8    
HELIX   37  37 GLU B  131  ALA B  141  1                                  11    
HELIX   38  38 GLU B  153  ASP B  164  1                                  12    
HELIX   39  39 ASN B  185  ASN B  201  1                                  17    
HELIX   40  40 ASP B  209  LYS B  219  1                                  11    
HELIX   41  41 GLY B  228  TRP B  230  5                                   3    
HELIX   42  42 ALA B  231  LYS B  239  1                                   9    
HELIX   43  43 ASN B  272  TYR B  283  1                                  12    
HELIX   44  44 THR B  286  LYS B  297  1                                  12    
HELIX   45  45 LEU B  304  ALA B  312  1                                   9    
HELIX   46  46 ARG B  328  SER B  330  5                                   3    
HELIX   47  47 GLY B  338  LYS B  342  5                                   5    
HELIX   48  48 THR B  357  HIS B  375  1                                  19    
HELIX   49  49 HIS B  382  GLY B  397  1                                  16    
HELIX   50  50 THR B  427  ALA B  442  1                                  16    
HELIX   51  51 SER B  454  LEU B  458  5                                   5    
HELIX   52  52 VAL B  464  HIS B  468  5                                   5    
HELIX   53  53 VAL B  475  MET B  485  1                                  11    
HELIX   54  54 ASP B  487  GLY B  499  1                                  13    
HELIX   55  55 GLY B  500  MET B  511  1                                  12    
HELIX   56  56 PRO B  523  GLU B  527  5                                   5    
HELIX   57  57 MET B  538  THR B  551  1                                  14    
HELIX   58  58 THR B  556  GLY B  574  1                                  19    
HELIX   59  59 SER B  585  LYS B  593  1                                   9    
HELIX   60  60 GLN B  602  GLY B  620  1                                  19    
HELIX   61  61 THR B  623  ARG B  634  1                                  12    
SHEET    1   A 6 VAL A  35  GLU A  38  0                                        
SHEET    2   A 6 LEU A   7  TRP A  10  1  N  LEU A   7   O  THR A  36           
SHEET    3   A 6 ILE A  59  ALA A  63  1  O  PHE A  61   N  TRP A  10           
SHEET    4   A 6 PHE A 258  ILE A 266 -1  O  GLY A 265   N  ILE A  60           
SHEET    5   A 6 TYR A 106  GLU A 111 -1  N  GLU A 111   O  GLY A 260           
SHEET    6   A 6 ALA A 301  VAL A 302 -1  O  ALA A 301   N  VAL A 110           
SHEET    1   B 5 VAL A  35  GLU A  38  0                                        
SHEET    2   B 5 LEU A   7  TRP A  10  1  N  LEU A   7   O  THR A  36           
SHEET    3   B 5 ILE A  59  ALA A  63  1  O  PHE A  61   N  TRP A  10           
SHEET    4   B 5 PHE A 258  ILE A 266 -1  O  GLY A 265   N  ILE A  60           
SHEET    5   B 5 GLU A 595  ILE A 596  1  O  GLU A 595   N  VAL A 259           
SHEET    1   C 2 ARG A  98  TYR A  99  0                                        
SHEET    2   C 2 LYS A 102  LEU A 103 -1  O  LYS A 102   N  TYR A  99           
SHEET    1   D 3 MET A 224  ASN A 227  0                                        
SHEET    2   D 3 SER A 114  ASN A 118 -1  N  ILE A 116   O  THR A 225           
SHEET    3   D 3 TYR A 242  THR A 245 -1  O  THR A 245   N  LEU A 115           
SHEET    1   E 2 TYR A 167  GLU A 172  0                                        
SHEET    2   E 2 LYS A 175  GLY A 182 -1  O  LYS A 175   N  GLU A 172           
SHEET    1   F 4 GLY A 332  LEU A 337  0                                        
SHEET    2   F 4 ARG A 345  THR A 351 -1  O  ILE A 349   N  ILE A 333           
SHEET    3   F 4 VAL A 400  ASP A 406 -1  O  LEU A 405   N  ILE A 346           
SHEET    4   F 4 ILE A 412  PHE A 416 -1  O  PHE A 416   N  TYR A 402           
SHEET    1   G 2 PHE A 422  PRO A 423  0                                        
SHEET    2   G 2 THR A 536  THR A 537 -1  O  THR A 537   N  PHE A 422           
SHEET    1   H 2 ARG A 450  ILE A 451  0                                        
