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Database: PDB
Entry: 5V60
LinkDB: 5V60
Original site: 5V60 
HEADER    TRANSFERASE                             15-MAR-17   5V60              
TITLE     PHOSPHO-ERK2 BOUND TO AMP-PCP                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   6 MAPK 2;                                                              
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 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: MAPK1, ERK2, PRKM1, PRKM2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE, MAPK, PHOSPHORYLATION, CANCER, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.C.LECHTENBERG,S.J.RIEDL                                             
REVDAT   3   18-APR-18 5V60    1       JRNL                                     
REVDAT   2   13-SEP-17 5V60    1       REMARK                                   
REVDAT   1   26-JUL-17 5V60    0                                                
JRNL        AUTH   B.C.LECHTENBERG,P.D.MACE,E.H.SESSIONS,R.WILLIAMSON,          
JRNL        AUTH 2 R.STALDER,Y.WALLEZ,G.P.ROTH,S.J.RIEDL,E.B.PASQUALE           
JRNL        TITL   STRUCTURE-GUIDED STRATEGY FOR THE DEVELOPMENT OF POTENT      
JRNL        TITL 2 BIVALENT ERK INHIBITORS.                                     
JRNL        REF    ACS MED CHEM LETT             V.   8   726 2017              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   28740606                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.7B00127                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.18 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 25169                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1336                            
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) : 2.18                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.24                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1821                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.3260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2858                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 82                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.57000                                              
REMARK   3    B22 (A**2) : -0.17000                                             
REMARK   3    B33 (A**2) : -1.40000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.207         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.417        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3052 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2818 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4126 ; 1.339 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6545 ; 0.913 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   359 ; 5.643 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   142 ;38.061 ;24.155       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   529 ;12.516 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.197 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   450 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3291 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   602 ; 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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   358                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3379  17.5870  23.9478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0513 T22:   0.0278                                     
REMARK   3      T33:   0.0937 T12:   0.0082                                     
REMARK   3      T13:   0.0025 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2358 L22:   0.9660                                     
REMARK   3      L33:   3.3391 L12:   0.0104                                     
REMARK   3      L13:   0.1110 L23:  -0.0517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0481 S12:   0.1534 S13:   0.0194                       
REMARK   3      S21:   0.2102 S22:   0.0144 S23:  -0.0589                       
REMARK   3      S31:   0.0193 S32:   0.1543 S33:  -0.0625                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
REMARK   4                                                                      
REMARK   4 5V60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226913.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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 FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26555                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.180                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.92600                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2ERK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 45% V/V           
REMARK 280  POLYPROPYLENE GLYCOL P400, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       20.87850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.28300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.25800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.28300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.87850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.25800            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     SER A   360                                                      
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   O2G  ACP A   401     O    HOH A   501              2.05            
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    TYR A  36       31.11   -142.56                                   
