HEADER TRANSFERASE/TRANSFERASE INHIBITOR 26-NOV-14 4X2F
TITLE SELECTION OF FRAGMENTS FOR KINASE INHIBITOR DESIGN: DECORATION IS KEY
CAVEAT 4X2F C-N BOND DISTANCE OF RESIDUES A LYS 213 AND A GLY 214 IS
CAVEAT 2 4X2F OUTSIDE OF THE NORMAL RANGE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TGF-BETA RECEPTOR TYPE-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 200-503;
COMPND 5 SYNONYM: TGFR-1,ACTIVIN A RECEPTOR TYPE II-LIKE PROTEIN KINASE OF
COMPND 6 53KD,ACTIVIN RECEPTOR-LIKE KINASE 5,ALK5,SERINE/THREONINE-PROTEIN
COMPND 7 KINASE RECEPTOR R4,SKR4,TGF-BETA TYPE I RECEPTOR,TRANSFORMING GROWTH
COMPND 8 FACTOR-BETA RECEPTOR TYPE I,TBETAR-I;
COMPND 9 EC: 2.7.11.30;
COMPND 10 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: TGFBR1, ALK5, SKR4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS TRANSFERASE, PROTEIN KINASE, INHIBITOR COMPLEX, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CZODROWSKI,G.HOELZEMANN,G.BARNICKEL,H.GREINER,D.MUSIL
REVDAT 2 28-FEB-24 4X2F 1 REMARK
REVDAT 1 28-OCT-15 4X2F 0
JRNL AUTH P.CZODROWSKI,G.HOLZEMANN,G.BARNICKEL,H.GREINER,D.MUSIL
JRNL TITL SELECTION OF FRAGMENTS FOR KINASE INHIBITOR DESIGN:
JRNL TITL 2 DECORATION IS KEY.
JRNL REF J.MED.CHEM. V. 58 457 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 25437144
JRNL DOI 10.1021/JM501597J
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.11.5
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 48011
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2401
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.53
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.92
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2608
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2130
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2478
REMARK 3 BIN R VALUE (WORKING SET) : 0.2132
REMARK 3 BIN FREE R VALUE : 0.2107
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.98
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 130
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 : 2429
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 263
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.32760
REMARK 3 B22 (A**2) : -2.19980
REMARK 3 B33 (A**2) : 0.87220
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) : 0.158
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.070
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.071
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.067
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.069
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 : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2558 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3467 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 918 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 61 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 380 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2558 ; 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 : 328 ; 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 : 3292 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.93
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 13.85
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0042 76.3805 12.1617
REMARK 3 T TENSOR
REMARK 3 T11: -0.0297 T22: -0.0156
REMARK 3 T33: -0.0258 T12: -0.0021
REMARK 3 T13: -0.0007 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.2703 L22: 0.4500
REMARK 3 L33: 0.6388 L12: 0.1596
REMARK 3 L13: 0.1539 L23: 0.3820
REMARK 3 S TENSOR
REMARK 3 S11: -0.0259 S12: -0.0084 S13: 0.0448
REMARK 3 S21: -0.0431 S22: 0.0021 S23: 0.0329
REMARK 3 S31: -0.0826 S32: 0.0077 S33: 0.0238
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4X2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000204952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-07
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48030
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 17.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 240 MM LI2SO4, 24% PEG
REMARK 280 4000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 21.12500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.92500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.76500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.92500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.12500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.76500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 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 LYS A 502
