GenomeNet

Database: PDB
Entry: 4GQ4
LinkDB: 4GQ4
Original site: 4GQ4 
HEADER    TRANSCRIPTION/TRANSCRIPTION INHIBITOR   22-AUG-12   4GQ4              
TITLE     HUMAN MENIN WITH BOUND INHIBITOR MI-2-2                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MEN1, SCG2;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TUMOR SUPPRESSOR, NUCLEUS, TRANSCRIPTION-TRANSCRIPTION INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SHI,M.J.MURAI,S.HE,G.L.LUND,T.HARTLEY,T.PUROHIT,G.REDDY,M.CHRUSZCZ, 
AUTHOR   2 J.GREMBECKA,T.CIERPICKI                                              
REVDAT   3   02-JAN-13 4GQ4    1       JRNL                                     
REVDAT   2   10-OCT-12 4GQ4    1       HETATM                                   
REVDAT   1   19-SEP-12 4GQ4    0                                                
JRNL        AUTH   A.SHI,M.J.MURAI,S.HE,G.LUND,T.HARTLEY,T.PUROHIT,G.REDDY,     
JRNL        AUTH 2 M.CHRUSZCZ,J.GREMBECKA,T.CIERPICKI                           
JRNL        TITL   STRUCTURAL INSIGHTS INTO INHIBITION OF THE BIVALENT          
JRNL        TITL 2 MENIN-MLL INTERACTION BY SMALL MOLECULES IN LEUKEMIA.        
JRNL        REF    BLOOD                         V. 120  4461 2012              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   22936661                                                     
JRNL        DOI    10.1182/BLOOD-2012-05-429274                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 119332                         
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) : 0.151                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6276                            
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) : 1.27                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.30                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5683                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 312                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3690                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 594                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.77000                                              
REMARK   3    B22 (A**2) : 0.23000                                              
REMARK   3    B33 (A**2) : -2.00000                                             
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): 0.046         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.046         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4010 ; 0.022 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2701 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5456 ; 1.983 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6580 ; 4.238 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   497 ; 5.617 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   182 ;32.381 ;23.736       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   663 ;11.652 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;18.370 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   601 ; 0.136 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4483 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   838 ; 0.018 ; 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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3914 ; 7.488 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3822 ;13.817 ; 5.000       
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 4GQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074497.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL                         
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 21-ID-D; 21-ID-F                   
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL; NULL                         
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD; MARMOSAIC    
REMARK 200                                   225 MM CCD                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129732                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.64600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
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   (%): 45.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES PH   
REMARK 280  7.5 AND 25% W/V PEG 3,350. THIS SOLUTION WAS MIXED 1:1 WITH         
REMARK 280  2.5MG/ML PROTEIN IN 50MM TRIS-HCL (PH 8.0), NBM1 PEPTIDE, 50MM      
REMARK 280  NACL, AND 1MM TCEP. PRIOR TO DATA COLLECTION, CRYSTALS WERE         
REMARK 280  TRANSFERRED INTO A CRYO-SOLUTION CONTAINING 20% PEG550 MME AND      
REMARK 280  FLASH-FROZEN IN LIQUID NITROGEN, 200 MM 0RT, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP                                                        
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       24.52200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.40600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.08000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.40600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.52200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.08000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     PRO A   540                                                      
REMARK 465     ALA A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     SER A   543                                                      
REMARK 465     PRO A   544                                                      
REMARK 465     PRO A   545                                                      
REMARK 465     PRO A   546                                                      
REMARK 465     GLU A   547                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     GLN A   590                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     VAL A   592                                                      
REMARK 465     SER A   593                                                      
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  30    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLY A 548    N    CA                                             
