GenomeNet

Database: PDB
Entry: 4XQ4
LinkDB: 4XQ4
Original site: 4XQ4 
HEADER    HYDROLASE                               19-JAN-15   4XQ4              
TITLE     X-RAY STRUCTURE ANALYSIS OF XYLANASE - N44D                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE 2;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SUBSTRATE-BINDING GROOVE, JELLY ROLL;                      
COMPND   5 SYNONYM: XYLANASE 2,1,4-BETA-D-XYLAN XYLANOHYDROLASE 2;              
COMPND   6 EC: 3.2.1.8;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HYPOCREA JECORINA;                              
SOURCE   3 ORGANISM_TAXID: 51453;                                               
SOURCE   4 GENE: XYN2;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD;                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJEXPRESS401                              
KEYWDS    JELLY ROLL, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.WAN,J.M.PARK,D.M.RICCARDI,L.B.HANSON,Z.FISHER,J.C.SMITH,            
AUTHOR   2 A.OSTERMANN,T.SCHRADER,D.E.GRAHAM,L.COATES,P.LANGAN,A.Y.KOVALEVSKY   
REVDAT   5   20-SEP-17 4XQ4    1       JRNL   REMARK                            
REVDAT   4   21-OCT-15 4XQ4    1       JRNL                                     
REVDAT   3   14-OCT-15 4XQ4    1       REMARK                                   
REVDAT   2   07-OCT-15 4XQ4    1       JRNL                                     
REVDAT   1   23-SEP-15 4XQ4    0                                                
JRNL        AUTH   Q.WAN,J.M.PARKS,B.L.HANSON,S.Z.FISHER,A.OSTERMANN,           
JRNL        AUTH 2 T.E.SCHRADER,D.E.GRAHAM,L.COATES,P.LANGAN,A.KOVALEVSKY       
JRNL        TITL   DIRECT DETERMINATION OF PROTONATION STATES AND VISUALIZATION 
JRNL        TITL 2 OF HYDROGEN BONDING IN A GLYCOSIDE HYDROLASE WITH NEUTRON    
JRNL        TITL 3 CRYSTALLOGRAPHY.                                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112 12384 2015              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   26392527                                                     
JRNL        DOI    10.1073/PNAS.1504986112                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.Y.KOVALEVSKY,B.L.HANSON,S.SEAVER,S.Z.FISHER,M.MUSTYAKIMOV, 
REMARK   1  AUTH 2 P.LANGAN                                                     
REMARK   1  TITL   PRELIMINARY JOINT X-RAY AND NEUTRON PROTEIN CRYSTALLOGRAPHIC 
REMARK   1  TITL 2 STUDIES OF ENDOXYLANASE II FROM THE FUNGUS TRICHODERMA       
REMARK   1  TITL 3 LONGIBRACHIATUM.                                             
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  67   283 2011              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   21301107                                                     
REMARK   1  DOI    10.1107/S174430911005075X                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Q.WAN,Q.ZHANG,S.HAMILTON-BREHM,K.WEISS,M.MUSTYAKIMOV,        
REMARK   1  AUTH 2 L.COATES,P.LANGAN,D.GRAHAM,A.KOVALEVSKY                      
REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC STUDIES OF FAMILY 11 XYLANASE         
REMARK   1  TITL 2 MICHAELIS AND PRODUCT COMPLEXES: IMPLICATIONS FOR THE        
REMARK   1  TITL 3 CATALYTIC MECHANISM.                                         
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  70    11 2014              
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   24419374                                                     
REMARK   1  DOI    10.1107/S1399004713023626                                    
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   Q.WAN,A.KOVALEVSKY,Q.ZHANG,S.HAMILTON-BREHM,R.UPTON,         
REMARK   1  AUTH 2 K.L.WEISS,M.MUSTYAKIMOV,D.GRAHAM,L.COATES,P.LANGAN           
REMARK   1  TITL   HETEROLOGOUS EXPRESSION, PURIFICATION, CRYSTALLIZATION AND   
