HEADER TRANSFERASE, HYDROLASE 05-SEP-05 2AXN
TITLE CRYSTAL STRUCTURE OF THE HUMAN INDUCIBLE FORM 6-PHOSPHOFRUCTO-2-
TITLE 2 KINASE/FRUCTOSE-2,6-BISPHOSPHATASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BIPHOSPHATASE 3 (6PF-
COMPND 3 2-K/FRU- 2,6-P2ASE BRAIN/PLACENTA-TYPE ISOZYME) (IPFK-2) [INCLUDES:
COMPND 4 6- PHOSPHOFRUCTO-2-KINASE (EC 2.7.1.105); FRUCTOSE-2,6-BISPHOSPHATASE
COMPND 5 (EC 3.1.3.46)];
COMPND 6 CHAIN: A;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PFKFB3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIFUNCTIONAL ENZYME, EDTA COMPLEX, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.KIM,N.P.MANES,M.R.EL-MAGHRABI,Y.H.LEE
REVDAT 6 23-AUG-23 2AXN 1 HETSYN
REVDAT 5 29-JUL-20 2AXN 1 COMPND REMARK HETNAM SITE
REVDAT 4 09-JUN-09 2AXN 1 REVDAT
REVDAT 3 24-FEB-09 2AXN 1 VERSN
REVDAT 2 20-JAN-09 2AXN 1 JRNL
REVDAT 1 06-DEC-05 2AXN 0
JRNL AUTH S.G.KIM,N.P.MANES,M.R.EL-MAGHRABI,Y.H.LEE
JRNL TITL CRYSTAL STRUCTURE OF THE HYPOXIA-INDUCIBLE FORM OF
JRNL TITL 2 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE
JRNL TITL 3 (PFKFB3): A POSSIBLE NEW TARGET FOR CANCER THERAPY.
JRNL REF J.BIOL.CHEM. V. 281 2939 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16316985
JRNL DOI 10.1074/JBC.M511019200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 44651
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4459
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3669
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CAMD
REMARK 200 BEAMLINE : GCPCC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.3808
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SILICON CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44651
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.68600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB 1K6M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ETHYLENE GLYCOL, TRIS,
REMARK 280 PHOSHATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 173.22667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 86.61333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 129.92000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 43.30667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 216.53333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 173.22667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 86.61333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 43.30667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 129.92000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 216.53333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 991 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 PRO A 1
REMARK 465 LYS A 29
REMARK 465 LEU A 30
REMARK 465 THR A 31
REMARK 465 GLU A 446
REMARK 465 ASP A 447
REMARK 465 ALA A 448
REMARK 465 LYS A 449
REMARK 465 LYS A 450
REMARK 465 GLY A 451
REMARK 465 PRO A 452
REMARK 465 VAL A 677
REMARK 465 THR A 678
REMARK 465 PRO A 679
REMARK 465 LEU A 680
REMARK 465 ALA A 681
REMARK 465 SER A 682
REMARK 465 PRO A 683
REMARK 465 GLU A 684
REMARK 465 PRO A 685
REMARK 465 THR A 686
REMARK 465 LYS A 687
REMARK 465 LYS A 688
REMARK 465 PRO A 689
REMARK 465 ARG A 690
REMARK 465 ILE A 691
REMARK 465 ASN A 692