REMARK 500    ASP A 149       37.56   -151.89                                   
REMARK 500    ASP A 167       75.29     60.56                                   
REMARK 500    ALA A 189      168.41     66.70                                   
REMARK 500    ASN A 201       61.02   -151.03                                   
REMARK 500    LEU A 294       48.01    -92.43                                   
REMARK 500    LEU A 294       48.01    -93.08                                   
REMARK 500    ASP A 318       96.00   -160.69                                   
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                              MG A 408  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 154   OD1                                                    
REMARK 620 2 ASP A 167   OD2  85.7                                              
REMARK 620 3 ACP A 401   O2G 139.8  60.8                                        
REMARK 620 4 ACP A 401   O2A  98.7  89.9 102.6                                  
REMARK 620 5 HOH A 501   O   106.2  89.0  55.7 155.0                            
REMARK 620 6 HOH A 550   O    91.2 172.4 124.6  83.7  98.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 409  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 167   OD1                                                    
REMARK 620 2 ASP A 167   OD2  56.0                                              
REMARK 620 3 ACP A 401   O1G 163.0 127.3                                        
REMARK 620 4 ACP A 401   O2G 112.0  57.2  70.3                                  
REMARK 620 5 ACP A 401   O2B  88.9  96.9  74.3  87.5                            
REMARK 620 6 HOH A 508   O   104.8 160.5  71.9 142.2  84.8                      
REMARK 620 7 HOH A 552   O    82.3  81.2 114.3  99.1 170.6  94.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 409                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5V61   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5V62   RELATED DB: PDB                                   
DBREF  5V60 A    8   360  UNP    P28482   MK01_HUMAN       8    360             
SEQADV 5V60 GLY A    5  UNP  P28482              EXPRESSION TAG                 
SEQADV 5V60 PRO A    6  UNP  P28482              EXPRESSION TAG                 
SEQADV 5V60 GLY A    7  UNP  P28482              EXPRESSION TAG                 
SEQRES   1 A  356  GLY PRO GLY GLY ALA GLY PRO GLU MET VAL ARG GLY GLN          
SEQRES   2 A  356  VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR          
SEQRES   3 A  356  ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR          
SEQRES   4 A  356  ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE          
SEQRES   5 A  356  SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU          
SEQRES   6 A  356  ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN          
SEQRES   7 A  356  ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE          
SEQRES   8 A  356  GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET          
SEQRES   9 A  356  GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU          
SEQRES  10 A  356  SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU          
SEQRES  11 A  356  ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS          
SEQRES  12 A  356  ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR          
SEQRES  13 A  356  CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL          
SEQRES  14 A  356  ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU TPO GLU          
SEQRES  15 A  356  PTR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET          
SEQRES  16 A  356  LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP          
SEQRES  17 A  356  SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG          
SEQRES  18 A  356  PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN          
SEQRES  19 A  356  HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP          
SEQRES  20 A  356  LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU          
SEQRES  21 A  356  LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG          
SEQRES  22 A  356  LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU          
SEQRES  23 A  356  ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU          
SEQRES  24 A  356  VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR          
SEQRES  25 A  356  TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE          
SEQRES  26 A  356  LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS          
SEQRES  27 A  356  LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN          
SEQRES  28 A  356  PRO GLY TYR ARG SER                                          
MODRES 5V60 TPO A  185  THR  MODIFIED RESIDUE                                   
MODRES 5V60 PTR A  187  TYR  MODIFIED RESIDUE                                   
HET    TPO  A 185      11                                                       
HET    PTR  A 187      16                                                       
HET    ACP  A 401      31                                                       
HET    GOL  A 402       6                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HET    GOL  A 407       6                                                       
HET     MG  A 408       1                                                       
HET     MG  A 409       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE                 
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   2  ACP    C11 H18 N5 O12 P3                                            