REMARK   1  TITL 2 PRELIMINARY X-RAY ANALYSIS OF TRICHODERMA REESEI XYLANASE II 
REMARK   1  TITL 3 AND FOUR VARIANTS.                                           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  69   320 2013              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   23519813                                                     
REMARK   1  DOI    10.1107/S1744309113001164                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 105854                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.143                           
REMARK   3   R VALUE            (WORKING SET) : 0.141                           
REMARK   3   FREE R VALUE                     : 0.168                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5281                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 27.2019 -  3.8804    0.99     3422   174  0.1776 0.2179        
REMARK   3     2  3.8804 -  3.0814    1.00     3416   183  0.1442 0.1502        
REMARK   3     3  3.0814 -  2.6923    1.00     3384   174  0.1502 0.1685        
REMARK   3     4  2.6923 -  2.4463    1.00     3400   163  0.1473 0.1989        
REMARK   3     5  2.4463 -  2.2710    1.00     3412   178  0.1385 0.1456        
REMARK   3     6  2.2710 -  2.1372    1.00     3352   175  0.1255 0.1586        
REMARK   3     7  2.1372 -  2.0302    0.99     3377   190  0.1211 0.1562        
REMARK   3     8  2.0302 -  1.9418    0.99     3327   187  0.1175 0.1387        
REMARK   3     9  1.9418 -  1.8671    0.99     3334   197  0.1189 0.1352        
REMARK   3    10  1.8671 -  1.8027    0.99     3360   148  0.1187 0.1469        
REMARK   3    11  1.8027 -  1.7463    0.99     3326   179  0.1216 0.1501        
REMARK   3    12  1.7463 -  1.6964    0.99     3330   180  0.1191 0.1539        
REMARK   3    13  1.6964 -  1.6518    0.99     3312   183  0.1205 0.1482        
REMARK   3    14  1.6518 -  1.6115    0.99     3341   157  0.1233 0.1648        
REMARK   3    15  1.6115 -  1.5749    0.99     3338   175  0.1186 0.1417        
REMARK   3    16  1.5749 -  1.5413    0.99     3352   161  0.1223 0.1408        
REMARK   3    17  1.5413 -  1.5105    0.99     3366   168  0.1263 0.1746        
REMARK   3    18  1.5105 -  1.4820    0.99     3280   172  0.1295 0.1671        
REMARK   3    19  1.4820 -  1.4555    0.99     3375   183  0.1377 0.1845        
REMARK   3    20  1.4555 -  1.4309    1.00     3362   198  0.1405 0.1745        
REMARK   3    21  1.4309 -  1.4078    1.00     3311   183  0.1403 0.1770        
REMARK   3    22  1.4078 -  1.3861    0.99     3367   160  0.1485 0.1859        
REMARK   3    23  1.3861 -  1.3657    1.00     3311   172  0.1554 0.1809        
REMARK   3    24  1.3657 -  1.3465    0.99     3397   153  0.1595 0.2070        
REMARK   3    25  1.3465 -  1.3283    1.00     3345   165  0.1663 0.1900        
REMARK   3    26  1.3283 -  1.3111    0.99     3350   165  0.1685 0.1991        
REMARK   3    27  1.3111 -  1.2947    0.99     3318   199  0.1782 0.1818        
REMARK   3    28  1.2947 -  1.2791    0.99     3327   192  0.1864 0.2050        
REMARK   3    29  1.2791 -  1.2642    0.99     3327   197  0.1961 0.2147        
REMARK   3    30  1.2642 -  1.2500    0.99     3354   170  0.2094 0.2314        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.100            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.620           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.53                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3150                                  
REMARK   3   ANGLE     :  1.302           4344                                  
REMARK   3   CHIRALITY :  0.089            435                                  
REMARK   3   PLANARITY :  0.006            576                                  