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     LYS A 588    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  UNK   UNX A   602    UNK   UNX A   606              1.72            
REMARK 500  UNK   UNX A   605    UNK   UNX A   606              1.82            
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  77      -61.59   -157.50                                   
REMARK 500    ASN A 189       15.89     59.85                                   
REMARK 500    SER A 226       40.31    -92.23                                   
REMARK 500    GLU A 356        2.87     99.60                                   
REMARK 500    ASP A 370      -59.92   -139.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1079        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A1156        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH A1218        DISTANCE =  5.43 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE4 A  612                                                       
REMARK 610     PE4 A  613                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0RT A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 614                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GPQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GQ3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GQ6   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CRYSTALLIZED SEQUENCE CORRESPONDS TO THE HUMAN MENIN ISOFORM 2   
DBREF  4GQ4 A    1   593  UNP    O00255   MEN1_HUMAN       1    593             
SEQADV 4GQ4 GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ4 GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ4 SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ4 SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ4 SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 4GQ4     A       UNP  O00255    ILE    54 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO    55 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    THR    56 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ASN    57 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    VAL    58 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO    59 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU    60 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LEU    61 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    THR    62 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PHE    63 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLN    64 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO    65 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    SER    66 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO    67 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA    68 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO    69 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ASP    70 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO    71 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO    72 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY    73 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    SER   394 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    THR   397 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   460 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   461 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   462 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   463 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   464 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   465 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   466 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   467 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   468 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   469 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   470 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    TRP   471 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   472 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   473 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   474 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   475 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   476 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   477 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   478 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   479 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   480 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   481 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   482 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   483 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   484 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   485 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   486 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    SER   487 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LYS   488 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   489 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   490 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   491 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   492 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   493 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   494 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   495 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LYS   496 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LYS   497 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   498 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   499 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LEU   500 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ASP   501 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LYS   502 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   503 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LEU   504 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   505 