HEADER TRANSFERASE 30-NOV-14 4X3J
TITLE SELECTION OF FRAGMENTS FOR KINASE INHIBITOR DESIGN: DECORATION IS KEY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOPOIETIN-1 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 802-1122;
COMPND 5 SYNONYM: ENDOTHELIAL TYROSINE KINASE,TUNICA INTERNA ENDOTHELIAL CELL
COMPND 6 KINASE,TYROSINE KINASE WITH IG AND EGF HOMOLOGY DOMAINS-2,TYROSINE-
COMPND 7 PROTEIN KINASE RECEPTOR TEK,TYROSINE-PROTEIN KINASE RECEPTOR TIE-2,
COMPND 8 HTIE2,P140 TEK;
COMPND 9 EC: 2.7.10.1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TEK, TIE2, VMCM, VMCM1;
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
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CZODROWSKI,G.HOELZEMANN,G.BARNICKEL,H.GREINER,D.MUSIL
REVDAT 2 21-JAN-15 4X3J 1 JRNL
REVDAT 1 24-DEC-14 4X3J 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. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
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) : 35.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 12878
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) : 0.257
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 629
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2961
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2600
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2814
REMARK 3 BIN R VALUE (WORKING SET) : 0.2572
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.96
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 147
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 : 1886
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.22220
REMARK 3 B22 (A**2) : -6.22220
REMARK 3 B33 (A**2) : 12.44440
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) : 0.490
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.405
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.285
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.390
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.284
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 : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1962 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2662 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 668 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 47 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 281 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1962 ; 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 : 246 ; 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 : 2293 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.12
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.81
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.80
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): 25.7044 16.0967 56.5154
REMARK 3 T TENSOR
REMARK 3 T11: -0.2647 T22: 0.0918
REMARK 3 T33: -0.3026 T12: 0.0012
REMARK 3 T13: 0.0090 T23: 0.0823
REMARK 3 L TENSOR
REMARK 3 L11: 1.5547 L22: 1.5491
REMARK 3 L33: 4.5186 L12: -0.1783
REMARK 3 L13: -0.7486 L23: -0.3666
REMARK 3 S TENSOR
REMARK 3 S11: -0.1157 S12: 0.0315 S13: 0.0560
REMARK 3 S21: -0.1288 S22: 0.2445 S23: -0.0201
REMARK 3 S31: 0.0944 S32: -0.3135 S33: -0.1288
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4X3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12936
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 36.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