REMARK   3   DIHEDRAL  : 12.695           1094                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206090.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
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          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 3.15, SCALEPACK           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114048                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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: 2DFB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG8000, 0.2 M NAI, 0.1 M NAOAC AT   
REMARK 280  PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       40.47000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.87500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       40.47000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.87500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     THR A     2                                                      
REMARK 465     THR B     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   4    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 117    CG1  CG2  CD1                                       
REMARK 470     GLN A 161    CD   OE1  NE2                                       
REMARK 470     LEU A 164    CB   CG   CD1  CD2                                  
REMARK 470     THR A 165    OG1  CG2                                            
REMARK 470     LYS B  56    CG   CD   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           DISTANCE          
REMARK 500   HG   SER A   146     O    HOH A   302              1.57            
REMARK 500   O    HOH A   358     O    HOH A   385              1.96            
REMARK 500   O    HOH A   318     O    HOH A   333              2.00            
REMARK 500   O    HOH B   333     O    HOH B   364              2.00            
REMARK 500   O    HOH A   463     O    HOH A   484              2.01            
REMARK 500   O    HOH A   334     O    HOH A   354              2.07            
REMARK 500   O    HOH B   349     O    HOH B   383              2.07            
REMARK 500   O    HOH B   425     O    HOH B   498              2.08            
REMARK 500   O    HOH B   366     O    HOH B   378              2.08            
REMARK 500   O    HOH A   398     O    HOH B   374              2.08            
REMARK 500   O    HOH A   358     O    HOH A   362              2.10            
REMARK 500   O    HOH A   372     O    HOH B   374              2.11            
REMARK 500   O    HOH A   325     O    HOH A   380              2.11            
REMARK 500   O    HOH A   333     O    HOH A   378              2.11            
REMARK 500   O    HOH B   374     O    HOH B   379              2.15            
REMARK 500   O    HOH B   539     O    HOH B   566              2.16            
REMARK 500   O    HOH A   375     O    HOH A   510              2.17            
REMARK 500   O    HOH A   559     O    HOH A   578              2.17            
REMARK 500   O    HOH B   559     O    HOH B   567              2.17            
REMARK 500   O    HOH B   413     O    HOH B   538              2.17            
REMARK 500   ND2  ASN B    69     O    HOH B   301              2.18            
REMARK 500   OE1  GLN A    34     O    HOH A   416              2.18            
REMARK 500   O    HOH B   372     O    HOH B   383              2.19            
REMARK 500   O    HOH B   548     O    HOH B   588              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   304     O    HOH B   304     2454     1.81            
REMARK 500   O    HOH A   304     O    HOH A   304     2555     1.85            
REMARK 500   O    HOH A   310     O    HOH B   360     2454     2.14            
REMARK 500   O    HOH A   365     O    HOH A   368     4445     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 170     -141.58   -105.05                                   
