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Database: PDB
Entry: 4ZKS
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Original site: 4ZKS 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-APR-15   4ZKS              
TITLE     THE CRYSTAL STRUCTURE OF UPAIN-1-W3A IN COMPLEX WITH INACTIVE UPA     
TITLE    2 (UPA-S195A) AT PH7.4                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: U;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 179-425;                                      
COMPND   5 SYNONYM: UPA;                                                        
COMPND   6 EC: 3.4.21.73;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: UPAIN-1-W3A;                                               
COMPND  11 CHAIN: P;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLAU;                                                          
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: X33;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  13 ORGANISM_TAXID: 32630                                                
KEYWDS    PEPTIDES INHIBITOR, UPA, SERINE PROTEASE, HYDROLASE-HYDROLASE         
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.JIANG,P.A.ANDREASEN,M.HUANG                                         
REVDAT   1   18-MAY-16 4ZKS    0                                                
JRNL        AUTH   L.JIANG,P.A.ANDREASEN,M.HUANG                                
JRNL        TITL   THE CRYSTAL STRUCTURE OF MUPAIN-1-IG IN COMPLEX WITH         
JRNL        TITL 2 MURINISED HUMAN UPA AT PH7.4                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 18829                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1017                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1362                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2025                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41000                                             
REMARK   3    B22 (A**2) : -0.41000                                             
REMARK   3    B33 (A**2) : 1.35000                                              
REMARK   3    B12 (A**2) : -0.41000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.167         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.155         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.109         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.572         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2060 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1945 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2757 ; 1.241 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4453 ; 0.702 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   236 ; 6.483 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    91 ;35.944 ;23.187       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   350 ;16.436 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ; 9.336 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   303 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2200 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   474 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   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   : 1.20                                          
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 4ZKS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209465.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19848                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM SODIUM CITRATE PH 4.6, 2.0 M       
REMARK 280  AMMONIUM SULFATE SUPPLEMENTED WITH 5% PEG400, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.37550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.85781            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       14.32033            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.37550            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.85781            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       14.32033            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.37550            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.85781            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       14.32033            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.71562            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       28.64067            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.71562            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       28.64067            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.71562            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       28.64067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, P                                  
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     GLU U   244                                                      
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   SG   CYS U    50     SG   CYS U   111              1.54            
REMARK 500   OD1  ASP U    97     N    LEU U    97B             1.98            
REMARK 500   O    HIS U    37     N    GLY U    37C             2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU P   7   CD    GLU P   7   OE2    -0.079                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP U  97   CB  -  CG  -  OD1 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ASP U  97   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    CYS U 111   CA  -  CB  -  SG  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG P   4   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN U  27       62.74   -161.43                                   
REMARK 500    ARG U  37A     102.12    -21.94                                   
REMARK 500    SER U  54     -157.40   -150.41                                   
REMARK 500    ASP U  97     -152.09   -119.06                                   
REMARK 500    LEU U  97B     -61.88   -121.64                                   
REMARK 500    MET U 126      122.78    -35.55                                   
REMARK 500    TYR U 171     -109.95    -91.05                                   
REMARK 500    SER U 214      -66.69   -122.78                                   
REMARK 500    SER P   2       47.01   -141.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS U   37     ARG U   37A                 149.32                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZKN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZKO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZKR   RELATED DB: PDB                                   
DBREF  4ZKS U   16   244  UNP    P00749   UROK_HUMAN     179    425             
DBREF  4ZKS P    1    10  PDB    4ZKS     4ZKS             1     10             
SEQADV 4ZKS ALA U  122  UNP  P00749    CYS   299 ENGINEERED MUTATION            
SEQADV 4ZKS GLN U  145  UNP  P00749    ASN   322 ENGINEERED MUTATION            
SEQADV 4ZKS ALA U  195  UNP  P00749    SER   376 ENGINEERED MUTATION            
SEQRES   1 U  247  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 U  247  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 U  247  VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS          
SEQRES   4 U  247  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 U  247  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 U  247  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 U  247  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 U  247  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 U  247  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 U  247  GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 U  247  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 U  247  GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 U  247  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 U  247  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 U  247  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 U  247  GLY ASP ALA GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 U  247  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 U  247  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 U  247  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU          
SEQRES   1 P   12  CYS SER ALA ARG GLY LEU GLU ASN HIS ALA ALA CYS              
FORMUL   3  HOH   *89(H2 O)                                                     
HELIX    1 AA1 THR U   23  GLN U   27  5                                   5    
HELIX    2 AA2 ALA U   55  PHE U   59  5                                   5    
HELIX    3 AA3 LYS U   61  GLU U   62A 5                                   3    
HELIX    4 AA4 SER U  164  GLN U  169  1                                   6    
HELIX    5 AA5 TYR U  172  VAL U  176  5                                   5    
HELIX    6 AA6 PHE U  234  LYS U  243  1                                  10    
SHEET    1 AA1 8 GLU U  20  PHE U  21  0                                        
SHEET    2 AA1 8 LYS U 156  ILE U 163 -1  O  MET U 157   N  GLU U  20           
SHEET    3 AA1 8 MET U 180  ALA U 184 -1  O  ALA U 184   N  LYS U 161           
SHEET    4 AA1 8 GLY U 226  ARG U 230 -1  O  TYR U 228   N  LEU U 181           
SHEET    5 AA1 8 ARG U 206  TRP U 215 -1  N  TRP U 215   O  VAL U 227           
SHEET    6 AA1 8 PRO U 198  LEU U 203 -1  N  LEU U 203   O  ARG U 206           
SHEET    7 AA1 8 SER U 135  GLY U 140 -1  N  GLU U 137   O  VAL U 200           
SHEET    8 AA1 8 LYS U 156  ILE U 163 -1  O  VAL U 160   N  CYS U 136           
SHEET    1 AA2 7 PHE U  30  ARG U  36  0                                        
SHEET    2 AA2 7 VAL U  38  SER U  48 -1  O  VAL U  41   N  ILE U  33           
SHEET    3 AA2 7 TRP U  51  SER U  54 -1  O  ILE U  53   N  SER U  45           
SHEET    4 AA2 7 ALA U 104  ARG U 109 -1  O  LEU U 106   N  VAL U  52           
SHEET    5 AA2 7 MET U  81  LEU U  90 -1  N  ILE U  89   O  LEU U 105           
SHEET    6 AA2 7 TYR U  64  LEU U  68 -1  N  VAL U  66   O  PHE U  83           
SHEET    7 AA2 7 PHE U  30  ARG U  36 -1  N  TYR U  34   O  ILE U  65           
SHEET    1 AA3 2 SER U  95  ALA U  96  0                                        
SHEET    2 AA3 2 HIS U  99  HIS U 100 -1  O  HIS U 100   N  SER U  95           
SSBOND   1 CYS U   42    CYS U   58                          1555   1555  2.02  
SSBOND   2 CYS U  136    CYS U  201                          1555   1555  2.02  
SSBOND   3 CYS U  168    CYS U  182                          1555   1555  2.00  
SSBOND   4 CYS U  191    CYS U  220                          1555   1555  2.09  
SSBOND   5 CYS P    1    CYS P   12                          1555   1555  2.03  
CRYST1  120.751  120.751   42.961  90.00  90.00 120.00 H 3           9          
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      0.008282  0.004781  0.000000        0.00000                         
SCALE2      0.000000  0.009563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023277        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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