SHEET    2   H 2 MET A 473  THR A 474 -1  O  MET A 473   N  ILE A 451           
SHEET    1   I 6 VAL B  35  GLU B  38  0                                        
SHEET    2   I 6 LEU B   7  ILE B  11  1  N  LEU B   7   O  THR B  36           
SHEET    3   I 6 ILE B  59  ALA B  63  1  O  PHE B  61   N  TRP B  10           
SHEET    4   I 6 PHE B 258  ILE B 266 -1  O  GLY B 265   N  ILE B  60           
SHEET    5   I 6 ALA B 105  GLU B 111 -1  N  ILE B 108   O  LEU B 262           
SHEET    6   I 6 ALA B 301  VAL B 302 -1  O  ALA B 301   N  VAL B 110           
SHEET    1   J 5 VAL B  35  GLU B  38  0                                        
SHEET    2   J 5 LEU B   7  ILE B  11  1  N  LEU B   7   O  THR B  36           
SHEET    3   J 5 ILE B  59  ALA B  63  1  O  PHE B  61   N  TRP B  10           
SHEET    4   J 5 PHE B 258  ILE B 266 -1  O  GLY B 265   N  ILE B  60           
SHEET    5   J 5 GLU B 595  ILE B 596  1  O  GLU B 595   N  VAL B 259           
SHEET    1   K 2 ARG B  98  TYR B  99  0                                        
SHEET    2   K 2 LYS B 102  LEU B 103 -1  O  LYS B 102   N  TYR B  99           
SHEET    1   L 4 SER B 145  LEU B 147  0                                        
SHEET    2   L 4 THR B 222  ASN B 227  1  O  ALA B 223   N  SER B 145           
SHEET    3   L 4 SER B 114  ASN B 118 -1  N  ASN B 118   O  ALA B 223           
SHEET    4   L 4 TYR B 242  THR B 245 -1  O  THR B 245   N  LEU B 115           
SHEET    1   M 2 TYR B 167  GLU B 172  0                                        
SHEET    2   M 2 LYS B 175  GLY B 182 -1  O  ASP B 177   N  LYS B 170           
SHEET    1   N 4 GLY B 332  LEU B 337  0                                        
SHEET    2   N 4 ARG B 345  THR B 351 -1  O  ILE B 349   N  ILE B 333           
SHEET    3   N 4 VAL B 400  ASP B 406 -1  O  LEU B 405   N  ILE B 346           
SHEET    4   N 4 ILE B 412  PHE B 416 -1  O  PHE B 416   N  TYR B 402           
SHEET    1   O 2 PHE B 422  PRO B 423  0                                        
SHEET    2   O 2 THR B 536  THR B 537 -1  O  THR B 537   N  PHE B 422           
SHEET    1   P 2 ARG B 450  ILE B 451  0                                        
SHEET    2   P 2 MET B 473  THR B 474 -1  O  MET B 473   N  ILE B 451           
SSBOND   1 CYS A  433    CYS A  479                          1555   1555  2.05  
SSBOND   2 CYS B  433    CYS B  479                          1555   1555  2.05  
LINK         NE2 HIS B  39                ZN    ZN B 702     1555   1555  1.94  
LINK         OH  TYR B  17                ZN    ZN B 702     1555   1555  1.96  
LINK         ND1 HIS A 514                ZN    ZN A 702     1555   1555  2.03  
LINK         NE2 HIS B 468                ZN    ZN B 701     1555   1555  2.06  
LINK         ND1 HIS A 509                ZN    ZN A 702     1555   1555  2.10  
LINK         NE2 HIS A 468                ZN    ZN A 701     1555   1555  2.13  
LINK         OD1 ASP A 164                ZN    ZN A 701     1555   1555  2.17  
LINK         OD1 ASP B 164                ZN    ZN B 701     1555   1555  2.36  
LINK         OD2 ASP B 164                ZN    ZN B 701     1555   1555  2.63  
LINK        ZN    ZN A 701                 O   HOH A 861     1555   1555  2.60  
CISPEP   1 GLU A  522    PRO A  523          0        -1.74                     
CISPEP   2 GLU B  522    PRO B  523          0        -4.75                     
SITE     1 AC1  3 ASP A 164  HIS A 468  HOH A 861                               
SITE     1 AC2  4 TYR A  17  HIS A  39  HIS A 509  HIS A 514                    
SITE     1 AC3  3 ASP B 164  HIS B 468  HOH B 803                               
SITE     1 AC4  4 TYR B  17  HIS B  39  HIS B 509  HIS B 514                    
CRYST1   48.316   74.177  103.130  83.54  77.64  89.98 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020697 -0.000006 -0.004564        0.00000                         
SCALE2      0.000000  0.013481 -0.001563        0.00000                         
SCALE3      0.000000  0.000000  0.009993        0.00000                         
(ATOM LINES ARE NOT SHOWN.)

DBGET integrated database retrieval system