REMARK 500    ASP B 170     -144.71   -108.01                                   
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 573        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 594        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH A 601        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B 575        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B 585        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH B 587        DISTANCE =  6.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 203                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4XPV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4XQD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4XQW   RELATED DB: PDB                                   
DBREF  4XQ4 A    2   190  UNP    P36217   XYN2_HYPJE      34    222             
DBREF  4XQ4 B    2   190  UNP    P36217   XYN2_HYPJE      34    222             
SEQADV 4XQ4 ASP A   44  UNP  P36217    ASN    76 ENGINEERED MUTATION            
SEQADV 4XQ4 ASP B   44  UNP  P36217    ASN    76 ENGINEERED MUTATION            
SEQRES   1 A  189  THR ILE GLN PRO GLY THR GLY TYR ASN ASN GLY TYR PHE          
SEQRES   2 A  189  TYR SER TYR TRP ASN ASP GLY HIS GLY GLY VAL THR TYR          
SEQRES   3 A  189  THR ASN GLY PRO GLY GLY GLN PHE SER VAL ASN TRP SER          
SEQRES   4 A  189  ASN SER GLY ASP PHE VAL GLY GLY LYS GLY TRP GLN PRO          
SEQRES   5 A  189  GLY THR LYS ASN LYS VAL ILE ASN PHE SER GLY SER TYR          
SEQRES   6 A  189  ASN PRO ASN GLY ASN SER TYR LEU SER VAL TYR GLY TRP          
SEQRES   7 A  189  SER ARG ASN PRO LEU ILE GLU TYR TYR ILE VAL GLU ASN          
SEQRES   8 A  189  PHE GLY THR TYR ASN PRO SER THR GLY ALA THR LYS LEU          
SEQRES   9 A  189  GLY GLU VAL THR SER ASP GLY SER VAL TYR ASP ILE TYR          
SEQRES  10 A  189  ARG THR GLN ARG VAL ASN GLN PRO SER ILE ILE GLY THR          
SEQRES  11 A  189  ALA THR PHE TYR GLN TYR TRP SER VAL ARG ARG ASN HIS          
SEQRES  12 A  189  ARG SER SER GLY SER VAL ASN THR ALA ASN HIS PHE ASN          
SEQRES  13 A  189  ALA TRP ALA GLN GLN GLY LEU THR LEU GLY THR MET ASP          
SEQRES  14 A  189  TYR GLN ILE VAL ALA VAL GLU GLY TYR PHE SER SER GLY          
SEQRES  15 A  189  SER ALA SER ILE THR VAL SER                                  
SEQRES   1 B  189  THR ILE GLN PRO GLY THR GLY TYR ASN ASN GLY TYR PHE          
SEQRES   2 B  189  TYR SER TYR TRP ASN ASP GLY HIS GLY GLY VAL THR TYR          
SEQRES   3 B  189  THR ASN GLY PRO GLY GLY GLN PHE SER VAL ASN TRP SER          
SEQRES   4 B  189  ASN SER GLY ASP PHE VAL GLY GLY LYS GLY TRP GLN PRO          
SEQRES   5 B  189  GLY THR LYS ASN LYS VAL ILE ASN PHE SER GLY SER TYR          
SEQRES   6 B  189  ASN PRO ASN GLY ASN SER TYR LEU SER VAL TYR GLY TRP          
SEQRES   7 B  189  SER ARG ASN PRO LEU ILE GLU TYR TYR ILE VAL GLU ASN          
SEQRES   8 B  189  PHE GLY THR TYR ASN PRO SER THR GLY ALA THR LYS LEU          
SEQRES   9 B  189  GLY GLU VAL THR SER ASP GLY SER VAL TYR ASP ILE TYR          
SEQRES  10 B  189  ARG THR GLN ARG VAL ASN GLN PRO SER ILE ILE GLY THR          
SEQRES  11 B  189  ALA THR PHE TYR GLN TYR TRP SER VAL ARG ARG ASN HIS          
SEQRES  12 B  189  ARG SER SER GLY SER VAL ASN THR ALA ASN HIS PHE ASN          
SEQRES  13 B  189  ALA TRP ALA GLN GLN GLY LEU THR LEU GLY THR MET ASP          
SEQRES  14 B  189  TYR GLN ILE VAL ALA VAL GLU GLY TYR PHE SER SER GLY          
SEQRES  15 B  189  SER ALA SER ILE THR VAL SER                                  
HET    IOD  A 201       1                                                       
HET    IOD  A 202       1                                                       
HET    IOD  B 201       1                                                       
HET    IOD  B 202       1                                                       
