GenomeNet

Database: PDB
Entry: 2VQ3
LinkDB: 2VQ3
Original site: 2VQ3 
HEADER    OXIDOREDUCTASE                          10-MAR-08   2VQ3              
TITLE     CRYSTAL STRUCTURE OF THE MEMBRANE PROXIMAL OXIDOREDUCTASE             
TITLE    2 DOMAIN OF HUMAN STEAP3, THE DOMINANT FERRIC REDUCTASE OF             
TITLE    3 THE ERYTHROID TRANSFERRIN CYCLE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METALLOREDUCTASE STEAP3;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: NADPH/FLAVIN DEPENDENT OXIDOREDUCTASE, RESIDUES            
COMPND   5  1-215;                                                              
COMPND   6 SYNONYM: STEAP3 DIMER WITH NADPH, SIX-TRANSMEMBRANE                  
COMPND   7  EPITHELIAL ANTIGEN OF PROSTATE 3, TUMOR                             
COMPND   8  SUPPRESSOR-ACTIVATED PATHWAY PROTEIN 6, HTSAP6, PHYDE,              
COMPND   9  HPHYDE, DUDULIN-2;                                                  
COMPND  10 EC: 1.16.1.2, 1.16.1.-;                                              
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: RESIDUES 1-215 CLONED, NADPH BOUND                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: KIDNEY;                                                       
SOURCE   6 TISSUE: RENAL CELL ADENOCARCINOMA;                                   
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VARIANT: RIL;                                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PDEST14                                   
KEYWDS    METAL-BINDING, TRANSMEMBRANE, ROSSMANN FOLD, TRANSPORT,               
KEYWDS   2 CELL CYCLE, TRANSFERRIN, FLAVOPROTEIN, ALTERNATIVE                   
KEYWDS   3 SPLICING, TRANSFERRIN RECEPTOR, FERRIREDUCTASE, FERRIC-              
KEYWDS   4 REDUCTASE, IRON TRANSPORT, PHOSPHOPROTEIN, OXIDOREDUCTASE,           
KEYWDS   5 STEAP3, COPPER, MEMBRANE, ENDOSOME, APOPTOSIS, TF, NAD,              
KEYWDS   6 TFR, FAD, FNO, NADP, TFR1, IRON, STEAP, POLYMORPHISM,                
KEYWDS   7 GLYCOPROTEIN, ION TRANSPORT, DINUCLEOTIDE-BINDING DOMAIN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.SENDAMARAI,R.S.OHGAMI,M.D.FLEMING,C.M.LAWRENCE                    
REVDAT   3   24-FEB-09 2VQ3    1       VERSN                                    
REVDAT   2   03-JUN-08 2VQ3    1       JRNL                                     
REVDAT   1   06-MAY-08 2VQ3    0                                                
JRNL        AUTH   A.K.SENDAMARAI,R.S.OHGAMI,M.D.FLEMING,C.M.LAWRENCE           
JRNL        TITL   STRUCTURE OF THE MEMBRANE PROXIMAL OXIDOREDUCTASE            
JRNL        TITL 2 DOMAIN OF HUMAN STEAP3, THE DOMINANT                         
JRNL        TITL 3 FERRIREDUCTASE OF THE ERYTHROID TRANSFERRIN CYCLE            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  7410 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18495927                                                     
JRNL        DOI    10.1073/PNAS.0801318105                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.S.OHGAMI,D.R.CAMPAGNA,E.L.GREER,B.ANTIOCHOS,               
REMARK   1  AUTH 2 A.MCDONALD,J.CHEN,J.J.SHARP,Y.FUJIWARA,J.E.BARKER,           
REMARK   1  AUTH 3 M.D.FLEMING                                                  
REMARK   1  TITL   IDENTIFICATION OF A FERRIREDUCTASE REQUIRED FOR              
REMARK   1  TITL 2 EFFICIENT TRANSFERRIN-DEPENDENT IRON UPTAKE IN               
REMARK   1  TITL 3 ERYTHROID CELLS                                              
REMARK   1  REF    NAT.GENET.                    V.  37  1264 2005              
REMARK   1  REFN                   ISSN 1061-4036                               
REMARK   1  PMID   16227996                                                     
REMARK   1  DOI    10.1038/NG1658                                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   R.S.OHGAMI,D.R.CAMPAGNA,B.ANTIOCHOS,E.B.WOOD,                
REMARK   1  AUTH 2 J.J.SHARP,J.E.BARKER,M.D.FLEMING                             
REMARK   1  TITL   NM1054, A SPONTANEOUS, RECESSIVE, HYPOCHROMIC,               
REMARK   1  TITL 2 MICROCYTIC ANEMIA MUTATION IN THE MOUSE                      
REMARK   1  REF    BLOOD                         V. 106  3625 2005              
REMARK   1  REFN                   ISSN 0006-4971                               
REMARK   1  PMID   15994289                                                     
REMARK   1  DOI    10.1182/BLOOD-2005-01-0379                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23736                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1293                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1620                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 97                           
REMARK   3   BIN FREE R VALUE                    : 0.2920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2794                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 109                                     
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.22000                                              
REMARK   3    B22 (A**2) : 1.73000                                              
REMARK   3    B33 (A**2) : -1.95000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.907         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2967 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1990 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4055 ; 1.498 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4852 ; 3.295 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   374 ;38.944 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;33.631 ;23.613       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   467 ;15.863 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;20.298 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   457 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3284 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   578 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   618 ; 0.237 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2002 ; 0.241 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1444 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1543 ; 0.099 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   143 ; 0.191 ; 0.200       
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):    19 ; 0.277 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.302 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.291 ; 0.200       
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):  2329 ; 1.531 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2967 ; 1.673 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1278 ; 2.058 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1086 ; 2.925 ; 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  : NULL                                       
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   : 1.20                                          
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          
REMARK   3  RIDING POSITIONS. DISORDERED REGION BETWEEN RESIDUES 159 TO         
REMARK   3  164 HAS POOR DENSITY FOR SIDE CHAINS.                               
