HEADER TRANSFERASE 03-AUG-07 2QU5
TITLE CRYSTAL STRUCTURE OF THE VEGFR2 KINASE DOMAIN IN COMPLEX WITH A
TITLE 2 BENZIMIDAZOLE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: VEGFR-2, KINASE INSERT DOMAIN RECEPTOR, PROTEIN-TYROSINE
COMPND 6 KINASE RECEPTOR FLK-1, CD309 ANTIGEN;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: KDR, FLK1;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS RECEPTOR TYROSINSE KINASE, KDR, ANGIOGENESIS, ATP-BINDING,
KEYWDS 2 DEVELOPMENTAL PROTEIN, DIFFERENTIATION, GLYCOPROTEIN, HOST-VIRUS
KEYWDS 3 INTERACTION, IMMUNOGLOBULIN DOMAIN, MEMBRANE, NUCLEOTIDE-BINDING,
KEYWDS 4 PHOSPHORYLATION, POLYMORPHISM, TRANSFERASE, TRANSMEMBRANE, TYROSINE-
KEYWDS 5 PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,J.L.KIM,A.M.LONG,P.ROSE,Y.GU,H.ZHAO
REVDAT 6 15-NOV-23 2QU5 1 REMARK
REVDAT 5 30-AUG-23 2QU5 1 REMARK
REVDAT 4 20-OCT-21 2QU5 1 SEQADV
REVDAT 3 02-AUG-17 2QU5 1 SOURCE REMARK
REVDAT 2 24-FEB-09 2QU5 1 VERSN
REVDAT 1 25-SEP-07 2QU5 0
JRNL AUTH M.H.POTASHMAN,J.BREADY,A.COXON,T.M.DEMELFI,L.DIPIETRO,
JRNL AUTH 2 N.DOERR,D.ELBAUM,J.ESTRADA,P.GALLANT,J.GERMAIN,Y.GU,
JRNL AUTH 3 J.C.HARMANGE,S.A.KAUFMAN,R.KENDALL,J.L.KIM,G.N.KUMAR,
JRNL AUTH 4 A.M.LONG,S.NEERVANNAN,V.F.PATEL,A.POLVERINO,P.ROSE,S.V.PLAS,
JRNL AUTH 5 D.WHITTINGTON,R.ZANON,H.ZHAO
JRNL TITL DESIGN, SYNTHESIS, AND EVALUATION OF ORALLY ACTIVE
JRNL TITL 2 BENZIMIDAZOLES AND BENZOXAZOLES AS VASCULAR ENDOTHELIAL
JRNL TITL 3 GROWTH FACTOR-2 RECEPTOR TYROSINE KINASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 50 4351 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17696416
JRNL DOI 10.1021/JM070034I
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 12418
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1273
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 : 2337
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.90600
REMARK 3 B22 (A**2) : -1.49400
REMARK 3 B33 (A**2) : -0.41200
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.44
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) : 0.50
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.380
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 2QU5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044058.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12783
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR 2.4
REMARK 200 STARTING MODEL: PDB ENTRY 2P2I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, LITHUM SULFATE, TRIS, PH
REMARK 280 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 33.42600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.91400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.42600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.91400
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 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 GLU A 815
REMARK 465 ARG A 1051
REMARK 465 ASP A 1052
REMARK 465 ILE A 1053
REMARK 465 PTR A 1054
REMARK 465 LYS A 1055
REMARK 465 ASP A 1056
REMARK 465 PRO A 1057
REMARK 465 ASP A 1058
REMARK 465 PTR A 1059
REMARK 465 VAL A 1060
REMARK 465 ARG A 1061
REMARK 465 LYS A 1062
REMARK 465 GLY A 1063
REMARK 465 ASP A 1171
REMARK 465 ARG A 1172
REMARK 465 HIS A 1173
REMARK 465 HIS A 1174
REMARK 465 HIS A 1175
REMARK 465 HIS A 1176
REMARK 465 HIS A 1177
REMARK 465 HIS A 1178
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 ASP A 857 -167.85 -115.20
REMARK 500 ALA A 860 157.60 161.08
REMARK 500 LYS A 907 152.49 -43.68
REMARK 500 GLU A 934 55.18 -144.85
REMARK 500 GLU A 993 -16.36 90.60
REMARK 500 ASP A 998 31.10 74.58
REMARK 500 ARG A1027 -25.74 94.02
REMARK 500 ASP A1028 53.10 -145.06
REMARK 500 SER A1037 -168.17 -103.66
REMARK 500 LYS A1039 50.56 70.42
REMARK 500 LEU A1067 55.41 37.61
REMARK 500 ARG A1080 55.84 39.34
REMARK 500 ALA A1103 173.67 -56.31
REMARK 500 ASP A1112 -156.98 -123.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QU6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE VEGFR2 KINASE DOMAIN IN COMPLEX WITH A
REMARK 900 BENZOXAZOLE INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS IS A DELETION MUTANT (RESIDUES 940-989) OF UNIPROT
REMARK 999 ENTRY P35968.