HET    IOD  B 203       1                                                       
HETNAM     IOD IODIDE ION                                                       
FORMUL   3  IOD    5(I 1-)                                                      
FORMUL   8  HOH   *593(H2 O)                                                    
HELIX    1 AA1 THR A  152  GLN A  162  1                                  11    
HELIX    2 AA2 THR B  152  GLN B  162  1                                  11    
SHEET    1 AA1 9 GLY A   6  ASN A  10  0                                        
SHEET    2 AA1 9 TYR A  13  ASN A  19 -1  O  TYR A  13   N  ASN A  10           
SHEET    3 AA1 9 ASP A  44  TRP A  51 -1  O  GLY A  50   N  PHE A  14           
SHEET    4 AA1 9 THR A 168  TYR A 179 -1  O  GLN A 172   N  TRP A  51           
SHEET    5 AA1 9 SER A  72  ARG A  81 -1  N  TYR A  77   O  ILE A 173           
SHEET    6 AA1 9 ILE A  85  PHE A  93 -1  O  TYR A  87   N  GLY A  78           
SHEET    7 AA1 9 ALA A 132  ARG A 141  1  O  ARG A 141   N  VAL A  90           
SHEET    8 AA1 9 SER A 113  GLN A 125 -1  N  ARG A 122   O  PHE A 134           
SHEET    9 AA1 9 THR A 103  SER A 110 -1  N  LEU A 105   O  ILE A 117           
SHEET    1 AA2 5 VAL A  25  ASN A  29  0                                        
SHEET    2 AA2 5 GLN A  34  TRP A  39 -1  O  SER A  36   N  THR A  28           
SHEET    3 AA2 5 SER A 182  SER A 190 -1  O  GLY A 183   N  TRP A  39           
SHEET    4 AA2 5 VAL A  59  ASN A  69 -1  N  ASN A  69   O  SER A 182           
SHEET    5 AA2 5 GLY A 148  ASN A 151 -1  O  VAL A 150   N  ILE A  60           
SHEET    1 AA3 9 GLY B   6  ASN B  10  0                                        
SHEET    2 AA3 9 TYR B  13  ASN B  19 -1  O  TYR B  15   N  GLY B   8           
SHEET    3 AA3 9 ASP B  44  TRP B  51 -1  O  GLY B  50   N  PHE B  14           
SHEET    4 AA3 9 THR B 168  TYR B 179 -1  O  VAL B 174   N  LYS B  49           
SHEET    5 AA3 9 SER B  72  ARG B  81 -1  N  TYR B  77   O  ILE B 173           
SHEET    6 AA3 9 ILE B  85  PHE B  93 -1  O  ILE B  89   N  VAL B  76           
SHEET    7 AA3 9 ALA B 132  ARG B 141  1  O  ARG B 141   N  VAL B  90           
SHEET    8 AA3 9 SER B 113  GLN B 125 -1  N  ARG B 122   O  PHE B 134           
SHEET    9 AA3 9 THR B 103  SER B 110 -1  N  LEU B 105   O  ILE B 117           
SHEET    1 AA4 5 VAL B  25  ASN B  29  0                                        
SHEET    2 AA4 5 GLN B  34  TRP B  39 -1  O  SER B  36   N  THR B  28           
SHEET    3 AA4 5 SER B 182  SER B 190 -1  O  GLY B 183   N  TRP B  39           
SHEET    4 AA4 5 VAL B  59  ASN B  69 -1  N  ASN B  69   O  SER B 182           
SHEET    5 AA4 5 GLY B 148  ASN B 151 -1  O  VAL B 150   N  ILE B  60           
CISPEP   1 GLN A   52    PRO A   53          0         1.05                     
CISPEP   2 ASN A   82    PRO A   83          0         7.10                     
CISPEP   3 GLN B   52    PRO B   53          0         1.25                     
CISPEP   4 ASN B   82    PRO B   83          0         7.64                     
SITE     1 AC1  2 ASN A  82  SER A 146                                          
SITE     1 AC2  2 SER A  65  SER A 184                                          
SITE     1 AC3  2 ASN B  82  SER B 146                                          
SITE     1 AC4  2 ASN B  67  SER B 184                                          
SITE     1 AC5  4 GLY B  24  THR B  26  ASN B  38  HOH B 514                    
CRYST1   80.940   69.750   78.281  90.00 117.45  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012355  0.000000  0.006418        0.00000                         
SCALE2      0.000000  0.014337  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014395        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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