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Database: PDB
Entry: 1H2L
LinkDB: 1H2L
Original site: 1H2L 
HEADER    TRANSCRIPTION ACTIVATOR/INHIBITOR       12-AUG-02   1H2L              
TITLE     FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA             
TITLE    2 FRAGMENT PEPTIDE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FACTOR INHIBITING HIF1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA;                          
COMPND   7 CHAIN: S;                                                            
COMPND   8 FRAGMENT: C-TERMINAL TRANSACTIVATION DOMAIN FRAGMENT, RESIDUES       
COMPND   9  786-826;                                                            
COMPND  10 SYNONYM: HIF-1 ALPHA, ARNT INTERACTING PROTEIN, MEMBER OF PAS        
COMPND  11  PROTEIN 1;                                                          
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A(+);                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PGEX-GP-1                                 
KEYWDS    TRANSCRIPTION ACTIVATOR-INHIBITOR COMPLEX, TRANSCRIPTION ACTIVATOR    
KEYWDS   2 INHIBITOR COMPLEX, OXYGENASE, TRANSCRIPTION, HYPOXIA, ASPARAGINYL    
KEYWDS   3 HYDROXYLASE, HYDROXYLASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,I.SCHLEMMINGER,J.F.SEIBEL,        
AUTHOR   2 C.J.SCHOFIELD                                                        
REVDAT   5   13-JUL-11 1H2L    1       VERSN                                    
REVDAT   4   22-DEC-09 1H2L    1       VERSN                                    
REVDAT   3   24-FEB-09 1H2L    1       VERSN                                    
REVDAT   2   30-JAN-03 1H2L    1       JRNL                                     
REVDAT   1   28-NOV-02 1H2L    0                                                
JRNL        AUTH   J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,J.F.SEIBEL,              
JRNL        AUTH 2 I.SCHLEMMINGER,C.PUGH,P.RATCLIFFE,C.J.SCHOFIELD              
JRNL        TITL   STRUCTURE OF FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR      
JRNL        TITL 2 (HIF) REVEALS MECHANISM OF OXIDATIVE MODIFICATION OF         
JRNL        TITL 3 HIF-1ALPHA                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 278  1802 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12446723                                                     
JRNL        DOI    10.1074/JBC.C200644200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 25127                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2104                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1783                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 170                          
REMARK   3   BIN FREE R VALUE                    : 0.2280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2863                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 139                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : -0.40000                                             
REMARK   3    B33 (A**2) : 0.80000                                              
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): 0.203         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.165         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.444         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
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):  2961 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2554 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4026 ; 1.404 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5966 ; 0.727 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   350 ; 4.037 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   515 ;18.189 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   413 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3315 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   602 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   693 ; 0.221 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2483 ; 0.204 ; 0.300       
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):   208 ; 0.156 ; 0.500       
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):    16 ; 0.256 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    63 ; 0.259 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.200 ; 0.500       
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):  1767 ; 0.649 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2847 ; 1.227 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1194 ; 1.887 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1179 ; 3.111 ; 4.500       
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 : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    15        A   349                          
REMARK   3    RESIDUE RANGE :   S   795        S   822                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.2240  27.6230  28.5830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1744 T22:   0.0216                                     
REMARK   3      T33:   0.0949 T12:  -0.0059                                     
REMARK   3      T13:  -0.0546 T23:   0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1183 L22:   2.4664                                     
REMARK   3      L33:   1.3415 L12:   0.7934                                     
REMARK   3      L13:   0.5409 L23:   1.2249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0358 S12:  -0.1772 S13:  -0.0521                       
REMARK   3      S21:   0.1763 S22:   0.0025 S23:   0.1089                       
REMARK   3      S31:   0.2114 S32:  -0.0339 S33:  -0.0383                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1H2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-02.                  