REMARK   4                                                                      
REMARK   4 2VQ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-35648.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1271                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : FLAT COLLIMATING MIRROR,           
REMARK 200                                   DOUBLE CRYSTAL                     
REMARK 200                                   MONOCHROMATOR, TOROID              
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27874                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.92                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.9                                
REMARK 200  R MERGE                    (I) : 0.03                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.27                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2VNS                                       
REMARK 200                                                                      
REMARK 200 REMARK: RIGID BODY REFINED AND FURTHER REFINE FROM APO-              
REMARK 200  STRUCTURE 2VNS                                                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M FECL3, 40-100MM                    
REMARK 280  NA3.CITRATE, 4% V/V JEFFAMINE M600 PH5.6                            
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       18.84300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.68300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.40600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.68300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.84300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.40600            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY:  1.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     ALA A   211                                                      
REMARK 465     TRP A   212                                                      
REMARK 465     LYS A   213                                                      
REMARK 465     VAL A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     VAL B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     ASP B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     LEU B   209                                                      
REMARK 465     PRO B   210                                                      
REMARK 465     ALA B   211                                                      
REMARK 465     TRP B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     VAL B   214                                                      
REMARK 465     PRO B   215                                                      
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     ASP A 104    CG   OD1  OD2                                       
REMARK 470     LEU A 209    CG   CD1  CD2                                       
REMARK 470     LEU B 208    CG   CD1  CD2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     ARG B  63    CG   CD   NE   CZ  NH1  NH2                         
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   NH1  ARG A    46  -  O    MET A   185              2.02            
REMARK 500   OG   SER B    36  -  O3X  NAP B  1210              1.86            
REMARK 500   CE   MET B   188  -  O    HOH B  2043              1.20            
REMARK 500   O2X  NAP A  1210  -  O    HOH A  2060              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   OG   SER A    82     OG   SER B    82     4546      2.04           
REMARK 500   OG   SER B    82     OG   SER A    82     4446      2.04           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR A  45   C     ARG A  46   N      -0.207                       
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    GLY A 161   N   -  CA  -  C   ANGL. DEV. = -16.4 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 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    ALA A  90       58.10    -99.90                                   
REMARK 500    PHE A 146        2.87     84.62                                   
REMARK 500    LEU A 208      -93.17    -97.67                                   
REMARK 500    ALA B  90       56.65    -98.78                                   
REMARK 500    PHE B 146        4.64     84.37                                   
REMARK 500    ARG B 159       24.46    -73.88                                   