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    THR   506 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   507 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLN   508 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   509 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   510 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    VAL   511 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    SER   512 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   513 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   514 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   515 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   516 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    LYS   517 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   518 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   519 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   520 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    THR   521 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    VAL   522 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   523 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   524 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    THR   525 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   526 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ARG   527 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   528 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    PRO   529 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLU   530 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   531 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLY   532 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    SER   533 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    THR   534 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    ALA   535 DELETION                       
SEQADV 4GQ4     A       UNP  O00255    GLN   536 DELETION                       
SEQADV 4GQ4 ALA A  541  UNP  O00255    THR   541 ENGINEERED MUTATION            
SEQRES   1 A  489  GLY GLY SER SER SER MET GLY LEU LYS ALA ALA GLN LYS          
SEQRES   2 A  489  THR LEU PHE PRO LEU ARG SER ILE ASP ASP VAL VAL ARG          
SEQRES   3 A  489  LEU PHE ALA ALA GLU LEU GLY ARG GLU GLU PRO ASP LEU          
SEQRES   4 A  489  VAL LEU LEU SER LEU VAL LEU GLY PHE VAL GLU HIS PHE          
SEQRES   5 A  489  LEU ALA VAL ASN ARG VAL GLY LEU THR TYR PHE PRO VAL          
SEQRES   6 A  489  ALA ASP LEU SER ILE ILE ALA ALA LEU TYR ALA ARG PHE          
SEQRES   7 A  489  THR ALA GLN ILE ARG GLY ALA VAL ASP LEU SER LEU TYR          
SEQRES   8 A  489  PRO ARG GLU GLY GLY VAL SER SER ARG GLU LEU VAL LYS          
SEQRES   9 A  489  LYS VAL SER ASP VAL ILE TRP ASN SER LEU SER ARG SER          
SEQRES  10 A  489  TYR PHE LYS ASP ARG ALA HIS ILE GLN SER LEU PHE SER          
SEQRES  11 A  489  PHE ILE THR GLY THR LYS LEU ASP SER SER GLY VAL ALA          
SEQRES  12 A  489  PHE ALA VAL VAL GLY ALA CYS GLN ALA LEU GLY LEU ARG          
SEQRES  13 A  489  ASP VAL HIS LEU ALA LEU SER GLU ASP HIS ALA TRP VAL          
SEQRES  14 A  489  VAL PHE GLY PRO ASN GLY GLU GLN THR ALA GLU VAL THR          
SEQRES  15 A  489  TRP HIS GLY LYS GLY ASN GLU ASP ARG ARG GLY GLN THR          
SEQRES  16 A  489  VAL ASN ALA GLY VAL ALA GLU ARG SER TRP LEU TYR LEU          
SEQRES  17 A  489  LYS GLY SER TYR MET ARG CYS ASP ARG LYS MET GLU VAL          
SEQRES  18 A  489  ALA PHE MET VAL CYS ALA ILE ASN PRO SER ILE ASP LEU          
SEQRES  19 A  489  HIS THR ASP SER LEU GLU LEU LEU GLN LEU GLN GLN LYS          
SEQRES  20 A  489  LEU LEU TRP LEU LEU TYR ASP LEU GLY HIS LEU GLU ARG          
SEQRES  21 A  489  TYR PRO MET ALA LEU GLY ASN LEU ALA ASP LEU GLU GLU          
SEQRES  22 A  489  LEU GLU PRO THR PRO GLY ARG PRO ASP PRO LEU THR LEU          
SEQRES  23 A  489  TYR HIS LYS GLY ILE ALA SER ALA LYS THR TYR TYR ARG          
SEQRES  24 A  489  ASP GLU HIS ILE TYR PRO TYR MET TYR LEU ALA GLY TYR          
SEQRES  25 A  489  HIS CYS ARG ASN ARG ASN VAL ARG GLU ALA LEU GLN ALA          
SEQRES  26 A  489  TRP ALA ASP THR ALA THR VAL ILE GLN ASP TYR ASN TYR          
SEQRES  27 A  489  CYS ARG GLU ASP GLU GLU ILE TYR LYS GLU PHE PHE GLU          
SEQRES  28 A  489  VAL ALA ASN ASP VAL ILE PRO ASN LEU LEU LYS GLU ALA          
SEQRES  29 A  489  ALA SER LEU LEU GLU ALA GLY SER GLN GLY SER ALA LEU          
SEQRES  30 A  489  GLN ASP PRO GLU CYS PHE ALA HIS LEU LEU ARG PHE TYR          
SEQRES  31 A  489  ASP GLY ILE CYS LYS TRP GLU GLU GLY SER PRO THR PRO          
SEQRES  32 A  489  VAL LEU HIS VAL GLY TRP ALA THR PHE LEU VAL GLN SER          
SEQRES  33 A  489  LEU GLY ARG PHE GLU GLY GLN VAL ARG GLN LYS VAL ARG          
SEQRES  34 A  489  ILE VAL SER VAL PRO ALA PRO ALA ALA SER PRO PRO PRO          
SEQRES  35 A  489  GLU GLY PRO VAL LEU THR PHE GLN SER GLU LYS MET LYS          
SEQRES  36 A  489  GLY MET LYS GLU LEU LEU VAL ALA THR LYS ILE ASN SER          
SEQRES  37 A  489  SER ALA ILE LYS LEU GLN LEU THR ALA GLN SER GLN VAL          
SEQRES  38 A  489  GLN MET LYS LYS GLN LYS VAL SER                              
HET    0RT  A 601      27                                                       
HET    UNX  A 602       1                                                       
HET    UNX  A 603       1                                                       
HET    UNX  A 604       1                                                       
HET    UNX  A 605       1                                                       
HET    UNX  A 606       1                                                       
HET    EPE  A 607      15                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    SO4  A 610       5                                                       
HET    SO4  A 611       5                                                       
HET    PE4  A 612      13                                                       
HET    PE4  A 613      10                                                       