REMARK 465 SER A 693
REMARK 465 PHE A 694
REMARK 465 GLU A 695
REMARK 465 GLU A 696
REMARK 465 HIS A 697
REMARK 465 VAL A 698
REMARK 465 ALA A 699
REMARK 465 SER A 700
REMARK 465 THR A 701
REMARK 465 SER A 702
REMARK 465 ALA A 703
REMARK 465 ALA A 704
REMARK 465 LEU A 705
REMARK 465 PRO A 706
REMARK 465 SER A 707
REMARK 465 CYS A 708
REMARK 465 LEU A 709
REMARK 465 PRO A 710
REMARK 465 PRO A 711
REMARK 465 GLU A 712
REMARK 465 VAL A 713
REMARK 465 PRO A 714
REMARK 465 THR A 715
REMARK 465 GLN A 716
REMARK 465 LEU A 717
REMARK 465 PRO A 718
REMARK 465 GLY A 719
REMARK 465 GLN A 720
REMARK 465 ASN A 721
REMARK 465 MET A 722
REMARK 465 LYS A 723
REMARK 465 GLY A 724
REMARK 465 SER A 725
REMARK 465 ARG A 726
REMARK 465 SER A 727
REMARK 465 SER A 728
REMARK 465 ALA A 729
REMARK 465 ASP A 730
REMARK 465 ARG A 733
REMARK 465 LYS A 734
REMARK 465 HIS A 735
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 SER A 25 -72.59 -107.29
REMARK 500 CYS A 26 173.40 100.71
REMARK 500 SER A 33 126.57 -26.92
REMARK 500 LYS A 79 -60.43 69.32
REMARK 500 ASN A 127 46.27 38.36
REMARK 500 LYS A 204 -99.91 -151.30
REMARK 500 ARG A 225 67.17 34.40
REMARK 500 GLU A 330 -11.40 79.26
REMARK 500 ASP A 350 65.03 -152.17
REMARK 500 GLU A 380 -110.19 -111.73
REMARK 500 CYS A 386 -134.76 -133.06
REMARK 500 ALA A 423 -112.82 55.56
REMARK 500 PRO A 454 -63.03 -29.19
REMARK 500 MET A 456 31.11 -98.18
REMARK 500 ASN A 459 94.15 31.35
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2AXN A 0 735 UNP Q16875 F263_HUMAN 1 520
SEQRES 1 A 520 MET PRO LEU GLU LEU THR GLN SER ARG VAL GLN LYS ILE
SEQRES 2 A 520 TRP VAL PRO VAL ASP HIS ARG PRO SER LEU PRO ARG SER
SEQRES 3 A 520 CYS GLY PRO LYS LEU THR ASN SER PRO THR VAL ILE VAL
SEQRES 4 A 520 MET VAL GLY LEU PRO ALA ARG GLY LYS THR TYR ILE SER
SEQRES 5 A 520 LYS LYS LEU THR ARG TYR LEU ASN TRP ILE GLY VAL PRO
SEQRES 6 A 520 THR LYS VAL PHE ASN VAL GLY GLU TYR ARG ARG GLU ALA
SEQRES 7 A 520 VAL LYS GLN TYR SER SER TYR ASN PHE PHE ARG PRO ASP
SEQRES 8 A 520 ASN GLU GLU ALA MET LYS VAL ARG LYS GLN CYS ALA LEU
SEQRES 9 A 520 ALA ALA LEU ARG ASP VAL LYS SER TYR LEU ALA LYS GLU
SEQRES 10 A 520 GLY GLY GLN ILE ALA VAL PHE ASP ALA THR ASN THR THR
SEQRES 11 A 520 ARG GLU ARG ARG HIS MET ILE LEU HIS PHE ALA LYS GLU
SEQRES 12 A 520 ASN ASP PHE LYS ALA PHE PHE ILE GLU SER VAL CYS ASP
SEQRES 13 A 520 ASP PRO THR VAL VAL ALA SER ASN ILE MET GLU VAL LYS
SEQRES 14 A 520 ILE SER SER PRO ASP TYR LYS ASP CYS ASN SER ALA GLU
SEQRES 15 A 520 ALA MET ASP ASP PHE MET LYS ARG ILE SER CYS TYR GLU
SEQRES 16 A 520 ALA SER TYR GLN PRO LEU ASP PRO ASP LYS CYS ASP ARG
SEQRES 17 A 520 ASP LEU SER LEU ILE LYS VAL ILE ASP VAL GLY ARG ARG
SEQRES 18 A 520 PHE LEU VAL ASN ARG VAL GLN ASP HIS ILE GLN SER ARG
SEQRES 19 A 520 ILE VAL TYR TYR LEU MET ASN ILE HIS VAL GLN PRO ARG
SEQRES 20 A 520 THR ILE TYR LEU CYS ARG HIS GLY GLU ASN GLU HIS ASN
SEQRES 21 A 520 LEU GLN GLY ARG ILE GLY GLY ASP SER GLY LEU SER SER
SEQRES 22 A 520 ARG GLY LYS LYS PHE ALA SER ALA LEU SER LYS PHE VAL
SEQRES 23 A 520 GLU GLU GLN ASN LEU LYS ASP LEU ARG VAL TRP THR SER
SEQRES 24 A 520 GLN LEU LYS SER THR ILE GLN THR ALA GLU ALA LEU ARG
