HEADER TRANSFERASE 27-FEB-15 5AJW
TITLE HUMAN PFKFB3 IN COMPLEX WITH AN INDOLE INHIBITOR 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 6PF-2-K/FRU-2,6-P2ASE 3,PFK/FBPASE 3,6PF-2-K/FRU-2,6-P2AS E
COMPND 5 BRAIN/PLACENTA-TYPE ISOZYME, RENAL CARCINOMA ANTIGEN NY-REN-56, IPFK-
COMPND 6 2, HUMAN PFKFB3;
COMPND 7 EC: 2.7.1.105, 2.7.1.105, 3.1.3.46;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BOYD,J.L.BROOKFIELD,S.E.CRITCHLOW,I.A.CUMMING,N.J.CURTIS,
AUTHOR 2 J.E.DEBRECZENI,S.L.DEGORCE,C.DONALD,N.J.EVANS,S.GROOMBRIDGE,
AUTHOR 3 P.HOPCROFT,N.P.JONES,J.G.KETTLE,S.LAMONT,H.J.LEWIS,P.MACFAULL,
AUTHOR 4 S.B.MCLOUGHLIN,L.J.M.RIGOREAU,J.M.SMITH,S.ST-GALLAY,J.K.STOCK,
AUTHOR 5 E.R.WHEATLEY,J.WINTER,J.WINGFIELD
REVDAT 3 29-JUL-20 5AJW 1 COMPND REMARK HETNAM SITE
REVDAT 2 13-MAY-15 5AJW 1 JRNL
REVDAT 1 22-APR-15 5AJW 0
JRNL AUTH S.BOYD,J.L.BROOKFIELD,S.E.CRITCHLOW,I.A.CUMMING,N.J.CURTIS,
JRNL AUTH 2 J.DEBRECZENI,S.L.DEGORCE,C.DONALD,N.J.EVANS,S.GROOMBRIDGE,
JRNL AUTH 3 P.HOPCROFT,N.P.JONES,J.G.KETTLE,S.LAMONT,H.J.LEWIS,
JRNL AUTH 4 P.MACFAULL,S.B.MCLOUGHLIN,L.J.M.RIGOREAU,J.M.SMITH,
JRNL AUTH 5 S.ST-GALLAY,J.K.STOCK,A.P.TURNBULL,E.R.WHEATLEY,J.WINTER,
JRNL AUTH 6 J.WINGFIELD
JRNL TITL STRUCTURE-BASED DESIGN OF POTENT AND SELECTIVE INHIBITORS OF
JRNL TITL 2 THE METABOLIC KINASE PFKFB3.
JRNL REF J.MED.CHEM. V. 58 3611 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 25849762
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00352
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 28821
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1496
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 : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2928
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2139
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2780
REMARK 3 BIN R VALUE (WORKING SET) : 0.2119
REMARK 3 BIN FREE R VALUE : 0.2549
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.05
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
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 : 3501
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 179
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.51200
REMARK 3 B22 (A**2) : -1.51200
REMARK 3 B33 (A**2) : 3.02400
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.358
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.278
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.206
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.259
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.201
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3663 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4978 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1280 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 90 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 562 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3663 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 470 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4258 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.94
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.42
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5485 -28.1683 -9.1075
REMARK 3 T TENSOR
REMARK 3 T11: 0.0298 T22: -0.2210
REMARK 3 T33: -0.1608 T12: -0.0136
REMARK 3 T13: 0.0295 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.9606 L22: 1.1625
REMARK 3 L33: 1.2986 L12: 0.0622
REMARK 3 L13: -0.1817 L23: -0.0197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: -0.0314 S13: -0.0964
REMARK 3 S21: 0.3946 S22: -0.1311 S23: 0.0681
REMARK 3 S31: 0.3290 S32: -0.0313 S33: 0.1130
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AJW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1290063152.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PIXEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28866
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 51.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.07000
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM MALONATE, 18W/V% PEG3350
REMARK 280 AND 0.1 M PCTP BUFFER PH 7.0
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 173.54000
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 86.77000
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 130.15500
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 43.38500
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 216.92500
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 173.54000
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 86.77000
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 43.38500
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 130.15500
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 216.92500
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.8 KCAL/MOL
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 350 BIOMT1 2 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -43.38500