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B1210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A1211                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VNS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MEMBRANE PROXIMAL                          
REMARK 900  OXIDOREDUCTASE DOMAIN OF HUMAN STEAP3, THE                          
REMARK 900  DOMINANT FERRIC REDUCTASE OF THE ERYTHROID                          
REMARK 900  TRANSFERRIN CYCLE                                                   
DBREF  2VQ3 A    1   215  UNP    Q658P3   STEA3_HUMAN      1    215             
DBREF  2VQ3 B    1   215  UNP    Q658P3   STEA3_HUMAN      1    215             
SEQRES   1 A  215  MET PRO GLU GLU MET ASP LYS PRO LEU ILE SER LEU HIS          
SEQRES   2 A  215  LEU VAL ASP SER ASP SER SER LEU ALA LYS VAL PRO ASP          
SEQRES   3 A  215  GLU ALA PRO LYS VAL GLY ILE LEU GLY SER GLY ASP PHE          
SEQRES   4 A  215  ALA ARG SER LEU ALA THR ARG LEU VAL GLY SER GLY PHE          
SEQRES   5 A  215  LYS VAL VAL VAL GLY SER ARG ASN PRO LYS ARG THR ALA          
SEQRES   6 A  215  ARG LEU PHE PRO SER ALA ALA GLN VAL THR PHE GLN GLU          
SEQRES   7 A  215  GLU ALA VAL SER SER PRO GLU VAL ILE PHE VAL ALA VAL          
SEQRES   8 A  215  PHE ARG GLU HIS TYR SER SER LEU CYS SER LEU SER ASP          
SEQRES   9 A  215  GLN LEU ALA GLY LYS ILE LEU VAL ASP VAL SER ASN PRO          
SEQRES  10 A  215  THR GLU GLN GLU HIS LEU GLN HIS ARG GLU SER ASN ALA          
SEQRES  11 A  215  GLU TYR LEU ALA SER LEU PHE PRO THR CYS THR VAL VAL          
SEQRES  12 A  215  LYS ALA PHE ASN VAL ILE SER ALA TRP THR LEU GLN ALA          
SEQRES  13 A  215  GLY PRO ARG ASP GLY ASN ARG GLN VAL PRO ILE CYS GLY          
SEQRES  14 A  215  ASP GLN PRO GLU ALA LYS ARG ALA VAL SER GLU MET ALA          
SEQRES  15 A  215  LEU ALA MET GLY PHE MET PRO VAL ASP MET GLY SER LEU          
SEQRES  16 A  215  ALA SER ALA TRP GLU VAL GLU ALA MET PRO LEU ARG LEU          
SEQRES  17 A  215  LEU PRO ALA TRP LYS VAL PRO                                  
SEQRES   1 B  215  MET PRO GLU GLU MET ASP LYS PRO LEU ILE SER LEU HIS          
SEQRES   2 B  215  LEU VAL ASP SER ASP SER SER LEU ALA LYS VAL PRO ASP          
SEQRES   3 B  215  GLU ALA PRO LYS VAL GLY ILE LEU GLY SER GLY ASP PHE          
SEQRES   4 B  215  ALA ARG SER LEU ALA THR ARG LEU VAL GLY SER GLY PHE          
SEQRES   5 B  215  LYS VAL VAL VAL GLY SER ARG ASN PRO LYS ARG THR ALA          
SEQRES   6 B  215  ARG LEU PHE PRO SER ALA ALA GLN VAL THR PHE GLN GLU          
SEQRES   7 B  215  GLU ALA VAL SER SER PRO GLU VAL ILE PHE VAL ALA VAL          
SEQRES   8 B  215  PHE ARG GLU HIS TYR SER SER LEU CYS SER LEU SER ASP          
SEQRES   9 B  215  GLN LEU ALA GLY LYS ILE LEU VAL ASP VAL SER ASN PRO          
SEQRES  10 B  215  THR GLU GLN GLU HIS LEU GLN HIS ARG GLU SER ASN ALA          
SEQRES  11 B  215  GLU TYR LEU ALA SER LEU PHE PRO THR CYS THR VAL VAL          
SEQRES  12 B  215  LYS ALA PHE ASN VAL ILE SER ALA TRP THR LEU GLN ALA          
SEQRES  13 B  215  GLY PRO ARG ASP GLY ASN ARG GLN VAL PRO ILE CYS GLY          
SEQRES  14 B  215  ASP GLN PRO GLU ALA LYS ARG ALA VAL SER GLU MET ALA          
SEQRES  15 B  215  LEU ALA MET GLY PHE MET PRO VAL ASP MET GLY SER LEU          
SEQRES  16 B  215  ALA SER ALA TRP GLU VAL GLU ALA MET PRO LEU ARG LEU          
SEQRES  17 B  215  LEU PRO ALA TRP LYS VAL PRO                                  
HET    NAP  A1210      48                                                       
HET    NAP  B1210      48                                                       
HET    CIT  A1211      13                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE                           
HETNAM   2 NAP  PHOSPHATE                                                       
HETNAM     CIT CITRIC ACID                                                      
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  CIT    C6 H8 O7                                                     
FORMUL   5  HOH   *125(H2 O1)                                                   
HELIX    1   1 GLY A   37  SER A   50  1                                  14    
HELIX    2   2 ASN A   60  ARG A   66  1                                   7    
HELIX    3   3 GLN A   77  VAL A   81  1                                   5    
HELIX    4   4 PHE A   92  TYR A   96  5                                   5    
HELIX    5   5 TYR A   96  SER A  101  5                                   6    
HELIX    6   6 LEU A  102  ALA A  107  1                                   6    
HELIX    7   7 THR A  118  HIS A  125  1                                   8    