SEQRES 25 A 520 LEU PRO TYR GLU GLN TRP LYS ALA LEU ASN GLU ILE ASP
SEQRES 26 A 520 ALA GLY VAL CYS GLU GLU LEU THR TYR GLU GLU ILE ARG
SEQRES 27 A 520 ASP THR TYR PRO GLU GLU TYR ALA LEU ARG GLU GLN ASP
SEQRES 28 A 520 LYS TYR TYR TYR ARG TYR PRO THR GLY GLU SER TYR GLN
SEQRES 29 A 520 ASP LEU VAL GLN ARG LEU GLU PRO VAL ILE MET GLU LEU
SEQRES 30 A 520 GLU ARG GLN GLU ASN VAL LEU VAL ILE CYS HIS GLN ALA
SEQRES 31 A 520 VAL LEU ARG CYS LEU LEU ALA TYR PHE LEU ASP LYS SER
SEQRES 32 A 520 ALA GLU GLU MET PRO TYR LEU LYS CYS PRO LEU HIS THR
SEQRES 33 A 520 VAL LEU LYS LEU THR PRO VAL ALA TYR GLY CYS ARG VAL
SEQRES 34 A 520 GLU SER ILE TYR LEU ASN VAL GLU SER VAL CYS THR HIS
SEQRES 35 A 520 ARG GLU ARG SER GLU ASP ALA LYS LYS GLY PRO ASN PRO
SEQRES 36 A 520 LEU MET ARG ARG ASN SER VAL THR PRO LEU ALA SER PRO
SEQRES 37 A 520 GLU PRO THR LYS LYS PRO ARG ILE ASN SER PHE GLU GLU
SEQRES 38 A 520 HIS VAL ALA SER THR SER ALA ALA LEU PRO SER CYS LEU
SEQRES 39 A 520 PRO PRO GLU VAL PRO THR GLN LEU PRO GLY GLN ASN MET
SEQRES 40 A 520 LYS GLY SER ARG SER SER ALA ASP SER SER ARG LYS HIS
HET F6P A 736 16
HET EDT A 737 20
HET ADP A 738 27
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-
HETNAM 2 EDT AMINO}-ACETIC ACID
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN F6P FRUCTOSE-6-PHOSPHATE; 6-O-PHOSPHONO-BETA-D-FRUCTOSE; 6-
HETSYN 2 F6P O-PHOSPHONO-D-FRUCTOSE; 6-O-PHOSPHONO-FRUCTOSE
FORMUL 2 F6P C6 H13 O9 P
FORMUL 3 EDT C10 H16 N2 O8
FORMUL 4 ADP C10 H15 N5 O10 P2
FORMUL 5 HOH *353(H2 O)
HELIX 1 1 GLY A 46 ILE A 61 1 16
HELIX 2 2 VAL A 70 LYS A 79 1 10
HELIX 3 3 SER A 83 ARG A 88 5 6
HELIX 4 4 ASN A 91 GLU A 116 1 26
HELIX 5 5 THR A 129 ASN A 143 1 15
HELIX 6 6 ASP A 156 LYS A 168 1 13
HELIX 7 7 SER A 171 LYS A 175 5 5
HELIX 8 8 ASN A 178 ALA A 195 1 18
HELIX 9 9 ASP A 228 MET A 239 1 12
HELIX 10 10 ASN A 256 GLY A 262 1 7
HELIX 11 11 SER A 271 ASN A 289 1 19
HELIX 12 12 LEU A 300 ALA A 309 1 10
HELIX 13 13 LYS A 318 ASN A 321 5 4
HELIX 14 14 ALA A 325 GLU A 329 5 5
HELIX 15 15 THR A 332 TYR A 340 1 9
HELIX 16 16 TYR A 340 ASP A 350 1 11
HELIX 17 17 SER A 361 GLN A 379 1 19
HELIX 18 18 HIS A 387 LEU A 399 1 13
HELIX 19 19 GLU A 405 LEU A 409 5 5
HELIX 20 20 ASN A 453 ARG A 457 5 5
SHEET 1 A 2 LEU A 4 GLN A 6 0
SHEET 2 A 2 TRP A 13 PRO A 15 -1 O VAL A 14 N THR A 5
SHEET 1 B 6 THR A 65 ASN A 69 0
SHEET 2 B 6 ILE A 120 ASP A 124 1 O VAL A 122 N PHE A 68
SHEET 3 B 6 THR A 35 VAL A 40 1 N ILE A 37 O ALA A 121
SHEET 4 B 6 LYS A 146 VAL A 153 1 O LYS A 146 N VAL A 36
SHEET 5 B 6 SER A 210 ILE A 215 1 O VAL A 214 N GLU A 151
SHEET 6 B 6 ARG A 220 ASN A 224 -1 O ASN A 224 N LEU A 211
SHEET 1 C 6 TYR A 314 GLN A 316 0
SHEET 2 C 6 ARG A 294 THR A 297 1 N THR A 297 O GLU A 315
SHEET 3 C 6 VAL A 382 CYS A 386 1 O ILE A 385 N TRP A 296
SHEET 4 C 6 ILE A 248 ARG A 252 1 N CYS A 251 O CYS A 386
SHEET 5 C 6 THR A 415 VAL A 422 -1 O LEU A 419 N ILE A 248
SHEET 6 C 6 GLY A 425 TYR A 432 -1 O GLU A 429 N LYS A 418
CISPEP 1 GLY A 27 PRO A 28 0 0.78
CRYST1 102.580 102.580 259.840 90.00 90.00 120.00 P 65 2 2 12
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 0.009748 0.005628 0.000000 0.00000
SCALE2 0.000000 0.011257 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END