REMARK 100 THE PDBE ID CODE IS EBI-11172.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.983                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27294                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.630                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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  (%): 63                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULPHATE, 4% PEG400,       
REMARK 280  0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH            
REMARK 280  1MM FE(II), 2.5MM AKG AND 2.5MM PEPTIDE                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       73.95700            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.13200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.13200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.97850            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.13200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.13200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      110.93550            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.13200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.13200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.97850            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.13200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.13200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      110.93550            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.95700            
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 300 DETAILS:THE PROTEIN IS A DIMERIC   FORMED BY CHAIN                   
REMARK 300  A.A HETERODIMERIC ASSOCIATION OF CHAIN A WITH                       
REMARK 300 CHAIN SPRODUCES A TETRAMER.THE BURIED SURFACE AREA                   
REMARK 300  SHOWN BELOW IS AN AVERAGECALCULATED FOR THE                         
REMARK 300 HETEROTETRAMER AND DOES NOTCORRESPOND TO THE BURIED                  
REMARK 300  SURFACE AREA FOR THEHOMODIMER OF CHAIN A                            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.59 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       86.26400            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       86.26400            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       73.95700            
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     ARG A   305                                                      
REMARK 465     ILE A   306                                                      
REMARK 465     SER S   786                                                      
REMARK 465     MET S   787                                                      
REMARK 465     ASP S   788                                                      
REMARK 465     GLU S   789                                                      
REMARK 465     SER S   790                                                      
REMARK 465     GLY S   791                                                      
REMARK 465     LEU S   792                                                      
REMARK 465     PRO S   793                                                      
REMARK 465     GLN S   794                                                      
REMARK 465     GLN S   807                                                      
REMARK 465     GLY S   808                                                      
REMARK 465     SER S   809                                                      
REMARK 465     ARG S   810                                                      
REMARK 465     ASN S   811                                                      
REMARK 465     LEU S   812                                                      
REMARK 465     ASP S   823                                                      
REMARK 465     GLN S   824                                                      
REMARK 465     VAL S   825                                                      
REMARK 465     ASN S   826                                                      
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     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  87    CG   OD1  ND2                                       
REMARK 470     LYS A 106    CD   CE   NZ                                        
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 133    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 136    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 137    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 157    CD   CE   NZ                                        
REMARK 470     LYS A 311    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   O    ALA A   300     OH   TYR S   798              2.18            
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    ARG A 347   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A 347   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 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    PHE A 100       69.92   -103.96                                   
REMARK 500    GLU A 202       30.06    -93.81                                   
REMARK 500    ILE A 210      -52.49   -120.13                                   
REMARK 500    ARG A 238       -8.37     79.36                                   