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: NULL
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 (%): 47.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS/HCL PH 7.0 0.05 M NACL 0.03
REMARK 280 M LITHIUMSULFAT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.22500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.22800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.22800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.61250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.22800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.22800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 133.83750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.22800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.22800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.61250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.22800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.22800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 133.83750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 89.22500
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 ALA A 802
REMARK 465 LEU A 803
REMARK 465 ASN A 804
REMARK 465 ARG A 805
REMARK 465 LYS A 806
REMARK 465 VAL A 807
REMARK 465 LYS A 808
REMARK 465 ASN A 809
REMARK 465 ASN A 810
REMARK 465 PRO A 811
REMARK 465 ASP A 812
REMARK 465 PRO A 813
REMARK 465 THR A 814
REMARK 465 ILE A 815
REMARK 465 TYR A 816
REMARK 465 PRO A 817
REMARK 465 VAL A 818
REMARK 465 LEU A 819
REMARK 465 ASP A 820
REMARK 465 TRP A 821
REMARK 465 ASN A 822
REMARK 465 ASP A 823
REMARK 465 ILE A 824
REMARK 465 LYS A 825
REMARK 465 PHE A 826
REMARK 465 GLN A 827
REMARK 465 ASP A 828
REMARK 465 VAL A 829
REMARK 465 ILE A 830
REMARK 465 GLY A 831
REMARK 465 GLU A 832
REMARK 465 GLY A 833
REMARK 465 ASN A 834
REMARK 465 PHE A 835
REMARK 465 GLY A 836
REMARK 465 GLN A 837
REMARK 465 ILE A 843
REMARK 465 LYS A 844
REMARK 465 LYS A 845
REMARK 465 ASP A 846
REMARK 465 GLY A 847
REMARK 465 LEU A 848
REMARK 465 ARG A 849
REMARK 465 ARG A 856
REMARK 465 MET A 857
REMARK 465 LYS A 858
REMARK 465 GLU A 859
REMARK 465 TYR A 860
REMARK 465 ALA A 861
REMARK 465 SER A 862
REMARK 465 LYS A 863
REMARK 465 ASP A 864
REMARK 465 ASP A 865
REMARK 465 HIS A 866
REMARK 465 ARG A 867
REMARK 465 ASP A 868
REMARK 465 PHE A 869
REMARK 465 ALA A 870
REMARK 465 GLY A 871
REMARK 465 GLY A 890
REMARK 465 ALA A 891
REMARK 465 CYS A 892
REMARK 465 GLU A 893
REMARK 465 HIS A 894
REMARK 465 ARG A 895
REMARK 465 GLY A 896
REMARK 465 TYR A 897
REMARK 465 LEU A 985
REMARK 465 SER A 986
REMARK 465 ARG A 987
REMARK 465 GLY A 988
REMARK 465 GLN A 989
REMARK 465 GLU A 990
REMARK 465 VAL A 991
REMARK 465 TYR A 992
REMARK 465 VAL A 993
REMARK 465 LYS A 994
REMARK 465 LYS A 995
REMARK 465 THR A 996
REMARK 465 MET A 997
REMARK 465 GLY A 998
REMARK 465 ARG A 999
REMARK 465 CYS A 1118
REMARK 465 SER A 1119
REMARK 465 ALA A 1120
REMARK 465 GLU A 1121
REMARK 465 GLU A 1122
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; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A 839 CG CD1 CD2
REMARK 480 MET A 850 CG SD CE
REMARK 480 LYS A 878 CG CD CE NZ
REMARK 480 TYR A 899 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 LYS A 1050 CG CD CE NZ
REMARK 480 GLU A 1109 CG CD OE1 OE2
REMARK 480 LYS A 1110 CG CD CE NZ
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 ALA A 841 -169.35 -124.96
REMARK 500 HIS A 881 40.63 -95.48