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 A2076 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 CYS A 26
REMARK 465 GLY A 27
REMARK 465 PRO A 28
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 ASN A 453
REMARK 465 PRO A 454
REMARK 465 LEU A 455
REMARK 465 MET A 456
REMARK 465 ARG A 457
REMARK 465 ARG A 458
REMARK 465 ASN A 459
REMARK 465 SER A 460
REMARK 465 VAL A 461
REMARK 465 THR A 462
REMARK 465 PRO A 463
REMARK 465 LEU A 464
REMARK 465 ALA A 465
REMARK 465 SER A 466
REMARK 465 PRO A 467
REMARK 465 GLU A 468
REMARK 465 PRO A 469
REMARK 465 THR A 470
REMARK 465 LYS A 471
REMARK 465 LYS A 472
REMARK 465 PRO A 473
REMARK 465 ARG A 474
REMARK 465 ILE A 475
REMARK 465 ASN A 476
REMARK 465 SER A 477
REMARK 465 PHE A 478
REMARK 465 GLU A 479
REMARK 465 GLU A 480
REMARK 465 HIS A 481
REMARK 465 VAL A 482
REMARK 465 ALA A 483
REMARK 465 SER A 484
REMARK 465 THR A 485
REMARK 465 SER A 486
REMARK 465 ALA A 487
REMARK 465 ALA A 488
REMARK 465 LEU A 489
REMARK 465 PRO A 490
REMARK 465 SER A 491
REMARK 465 CYS A 492
REMARK 465 LEU A 493
REMARK 465 PRO A 494
REMARK 465 PRO A 495
REMARK 465 GLU A 496
REMARK 465 VAL A 497
REMARK 465 PRO A 498
REMARK 465 THR A 499
REMARK 465 GLN A 500
REMARK 465 LEU A 501
REMARK 465 PRO A 502
REMARK 465 GLY A 503
REMARK 465 GLN A 504
REMARK 465 ASN A 505
REMARK 465 MET A 506
REMARK 465 LYS A 507
REMARK 465 GLY A 508
REMARK 465 SER A 509
REMARK 465 ARG A 510
REMARK 465 SER A 511
REMARK 465 SER A 512
REMARK 465 ALA A 513
REMARK 465 ASP A 514
REMARK 465 SER A 515
REMARK 465 SER A 516
REMARK 465 ARG A 517
REMARK 465 LYS A 518
REMARK 465 HIS A 519
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 ARG A 24 CD NE CZ NH1 NH2
REMARK 470 LYS A 79 CG CD CE NZ
REMARK 470 GLN A 80 CG CD OE1 NE2
REMARK 470 LYS A 96 CD CE NZ
REMARK 470 GLN A 119 CG CD OE1 NE2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 GLU A 166 CG CD OE1 OE2
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 LYS A 188 CG CD CE NZ
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 ARG A 207 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 219 CD NE CZ NH1 NH2
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 LYS A 283 CG CD CE NZ
REMARK 470 LYS A 291 CG CD CE NZ
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 GLU A 404 CG CD OE1 OE2
REMARK 470 LYS A 410 CG CD CE NZ
REMARK 470 GLU A 443 CG CD OE1 OE2
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 33 130.08 -38.62
REMARK 500 LYS A 79 -74.08 -40.99
REMARK 500 LYS A 204 -71.41 -120.17
REMARK 500 GLU A 380 -103.16 -110.11
REMARK 500 CYS A 386 -139.86 -135.08
REMARK 500 ALA A 423 71.40 39.26
REMARK 500 TYR A 424 -45.24 81.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AJV RELATED DB: PDB
REMARK 900 HUMAN PFKFB3 IN COMPLEX WITH AN INDOLE INHIBITOR 1
REMARK 900 RELATED ID: 5AJX RELATED DB: PDB
REMARK 900 HUMAN PFKFB3 IN COMPLEX WITH AN INDOLE INHIBITOR 3
REMARK 900 RELATED ID: 5AJY RELATED DB: PDB
REMARK 900 HUMAN PFKFB3 IN COMPLEX WITH AN INDOLE INHIBITOR 4
REMARK 900 RELATED ID: 5AJZ RELATED DB: PDB
REMARK 900 HUMAN PFKFB3 IN COMPLEX WITH AN INDOLE INHIBITOR 5
REMARK 900 RELATED ID: 5AK0 RELATED DB: PDB
REMARK 900 HUMAN PFKFB3 IN COMPLEX WITH AN INDOLE INHIBITOR 6
DBREF 5AJW A 0 519 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 PHS A1446 4
HET PO4 A1447 5
HET F6P A1448 16
HET S6L A1449 31
HETNAM PHS PHOSPHONIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM S6L 2-AMINO-N-[4-(2-AMINO-1-BENZYL-3-CYANO-INDOL-5-YL)
HETNAM 2 S6L OXYPHENYL]ACETAMIDE
FORMUL 2 PHS H3 O3 P
FORMUL 3 PO4 O4 P 3-
FORMUL 4 F6P C6 H13 O9 P
FORMUL 5 S6L C24 H21 N5 O2
FORMUL 6 HOH *179(H2 O)
HELIX 1 1 GLY A 46 ILE A 61 1 16
HELIX 2 2 VAL A 70 VAL A 78 1 9
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 ILE A 241 1 14
HELIX 10 10 ASN A 256 GLY A 262 1 7
HELIX 11 11 SER A 271 GLN A 288 1 18
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
SHEET 1 AA 2 LEU A 4 GLN A 6 0
SHEET 2 AA 2 TRP A 13 PRO A 15 -1 O VAL A 14 N THR A 5
SHEET 1 AB 6 THR A 65 ASN A 69 0
SHEET 2 AB 6 ILE A 120 ASP A 124 1 O ILE A 120 N LYS A 66
SHEET 3 AB 6 THR A 35 VAL A 40 1 O THR A 35 N ALA A 121
SHEET 4 AB 6 LYS A 146 VAL A 153 1 O LYS A 146 N VAL A 36
SHEET 5 AB 6 LEU A 211 ILE A 215 1 O ILE A 212 N GLU A 151
SHEET 6 AB 6 ARG A 220 ASN A 224 -1 O ARG A 220 N ILE A 215
SHEET 1 AC 6 GLU A 315 GLN A 316 0
SHEET 2 AC 6 ARG A 294 THR A 297 1 O VAL A 295 N GLU A 315
SHEET 3 AC 6 VAL A 382 CYS A 386 1 O LEU A 383 N TRP A 296
SHEET 4 AC 6 ILE A 248 ARG A 252 1 O TYR A 249 N VAL A 384
SHEET 5 AC 6 THR A 415 VAL A 422 -1 O LEU A 417 N LEU A 250
SHEET 6 AC 6 GLY A 425 TYR A 432 -1 O GLY A 425 N VAL A 422
CRYST1 102.530 102.530 260.310 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 0.009753 0.005631 0.000000 0.00000
SCALE2 0.000000 0.011262 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003842 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