DBREF 2QU5 A 815 939 UNP P35968 VGFR2_HUMAN 815 939
DBREF 2QU5 A 990 1171 UNP P35968 VGFR2_HUMAN 990 1171
SEQADV 2QU5 ALA A 817 UNP P35968 CYS 817 ENGINEERED MUTATION
SEQADV 2QU5 THR A 916 UNP P35968 VAL 916 ENGINEERED MUTATION
SEQADV 2QU5 VAL A 990 UNP P35968 GLU 990 ENGINEERED MUTATION
SEQADV 2QU5 PTR A 1054 UNP P35968 TYR 1054 MODIFIED RESIDUE
SEQADV 2QU5 PTR A 1059 UNP P35968 TYR 1059 MODIFIED RESIDUE
SEQADV 2QU5 ARG A 1172 UNP P35968 EXPRESSION TAG
SEQADV 2QU5 HIS A 1173 UNP P35968 EXPRESSION TAG
SEQADV 2QU5 HIS A 1174 UNP P35968 EXPRESSION TAG
SEQADV 2QU5 HIS A 1175 UNP P35968 EXPRESSION TAG
SEQADV 2QU5 HIS A 1176 UNP P35968 EXPRESSION TAG
SEQADV 2QU5 HIS A 1177 UNP P35968 EXPRESSION TAG
SEQADV 2QU5 HIS A 1178 UNP P35968 EXPRESSION TAG
SEQRES 1 A 314 GLU HIS ALA GLU ARG LEU PRO TYR ASP ALA SER LYS TRP
SEQRES 2 A 314 GLU PHE PRO ARG ASP ARG LEU LYS LEU GLY LYS PRO LEU
SEQRES 3 A 314 GLY ARG GLY ALA PHE GLY GLN VAL ILE GLU ALA ASP ALA
SEQRES 4 A 314 PHE GLY ILE ASP LYS THR ALA THR CYS ARG THR VAL ALA
SEQRES 5 A 314 VAL LYS MET LEU LYS GLU GLY ALA THR HIS SER GLU HIS
SEQRES 6 A 314 ARG ALA LEU MET SER GLU LEU LYS ILE LEU ILE HIS ILE
SEQRES 7 A 314 GLY HIS HIS LEU ASN VAL VAL ASN LEU LEU GLY ALA CYS
SEQRES 8 A 314 THR LYS PRO GLY GLY PRO LEU MET VAL ILE THR GLU PHE
SEQRES 9 A 314 CYS LYS PHE GLY ASN LEU SER THR TYR LEU ARG SER LYS
SEQRES 10 A 314 ARG ASN GLU PHE VAL PRO TYR LYS VAL ALA PRO GLU ASP
SEQRES 11 A 314 LEU TYR LYS ASP PHE LEU THR LEU GLU HIS LEU ILE CYS
SEQRES 12 A 314 TYR SER PHE GLN VAL ALA LYS GLY MET GLU PHE LEU ALA
SEQRES 13 A 314 SER ARG LYS CYS ILE HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 14 A 314 ILE LEU LEU SER GLU LYS ASN VAL VAL LYS ILE CYS ASP
SEQRES 15 A 314 PHE GLY LEU ALA ARG ASP ILE PTR LYS ASP PRO ASP PTR
SEQRES 16 A 314 VAL ARG LYS GLY ASP ALA ARG LEU PRO LEU LYS TRP MET