HELIX    8   8 SER A  128  PHE A  137  1                                  10    
HELIX    9   9 SER A  150  GLY A  157  1                                   8    
HELIX   10  10 GLN A  171  MET A  185  1                                  15    
HELIX   11  11 SER A  194  ALA A  196  5                                   3    
HELIX   12  12 SER A  197  ALA A  203  1                                   7    
HELIX   13  13 GLY B   37  SER B   50  1                                  14    
HELIX   14  14 ASN B   60  ARG B   66  1                                   7    
HELIX   15  15 GLN B   77  VAL B   81  1                                   5    
HELIX   16  16 PHE B   92  SER B  101  5                                  10    
HELIX   17  17 LEU B  102  ALA B  107  1                                   6    
HELIX   18  18 THR B  118  HIS B  125  1                                   8    
HELIX   19  19 SER B  128  PHE B  137  1                                  10    
HELIX   20  20 SER B  150  GLY B  157  1                                   8    
HELIX   21  21 GLN B  171  MET B  185  1                                  15    
HELIX   22  22 SER B  194  ALA B  196  5                                   3    
HELIX   23  23 SER B  197  ALA B  203  1                                   7    
SHEET    1  AA 8 GLN A  73  PHE A  76  0                                        
SHEET    2  AA 8 VAL A  54  SER A  58  1  O  VAL A  54   N  GLN A  73           
SHEET    3  AA 8 VAL A  31  LEU A  34  1  O  VAL A  31   N  VAL A  55           
SHEET    4  AA 8 VAL A  86  VAL A  89  1  O  VAL A  86   N  GLY A  32           
SHEET    5  AA 8 ILE A 110  ASP A 113  1  O  ILE A 110   N  ILE A  87           
SHEET    6  AA 8 THR A 141  ALA A 145  1  O  THR A 141   N  LEU A 111           
SHEET    7  AA 8 GLN A 164  GLY A 169 -1  O  CYS A 168   N  LYS A 144           
SHEET    8  AA 8 MET A 188  ASP A 191  1  O  MET A 188   N  VAL A 165           
SHEET    1  BA 8 GLN B  73  PHE B  76  0                                        
SHEET    2  BA 8 VAL B  54  SER B  58  1  O  VAL B  54   N  GLN B  73           
SHEET    3  BA 8 VAL B  31  LEU B  34  1  O  VAL B  31   N  VAL B  55           
SHEET    4  BA 8 VAL B  86  VAL B  89  1  O  VAL B  86   N  GLY B  32           
SHEET    5  BA 8 ILE B 110  ASP B 113  1  O  ILE B 110   N  ILE B  87           
SHEET    6  BA 8 THR B 141  ALA B 145  1  O  THR B 141   N  LEU B 111           
SHEET    7  BA 8 GLN B 164  GLY B 169 -1  O  CYS B 168   N  LYS B 144           
SHEET    8  BA 8 MET B 188  ASP B 191  1  O  MET B 188   N  VAL B 165           
CISPEP   1 PRO A   29    LYS A   30          0       -14.72                     
CISPEP   2 ASP A  160    GLY A  161          0        -9.94                     
CISPEP   3 PRO B   29    LYS B   30          0       -26.22                     
CISPEP   4 ARG B  207    LEU B  208          0        -7.70                     
SITE     1 AC1 24 SER A  36  GLY A  37  ASP A  38  PHE A  39                    
SITE     2 AC1 24 SER A  58  ARG A  59  ALA A  90  VAL A  91                    
SITE     3 AC1 24 PHE A  92  HIS A  95  SER A  98  VAL A 114                    
SITE     4 AC1 24 SER A 115  ASN A 116  ASN A 147  ILE A 149                    
SITE     5 AC1 24 SER A 150  ALA A 151  HOH A2013  HOH A2057                    
SITE     6 AC1 24 HOH A2058  HOH A2059  HOH A2060  HOH A2061                    
SITE     1 AC2 24 GLY B  35  SER B  36  GLY B  37  ASP B  38                    
SITE     2 AC2 24 PHE B  39  SER B  58  ARG B  59  ALA B  90                    
SITE     3 AC2 24 VAL B  91  PHE B  92  HIS B  95  SER B  98                    
SITE     4 AC2 24 VAL B 114  SER B 115  ASN B 116  ILE B 149                    
SITE     5 AC2 24 ALA B 151  HOH B2014  HOH B2023  HOH B2058                    
SITE     6 AC2 24 HOH B2060  HOH B2061  HOH B2062  HOH B2063                    
SITE     1 AC3  3 LYS B  62  ARG B  66  HOH C2001                               
CRYST1   37.686   66.812  143.366  90.00  90.00  90.00 P 21 21 21    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      0.026535  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014967  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006975        0.00000                         
MTRIX1   1 -1.000000  0.005000 -0.007000       57.10159    1                    
MTRIX2   1 -0.005000 -0.998000  0.065000      -37.85538    1                    
MTRIX3   1 -0.007000  0.065000  0.998000        1.41790    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system