FORMUL   3  GOL    6(C3 H8 O3)                                                  
FORMUL   9   MG    2(MG 2+)                                                     
FORMUL  11  HOH   *82(H2 O)                                                     
HELIX    1 AA1 HIS A   61  PHE A   78  1                                  18    
HELIX    2 AA2 LEU A  112  GLN A  119  1                                   8    
HELIX    3 AA3 SER A  122  ALA A  143  1                                  22    
HELIX    4 AA4 LYS A  151  SER A  153  5                                   3    
HELIX    5 AA5 THR A  190  ARG A  194  5                                   5    
HELIX    6 AA6 ALA A  195  ASN A  201  1                                   7    
HELIX    7 AA7 LYS A  207  ASN A  224  1                                  18    
HELIX    8 AA8 HIS A  232  GLY A  245  1                                  14    
HELIX    9 AA9 SER A  248  CYS A  254  1                                   7    
HELIX   10 AB1 ASN A  257  SER A  266  1                                  10    
HELIX   11 AB2 PRO A  274  PHE A  279  1                                   6    
HELIX   12 AB3 ASP A  283  LEU A  294  1                                  12    
HELIX   13 AB4 GLU A  303  ALA A  309  1                                   7    
HELIX   14 AB5 HIS A  310  GLU A  314  5                                   5    
HELIX   15 AB6 ASP A  318  GLU A  322  5                                   5    
HELIX   16 AB7 LYS A  330  LEU A  335  5                                   6    
HELIX   17 AB8 PRO A  339  THR A  351  1                                  13    
HELIX   18 AB9 ALA A  352  GLN A  355  5                                   4    
SHEET    1 AA1 2 MET A  13  VAL A  14  0                                        
SHEET    2 AA1 2 GLN A  17  VAL A  18 -1  O  GLN A  17   N  VAL A  14           
SHEET    1 AA2 5 TYR A  25  GLY A  34  0                                        
SHEET    2 AA2 5 GLY A  37  ASP A  44 -1  O  VAL A  39   N  GLY A  32           
SHEET    3 AA2 5 VAL A  49  ILE A  56 -1  O  VAL A  49   N  ASP A  44           
SHEET    4 AA2 5 VAL A 101  ASP A 106 -1  O  GLN A 105   N  ALA A  52           
SHEET    5 AA2 5 ASP A  88  ILE A  90 -1  N  ASP A  88   O  VAL A 104           
SHEET    1 AA3 3 THR A 110  ASP A 111  0                                        
SHEET    2 AA3 3 LEU A 155  LEU A 157 -1  O  LEU A 157   N  THR A 110           
SHEET    3 AA3 3 LEU A 163  ILE A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1 AA4 2 VAL A 145  LEU A 146  0                                        
SHEET    2 AA4 2 ARG A 172  VAL A 173 -1  O  ARG A 172   N  LEU A 146           
LINK         OD1 ASN A 154                MG    MG A 408     1555   1555  2.22  
LINK         OD1 ASP A 167                MG    MG A 409     1555   1555  2.21  
LINK         OD2 ASP A 167                MG    MG A 409     1555   1555  2.42  
LINK         OD2 ASP A 167                MG    MG A 408     1555   1555  2.17  
LINK         C   LEU A 184                 N   TPO A 185     1555   1555  1.33  
LINK         C   TPO A 185                 N   GLU A 186     1555   1555  1.33  
LINK         C   GLU A 186                 N   PTR A 187     1555   1555  1.33  
LINK         C   PTR A 187                 N   VAL A 188     1555   1555  1.33  
LINK         O1G ACP A 401                MG    MG A 409     1555   1555  2.20  
LINK         O2G ACP A 401                MG    MG A 409     1555   1555  2.20  
LINK         O2G ACP A 401                MG    MG A 408     1555   1555  2.22  
LINK         O2B ACP A 401                MG    MG A 409     1555   1555  2.17  
LINK         O2A ACP A 401                MG    MG A 408     1555   1555  2.19  
LINK        MG    MG A 408                 O   HOH A 501     1555   1555  2.19  
LINK        MG    MG A 408                 O   HOH A 550     1555   1555  2.18  
LINK        MG    MG A 409                 O   HOH A 508     1555   1555  2.18  
LINK        MG    MG A 409                 O   HOH A 552     1555   1555  2.19  
CISPEP   1 GLY A   22    PRO A   23          0         1.47                     
SITE     1 AC1 23 ILE A  31  GLU A  33  GLY A  34  VAL A  39                    
SITE     2 AC1 23 ALA A  52  LYS A  54  ASP A 106  MET A 108                    
SITE     3 AC1 23 ASP A 111  LYS A 114  SER A 153  ASN A 154                    
SITE     4 AC1 23 LEU A 156  ASP A 167   MG A 408   MG A 409                    
SITE     5 AC1 23 HOH A 501  HOH A 505  HOH A 508  HOH A 527                    
SITE     6 AC1 23 HOH A 544  HOH A 550  HOH A 569                               
SITE     1 AC2  3 ASN A 158  THR A 159  CYS A 161                               
SITE     1 AC3  2 LEU A 234  TYR A 263                                          
SITE     1 AC4  1 HIS A 120                                                     
SITE     1 AC5  4 GLU A  81  TYR A 128  ASP A 321  HOH A 513                    
SITE     1 AC6  5 ASN A 154  ASP A 167  ACP A 401  HOH A 501                    
SITE     2 AC6  5 HOH A 550                                                     
SITE     1 AC7  4 ASP A 167  ACP A 401  HOH A 508  HOH A 552                    
CRYST1   41.757   78.516  152.566  90.00  90.00  90.00 P 21 21 21    4          
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      0.023948  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012736  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006555        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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