HET    DMS  A 614       4                                                       
HETNAM     0RT 4-[4-(5,5-DIMETHYL-4,5-DIHYDRO-1,3-THIAZOL-2-YL)                 
HETNAM   2 0RT  PIPERAZIN-1-YL]-6-(2,2,2-TRIFLUOROETHYL)THIENO[2,3-             
HETNAM   3 0RT  D]PYRIMIDINE                                                    
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-              
HETNAM   2 PE4  ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL                                 
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     EPE HEPES                                                            
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000                                      
FORMUL   2  0RT    C17 H20 F3 N5 S2                                             
FORMUL   3  UNX    5(X)                                                         
FORMUL   8  EPE    C8 H18 N2 O4 S                                               
FORMUL   9  SO4    4(O4 S 2-)                                                   
FORMUL  13  PE4    2(C16 H34 O8)                                                
FORMUL  15  DMS    C2 H6 O S                                                    
FORMUL  16  HOH   *594(H2 O)                                                    
HELIX    1   1 LYS A    4  THR A    9  1                                   6    
HELIX    2   2 SER A   15  GLY A   28  1                                  14    
HELIX    3   3 ASP A   33  VAL A   50  1                                  18    
HELIX    4   4 ASP A   82  VAL A  101  1                                  20    
HELIX    5   5 ASP A  102  TYR A  106  5                                   5    
HELIX    6   6 ARG A  108  VAL A  112  5                                   5    
HELIX    7   7 SER A  114  SER A  128  1                                  15    
HELIX    8   8 SER A  142  THR A  150  1                                   9    
HELIX    9   9 ASP A  153  LEU A  168  1                                  16    
HELIX   10  10 GLY A  187  GLU A  191  5                                   5    
HELIX   11  11 VAL A  211  GLU A  217  1                                   7    
HELIX   12  12 SER A  219  SER A  226  5                                   8    
HELIX   13  13 ASP A  231  ALA A  242  1                                  12    
HELIX   14  14 SER A  253  GLY A  271  1                                  19    
HELIX   15  15 TYR A  276  GLU A  290  1                                  15    
HELIX   16  16 ASP A  297  TYR A  313  1                                  17    
HELIX   17  17 ILE A  318  ASN A  331  1                                  14    
HELIX   18  18 ASN A  333  GLN A  349  1                                  17    
HELIX   19  19 ASP A  357  ASP A  370  1                                  14    
HELIX   20  20 ASP A  370  ALA A  385  1                                  16    
HELIX   21  21 SER A  402  GLN A  405  5                                   4    
HELIX   22  22 ASP A  406  GLU A  425  1                                  20    
HELIX   23  23 HIS A  433  ARG A  446  1                                  14    
HELIX   24  24 GLU A  448  GLN A  453  1                                   6    
HELIX   25  25 SER A  555  LYS A  562  1                                   8    
HELIX   26  26 GLU A  563  LEU A  565  5                                   3    
HELIX   27  27 ASN A  571  ALA A  581  1                                  11    
SHEET    1   A 4 GLN A 192  ALA A 194  0                                        
SHEET    2   A 4 ALA A 182  PHE A 186 -1  N  VAL A 184   O  ALA A 194           
SHEET    3   A 4 HIS A 174  LEU A 177 -1  N  ALA A 176   O  TRP A 183           
SHEET    4   A 4 MET A 228  ARG A 229 -1  O  MET A 228   N  LEU A 177           
SHEET    1   B 2 SER A 246  ASP A 248  0                                        
SHEET    2   B 2 THR A 251  ASP A 252 -1  O  THR A 251   N  ILE A 247           
SHEET    1   C 2 ARG A 456  VAL A 458  0                                        
SHEET    2   C 2 VAL A 550  THR A 552  1  O  LEU A 551   N  VAL A 458           
CISPEP   1 PHE A   11    PRO A   12          0         2.96                     
CISPEP   2 VAL A  460    PRO A  461          0        12.89                     
SITE     1 AC1 14 SER A 155  LEU A 177  SER A 178  ASP A 180                    
SITE     2 AC1 14 HIS A 181  ALA A 182  PHE A 238  TYR A 276                    
SITE     3 AC1 14 MET A 278  ASN A 282  TYR A 319  MET A 322                    
SITE     4 AC1 14 TYR A 323  HOH A 823                                          
SITE     1 AC2 11 VAL A  50  ASN A 331  ARG A 332  ASN A 333                    
SITE     2 AC2 11 VAL A 334  ARG A 335  GLY A 401  ALA A 403                    
SITE     3 AC2 11 HOH A 966  HOH A1050  HOH A1089                               
SITE     1 AC3  2 ARG A  14  HOH A1243                                          
SITE     1 AC4  5 PHE A  47  GLY A 386  GLN A 400  HOH A 835                    
SITE     2 AC4  5 HOH A 904                                                     
SITE     1 AC5  5 TYR A 133  PHE A 134  LYS A 151  ARG A 332                    
SITE     2 AC5  5 HOH A1291                                                     
SITE     1 AC6  2 ARG A 446  HOH A 858                                          
SITE     1 AC7  6 LEU A  75  THR A  76  PHE A 365  HOH A 728                    
SITE     2 AC7  6 HOH A 913  HOH A 965                                          
SITE     1 AC8  6 TRP A 126  ASN A 127  LEU A 129  SER A 130                    
SITE     2 AC8  6 LYS A 135  TRP A 198                                          
SITE     1 AC9  6 VAL A 185  GLY A 190  GLU A 191  TYR A 227                    
SITE     2 AC9  6 ARG A 229  SER A 583                                          
CRYST1   49.044   80.160  124.812  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      0.020390  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012475  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008012        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system