REMARK 465 MET A 503
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 LYS A 213 C GLY A 214 N -0.183
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 263 -61.09 -101.27
REMARK 500 GLN A 324 49.97 -103.20
REMARK 500 ARG A 332 -5.05 76.58
REMARK 500 ASP A 333 43.53 -149.31
REMARK 500 ALA A 350 -169.63 -129.57
REMARK 500 ALA A 368 67.34 39.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 424 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3WJ A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X2G RELATED DB: PDB
DBREF 4X2F A 200 503 UNP P36897 TGFR1_HUMAN 200 503
SEQADV 4X2F GLY A 199 UNP P36897 EXPRESSION TAG
SEQRES 1 A 305 GLY THR ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE
SEQRES 2 A 305 GLY LYS GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP
SEQRES 3 A 305 ARG GLY GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG
SEQRES 4 A 305 GLU GLU ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN
SEQRES 5 A 305 THR VAL MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE
SEQRES 6 A 305 ALA ALA ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU
SEQRES 7 A 305 TRP LEU VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE
SEQRES 8 A 305 ASP TYR LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET
SEQRES 9 A 305 ILE LYS LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS
SEQRES 10 A 305 LEU HIS MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA
SEQRES 11 A 305 ILE ALA HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL
SEQRES 12 A 305 LYS LYS ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU
SEQRES 13 A 305 ALA VAL ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE
SEQRES 14 A 305 ALA PRO ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA
SEQRES 15 A 305 PRO GLU VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE
SEQRES 16 A 305 GLU SER PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU
SEQRES 17 A 305 VAL PHE TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY
SEQRES 18 A 305 ILE HIS GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL
SEQRES 19 A 305 PRO SER ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL
SEQRES 20 A 305 CYS GLU GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP
SEQRES 21 A 305 GLN SER CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET
SEQRES 22 A 305 ARG GLU CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR
SEQRES 23 A 305 ALA LEU ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN
SEQRES 24 A 305 GLN GLU GLY ILE LYS MET
HET 3WJ A 601 19
HET SO4 A 602 5
HETNAM 3WJ 4-AMINO-8-(4-AMINOPHENYL)PYRIDO[2,3-D]PYRIMIDIN-5(8H)-
HETNAM 2 3WJ ONE
HETNAM SO4 SULFATE ION
FORMUL 2 3WJ C13 H11 N5 O
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *263(H2 O)
HELIX 1 AA1 ILE A 201 ARG A 203 5 3
HELIX 2 AA2 GLU A 238 GLN A 250 1 13
HELIX 3 AA3 SER A 287 TYR A 295 1 9
HELIX 4 AA4 THR A 298 MET A 318 1 21
HELIX 5 AA5 LYS A 335 LYS A 337 5 3
HELIX 6 AA6 ASP A 351 ALA A 355 5 5
HELIX 7 AA7 THR A 375 MET A 379 5 5
HELIX 8 AA8 ALA A 380 ASP A 385 1 6
HELIX 9 AA9 HIS A 392 ARG A 414 1 23
HELIX 10 AB1 SER A 437 CYS A 446 1 10
HELIX 11 AB2 PRO A 455 SER A 460 5 6
HELIX 12 AB3 CYS A 461 TRP A 475 1 15
HELIX 13 AB4 ASN A 478 ARG A 482 5 5
HELIX 14 AB5 THR A 484 GLY A 500 1 17
SHEET 1 AA1 5 ILE A 205 LYS A 213 0
SHEET 2 AA1 5 GLU A 218 TRP A 224 -1 O ARG A 221 N GLN A 208
SHEET 3 AA1 5 GLU A 227 SER A 235 -1 O ILE A 233 N GLU A 218
SHEET 4 AA1 5 THR A 274 ASP A 281 -1 O LEU A 278 N LYS A 232
SHEET 5 AA1 5 PHE A 262 ASP A 269 -1 N ALA A 264 O VAL A 279
SHEET 1 AA2 3 ILE A 329 ALA A 330 0
SHEET 2 AA2 3 VAL A 356 ASP A 359 -1 O VAL A 356 N ALA A 330
SHEET 3 AA2 3 THR A 364 ILE A 365 -1 O THR A 364 N ASP A 359
SHEET 1 AA3 2 ILE A 339 VAL A 341 0
SHEET 2 AA3 2 CYS A 347 ILE A 349 -1 O CYS A 348 N LEU A 340
SITE 1 AC1 12 ILE A 211 ALA A 230 LEU A 260 SER A 280
SITE 2 AC1 12 ASP A 281 TYR A 282 HIS A 283 SER A 287
SITE 3 AC1 12 ASP A 290 LEU A 340 HOH A 815 HOH A 861
SITE 1 AC2 8 LYS A 337 ARG A 377 ASP A 435 HOH A 752
SITE 2 AC2 8 HOH A 806 HOH A 817 HOH A 877 HOH A 904
CRYST1 42.250 77.530 89.850 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023669 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011130 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