REMARK 500 ARG A 963 -7.98 75.00
REMARK 500 ASN A 964 39.95 -140.16
REMARK 500 LYS A1110 27.59 -78.68
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 3WR A 1201
DBREF 4X3J A 802 1122 UNP Q02763 TIE2_HUMAN 802 1122
SEQADV 4X3J ASN A 964 UNP Q02763 ASP 964 ENGINEERED MUTATION
SEQRES 1 A 321 ALA LEU ASN ARG LYS VAL LYS ASN ASN PRO ASP PRO THR
SEQRES 2 A 321 ILE TYR PRO VAL LEU ASP TRP ASN ASP ILE LYS PHE GLN
SEQRES 3 A 321 ASP VAL ILE GLY GLU GLY ASN PHE GLY GLN VAL LEU LYS
SEQRES 4 A 321 ALA ARG ILE LYS LYS ASP GLY LEU ARG MET ASP ALA ALA
SEQRES 5 A 321 ILE LYS ARG MET LYS GLU TYR ALA SER LYS ASP ASP HIS
SEQRES 6 A 321 ARG ASP PHE ALA GLY GLU LEU GLU VAL LEU CYS LYS LEU
SEQRES 7 A 321 GLY HIS HIS PRO ASN ILE ILE ASN LEU LEU GLY ALA CYS
SEQRES 8 A 321 GLU HIS ARG GLY TYR LEU TYR LEU ALA ILE GLU TYR ALA
SEQRES 9 A 321 PRO HIS GLY ASN LEU LEU ASP PHE LEU ARG LYS SER ARG
SEQRES 10 A 321 VAL LEU GLU THR ASP PRO ALA PHE ALA ILE ALA ASN SER
SEQRES 11 A 321 THR ALA SER THR LEU SER SER GLN GLN LEU LEU HIS PHE
SEQRES 12 A 321 ALA ALA ASP VAL ALA ARG GLY MET ASP TYR LEU SER GLN
SEQRES 13 A 321 LYS GLN PHE ILE HIS ARG ASN LEU ALA ALA ARG ASN ILE
SEQRES 14 A 321 LEU VAL GLY GLU ASN TYR VAL ALA LYS ILE ALA ASP PHE
SEQRES 15 A 321 GLY LEU SER ARG GLY GLN GLU VAL TYR VAL LYS LYS THR
SEQRES 16 A 321 MET GLY ARG LEU PRO VAL ARG TRP MET ALA ILE GLU SER
SEQRES 17 A 321 LEU ASN TYR SER VAL TYR THR THR ASN SER ASP VAL TRP
SEQRES 18 A 321 SER TYR GLY VAL LEU LEU TRP GLU ILE VAL SER LEU GLY
SEQRES 19 A 321 GLY THR PRO TYR CYS GLY MET THR CYS ALA GLU LEU TYR
SEQRES 20 A 321 GLU LYS LEU PRO GLN GLY TYR ARG LEU GLU LYS PRO LEU
SEQRES 21 A 321 ASN CYS ASP ASP GLU VAL TYR ASP LEU MET ARG GLN CYS
SEQRES 22 A 321 TRP ARG GLU LYS PRO TYR GLU ARG PRO SER PHE ALA GLN
SEQRES 23 A 321 ILE LEU VAL SER LEU ASN ARG MET LEU GLU GLU ARG LYS
SEQRES 24 A 321 THR TYR VAL ASN THR THR LEU TYR GLU LYS PHE THR TYR
SEQRES 25 A 321 ALA GLY ILE ASP CYS SER ALA GLU GLU
HET 3WR A1201 33
HETNAM 3WR 1-[4-(4-AMINO-5-OXOPYRIDO[2,3-D]PYRIMIDIN-8(5H)-YL)
HETNAM 2 3WR PHENYL]-3-[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]UREA
FORMUL 2 3WR C21 H14 F4 N6 O2
FORMUL 3 HOH *17(H2 O)
HELIX 1 AA1 LEU A 873 LEU A 879 1 7
HELIX 2 AA2 ASN A 909 SER A 917 1 9
HELIX 3 AA3 ARG A 918 ASP A 923 1 6
HELIX 4 AA4 ASP A 923 SER A 931 1 9
HELIX 5 AA5 SER A 937 LYS A 958 1 22
HELIX 6 AA6 ALA A 966 ARG A 968 5 3
HELIX 7 AA7 GLU A 974 TYR A 976 5 3
HELIX 8 AA8 ALA A 1006 SER A 1013 1 8
HELIX 9 AA9 THR A 1016 SER A 1033 1 18
HELIX 10 AB1 THR A 1043 LEU A 1051 1 9
HELIX 11 AB2 ASP A 1064 TRP A 1075 1 12
HELIX 12 AB3 LYS A 1078 ARG A 1082 5 5
HELIX 13 AB4 SER A 1084 GLU A 1098 1 15
SHEET 1 AA1 3 LEU A 839 ALA A 841 0
SHEET 2 AA1 3 ALA A 852 ILE A 854 -1 O ILE A 854 N LEU A 839
SHEET 3 AA1 3 ALA A 901 GLU A 903 -1 O ILE A 902 N ALA A 853
SHEET 1 AA2 2 ILE A 970 VAL A 972 0
SHEET 2 AA2 2 ALA A 978 ILE A 980 -1 O LYS A 979 N LEU A 971
SITE 1 AC1 14 ALA A 853 GLU A 872 VAL A 875 ILE A 902
SITE 2 AC1 14 GLU A 903 TYR A 904 ALA A 905 PHE A 960
SITE 3 AC1 14 HIS A 962 LEU A 971 ILE A 980 ALA A 981
SITE 4 AC1 14 ASP A 982 PHE A 983
CRYST1 62.456 62.456 178.450 90.00 90.00 90.00 P 41 21 2 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 0.016011 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016011 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005604 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