SEQRES 17 A 314 ALA PRO GLU THR ILE PHE ASP ARG VAL TYR THR ILE GLN
SEQRES 18 A 314 SER ASP VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE
SEQRES 19 A 314 PHE SER LEU GLY ALA SER PRO TYR PRO GLY VAL LYS ILE
SEQRES 20 A 314 ASP GLU GLU PHE CYS ARG ARG LEU LYS GLU GLY THR ARG
SEQRES 21 A 314 MET ARG ALA PRO ASP TYR THR THR PRO GLU MET TYR GLN
SEQRES 22 A 314 THR MET LEU ASP CYS TRP HIS GLY GLU PRO SER GLN ARG
SEQRES 23 A 314 PRO THR PHE SER GLU LEU VAL GLU HIS LEU GLY ASN LEU
SEQRES 24 A 314 LEU GLN ALA ASN ALA GLN GLN ASP ARG HIS HIS HIS HIS
SEQRES 25 A 314 HIS HIS
HET 276 A 501 32
HETNAM 276 4-[[2-[[4-CHLORO-3-(TRIFLUOROMETHYL)PHENYL]AMINO]-3H-
HETNAM 2 276 BENZIMIDAZOL-5-YL]OXY]-N-METHYL-PYRIDINE-2-CARBOXAMIDE
FORMUL 2 276 C21 H15 CL F3 N5 O2
FORMUL 3 HOH *6(H2 O)
HELIX 1 1 ASP A 823 GLU A 828 1 6
HELIX 2 2 PRO A 830 ASP A 832 5 3
HELIX 3 3 SER A 877 GLY A 893 1 17
HELIX 4 4 ASN A 923 SER A 930 1 8
HELIX 5 5 THR A 1001 ARG A 1022 1 22
HELIX 6 6 ALA A 1030 ARG A 1032 5 3
HELIX 7 7 LEU A 1067 MET A 1072 5 6
HELIX 8 8 ALA A 1073 ARG A 1080 1 8
HELIX 9 9 THR A 1083 PHE A 1099 1 17
HELIX 10 10 ASP A 1112 GLY A 1122 1 11
HELIX 11 11 THR A 1132 TRP A 1143 1 12
HELIX 12 12 GLU A 1146 ARG A 1150 5 5
HELIX 13 13 THR A 1152 GLN A 1170 1 19
SHEET 1 A 5 LEU A 834 ARG A 842 0
SHEET 2 A 5 GLY A 846 PHE A 854 -1 O VAL A 848 N LEU A 840
SHEET 3 A 5 CYS A 862 LEU A 870 -1 O VAL A 867 N ILE A 849
SHEET 4 A 5 MET A 913 GLU A 917 -1 O THR A 916 N ALA A 866
SHEET 5 A 5 LEU A 901 CYS A 905 -1 N GLY A 903 O ILE A 915
SHEET 1 B 2 ILE A1034 LEU A1036 0
SHEET 2 B 2 VAL A1042 ILE A1044 -1 O LYS A1043 N LEU A1035
CISPEP 1 ALA A 991 PRO A 992 0 0.49
CRYST1 66.852 143.828 58.483 90.00 90.00 90.00 P 21 21 2 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 0.014958 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017099 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