REMARK 500    ASN A 246       74.87   -150.51                                   
REMARK 500    TYR A 276       -6.90     78.51                                   
REMARK 500    ASP S 799     -158.26    -95.49                                   
REMARK 500    ALA S 804      148.51   -170.04                                   
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                             FE2 A1350  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 199   NE2                                                    
REMARK 620 2 ASP A 201   OD2 103.4                                              
REMARK 620 3 HIS A 279   NE2  83.1  86.0                                        
REMARK 620 4 AKG A1351   O1  168.9  87.6  98.2                                  
REMARK 620 5 AKG A1351   O5   87.0 169.4  97.2  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A1350                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1352                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG A1351                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D7G   RELATED DB: PDB                                   
REMARK 900  A MODEL FOR THE COMPLEX BETWEEN THE                                 
REMARK 900  HYPOXIA-INDUCIBLE FACTOR-1 (HIF-1) AND ITS                          
REMARK 900   CONSENSUS DEOXYRIBONUCLEIC ACID SEQUENCE                           
REMARK 900 RELATED ID: 1H2K   RELATED DB: PDB                                   
REMARK 900  FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX                            
REMARK 900  WITH HIF-1 ALPHA FRAGMENT PEPTIDE                                   
REMARK 900 RELATED ID: 1H2M   RELATED DB: PDB                                   
REMARK 900  FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX                            
REMARK 900  WITH HIF-1 ALPHA FRAGMENT PEPTIDE                                   
REMARK 900 RELATED ID: 1H2N   RELATED DB: PDB                                   
REMARK 900  FACTOR INHIBITING HIF-1 ALPHA                                       
REMARK 900 RELATED ID: 1L8C   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS FOR HIF-1ALPHA/CBP                                 
REMARK 900  RECOGNITION IN THECELLULAR HYPOXIC RESPONSE                         
REMARK 900 RELATED ID: 1LM8   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A HIF-1A-PVHL-ELONGINB-                                
REMARK 900  ELONGINC COMPLEX                                                    
REMARK 900 RELATED ID: 1LQB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A HYDROXYLATED HIF-1                           
REMARK 900  ALPHA PEPTIDEBOUND TO THE PVHL/ELONGIN-C/                           
REMARK 900  ELONGIN-B COMPLEX                                                   
DBREF  1H2L A    1   349  UNP    Q969Q7   Q969Q7           1    349             
DBREF  1H2L S  786   826  UNP    Q16665   HIFA_HUMAN     786    826             
SEQRES   1 A  349  MET ALA ALA THR ALA ALA GLU ALA VAL ALA SER GLY SER          
SEQRES   2 A  349  GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY PRO ALA          
SEQRES   3 A  349  TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE PRO THR          
SEQRES   4 A  349  ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO ARG ALA          
SEQRES   5 A  349  GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL LEU THR          
SEQRES   6 A  349  ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP ASP LEU          
SEQRES   7 A  349  GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP PHE SER          
SEQRES   8 A  349  VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR TYR ASP          
SEQRES   9 A  349  GLU LYS LYS MET ALA ASN PHE GLN ASN PHE LYS PRO ARG          
SEQRES  10 A  349  SER ASN ARG GLU GLU MET LYS PHE HIS GLU PHE VAL GLU          
SEQRES  11 A  349  LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU GLU ARG          
SEQRES  12 A  349  LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL GLY ARG          
SEQRES  13 A  349  LYS ILE VAL MET ASP PHE LEU GLY PHE ASN TRP ASN TRP          
SEQRES  14 A  349  ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY GLN LEU          
SEQRES  15 A  349  THR SER ASN LEU LEU LEU ILE GLY MET GLU GLY ASN VAL          
SEQRES  16 A  349  THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE PHE ALA          
SEQRES  17 A  349  GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE PRO PRO          
SEQRES  18 A  349  ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL HIS HIS          
SEQRES  19 A  349  PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP ASN PRO          
SEQRES  20 A  349  ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL VAL GLY          
SEQRES  21 A  349  TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU TYR ILE          
SEQRES  22 A  349  PRO MET TYR TRP TRP HIS HIS ILE GLU SER LEU LEU ASN          
SEQRES  23 A  349  GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR LYS GLY          
SEQRES  24 A  349  ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU LYS ALA          
SEQRES  25 A  349  HIS GLN LYS VAL ALA ILE MET ARG ASN ILE GLU LYS MET          
SEQRES  26 A  349  LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL GLY PRO          
SEQRES  27 A  349  LEU LEU ASN THR MET ILE LYS GLY ARG TYR ASN                  
SEQRES   1 S   41  SER MET ASP GLU SER GLY LEU PRO GLN LEU THR SER TYR          
SEQRES   2 S   41  ASP CYS GLU VAL ASN ALA PRO ILE GLN GLY SER ARG ASN          
SEQRES   3 S   41  LEU LEU GLN GLY GLU GLU LEU LEU ARG ALA LEU ASP GLN          
SEQRES   4 S   41  VAL ASN                                                      
HET    FE2  A1350       1                                                       
HET    SO4  A1352       5                                                       
HET    SO4  A1353       5                                                       
HET    AKG  A1351      10                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     AKG 2-OXOGLUTARIC ACID                                               
FORMUL   3  FE2    FE 2+                                                        
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   6  AKG    C5 H6 O5                                                     
FORMUL   7  HOH   *139(H2 O)                                                    
HELIX    1   1 ASP A   28  LEU A   32  5                                   5    
HELIX    2   2 ASP A   49  ASN A   58  1                                  10    
HELIX    3   3 VAL A   70  TRP A   76  5                                   7    
HELIX    4   4 ASP A   77  ILE A   85  1                                   9    
HELIX    5   5 ASP A  104  PHE A  111  5                                   8    
HELIX    6   6 LYS A  124  ARG A  138  1                                  15    
HELIX    7   7 GLY A  155  GLY A  164  1                                  10    
HELIX    8   8 ASN A  166  GLY A  178  1                                  13    
HELIX    9   9 PRO A  220  ASP A  222  5                                   3    
HELIX   10  10 GLN A  223  TYR A  228  1                                   6    
HELIX   11  11 PHE A  252  VAL A  258  5                                   7    
HELIX   12  12 LYS A  311  GLY A  331  1                                  21    
HELIX   13  13 ASN A  332  GLN A  334  5                                   3    
HELIX   14  14 GLU A  335  LYS A  345  1                                  11    
HELIX   15  15 GLN S  814  LEU S  822  1                                   9    
SHEET    1  AA 5 THR A  39  PRO A  41  0                                        
SHEET    2  AA 5 GLY A 260  VAL A 265  1  O  GLY A 260   N  ARG A  40           
SHEET    3  AA 5 LYS A 214  PHE A 219 -1  O  LYS A 214   N  VAL A 265           
SHEET    4  AA 5 TRP A 278  SER A 283 -1  O  TRP A 278   N  PHE A 219           
SHEET    5  AA 5 VAL A 195  HIS A 199 -1  O  THR A 196   N  ILE A 281           
SHEET    1  AB 6 ARG A  44  LEU A  45  0                                        
SHEET    2  AB 6 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3  AB 6 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4  AB 6 GLN A 204  LYS A 211 -1  O  ASN A 205   N  ILE A 273           
SHEET    5  AB 6 THR A 290  TYR A 297 -1  O  ILE A 291   N  ILE A 210           
SHEET    6  AB 6 LEU A 182  SER A 184 -1  N  THR A 183   O  TRP A 296           
SHEET    1  AC 9 ARG A  44  LEU A  45  0                                        
SHEET    2  AC 9 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3  AC 9 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4  AC 9 GLN A 204  LYS A 211 -1  O  ASN A 205   N  ILE A 273           
SHEET    5  AC 9 THR A 290  TYR A 297 -1  O  ILE A 291   N  ILE A 210           
SHEET    6  AC 9 LEU A 186  GLY A 190 -1  O  LEU A 186   N  ASN A 294           
SHEET    7  AC 9 ARG A 143  THR A 149 -1  O  LEU A 146   N  ILE A 189           
SHEET    8  AC 9 PHE A  90  ALA A  95 -1  O  SER A  91   N  GLN A 147           
SHEET    9  AC 9 SER A 118  MET A 123 -1  O  ASN A 119   N  SER A  94           
LINK        FE   FE2 A1350                 NE2 HIS A 199     1555   1555  2.06  
LINK        FE   FE2 A1350                 OD2 ASP A 201     1555   1555  2.09  
LINK        FE   FE2 A1350                 NE2 HIS A 279     1555   1555  2.05  
LINK        FE   FE2 A1350                 O1  AKG A1351     1555   1555  2.07  
LINK        FE   FE2 A1350                 O5  AKG A1351     1555   1555  2.18  
CISPEP   1 TYR A  308    PRO A  309          0         1.27                     
SITE     1 AC1  4 HIS A 199  ASP A 201  HIS A 279  AKG A1351                    
SITE     1 AC2  4 ARG A 138  GLY A 140  GLU A 141  GLU A 142                    
SITE     1 AC3  5 ARG A 143  GLU A 192  GLY A 193  LEU A 285                    
SITE     2 AC3  5 ASN A 286                                                     
SITE     1 AC4 13 TYR A 145  THR A 196  HIS A 199  ASP A 201                    
SITE     2 AC4 13 ASN A 205  PHE A 207  LYS A 214  HIS A 279                    
SITE     3 AC4 13 ILE A 281  ASN A 294  TRP A 296  FE2 A1350                    
SITE     4 AC4 13 HOH A2065                                                     
CRYST1   86.264   86.264  147.914  90.00  90.00  90.00 P 41 21 2     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      0.011592  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011592  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006761        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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