HEADER TRANSFERASE 15-MAY-18 5ZWJ
TITLE CRYSTAL STRUCTURE OF EGFR 675-1022 T790M/C797S/V948R IN COMPLEX WITH
TITLE 2 EAI045
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE
COMPND 5 ERBB-1;
COMPND 6 EC: 2.7.10.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: EGFR, ERBB, ERBB1, HER1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS EGFR T790M, C797S, EAI045, SIGNALING PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.ZHAO,C.H.YUN
REVDAT 2 27-MAR-24 5ZWJ 1 REMARK
REVDAT 1 25-JUL-18 5ZWJ 0
JRNL AUTH P.ZHAO,M.Y.YAO,S.J.ZHU,J.Y.CHEN,C.H.YUN
JRNL TITL CRYSTAL STRUCTURE OF EGFR T790M/C797S/V948R IN COMPLEX WITH
JRNL TITL 2 EAI045.
JRNL REF BIOCHEM. BIOPHYS. RES. V. 502 332 2018
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 29802850
JRNL DOI 10.1016/J.BBRC.2018.05.154
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 9563
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 464
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.6933 - 4.1820 0.99 3177 161 0.2322 0.2368
REMARK 3 2 4.1820 - 3.3196 1.00 2976 156 0.2793 0.3229
REMARK 3 3 3.3196 - 2.9001 1.00 2946 147 0.3389 0.3792
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.016 2144
REMARK 3 ANGLE : 1.392 2915
REMARK 3 CHIRALITY : 0.300 334
REMARK 3 PLANARITY : 0.005 361
REMARK 3 DIHEDRAL : 19.374 768
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5ZWJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1300007787.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91905
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10084
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 17.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 4000, 0.1 M KCL, 0.05 M TRIS
REMARK 280 PH 7.5-8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 71.69167
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 143.38333
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 107.53750
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 179.22917
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 35.84583
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 71.69167
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 143.38333
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 179.22917
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 107.53750
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 35.84583
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 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 GLY A 674
REMARK 465 ARG A 675
REMARK 465 LYS A 676
REMARK 465 ARG A 677
REMARK 465 THR A 678
REMARK 465 LEU A 679
REMARK 465 ARG A 680
REMARK 465 ARG A 681
REMARK 465 LEU A 682
REMARK 465 LEU A 683
REMARK 465 GLN A 684
REMARK 465 GLU A 685
REMARK 465 ARG A 686
REMARK 465 GLU A 687
REMARK 465 LEU A 688
REMARK 465 VAL A 689
REMARK 465 GLU A 690
REMARK 465 PRO A 691
REMARK 465 LEU A 692
REMARK 465 THR A 693
REMARK 465 PRO A 694
REMARK 465 SER A 695
REMARK 465 GLY A 696
REMARK 465 GLU A 697
REMARK 465 ALA A 698
REMARK 465 PRO A 699
REMARK 465 ASN A 700
REMARK 465 GLN A 701
REMARK 465 ALA A 859
REMARK 465 LYS A 860
REMARK 465 LEU A 861
REMARK 465 LEU A 862
REMARK 465 GLY A 863
REMARK 465 ALA A 864
REMARK 465 GLU A 865
REMARK 465 GLU A 866
REMARK 465 LYS A 867
REMARK 465 GLU A 868
REMARK 465 TYR A 869
REMARK 465 HIS A 870
REMARK 465 ALA A 871
REMARK 465 GLU A 872
REMARK 465 GLY A 873
REMARK 465 GLY A 874
REMARK 465 LYS A 875
REMARK 465 ARG A 986
REMARK 465 MET A 987
REMARK 465 HIS A 988
REMARK 465 LEU A 989
REMARK 465 PRO A 990
REMARK 465 SER A 991
REMARK 465 PRO A 992
REMARK 465 THR A 993
REMARK 465 ASP A 994
REMARK 465 SER A 995
REMARK 465 ASN A 996
REMARK 465 PHE A 997
REMARK 465 TYR A 998
REMARK 465 ARG A 999
REMARK 465 ALA A 1000
REMARK 465 LEU A 1001
REMARK 465 MET A 1002
REMARK 465 ASP A 1003
REMARK 465 GLU A 1004
REMARK 465 GLU A 1005
REMARK 465 ASP A 1006
REMARK 465 MET A 1007
REMARK 465 ASP A 1008
REMARK 465 ASP A 1009
REMARK 465 VAL A 1010
REMARK 465 VAL A 1011
REMARK 465 ASP A 1012
REMARK 465 ALA A 1013
REMARK 465 ASP A 1014
REMARK 465 GLU A 1015
REMARK 465 TYR A 1016
REMARK 465 LEU A 1017
REMARK 465 ILE A 1018
REMARK 465 PRO A 1019
REMARK 465 GLN A 1020
REMARK 465 GLN A 1021
REMARK 465 GLY A 1022
REMARK 465 HIS A 1023
REMARK 465 HIS A 1024
REMARK 465 HIS A 1025
REMARK 465 HIS A 1026
REMARK 465 HIS A 1027
REMARK 465 HIS A 1028
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 LYS A 716 CG CD CE NZ
REMARK 470 LYS A 728 CG CD CE NZ
REMARK 470 GLU A 734 CG CD OE1 OE2
REMARK 470 GLU A 736 CD OE1 OE2
REMARK 470 LYS A 737 CG CD CE NZ
REMARK 470 LYS A 739 CG CD CE NZ
REMARK 470 ARG A 748 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 749 CG CD OE1 OE2
REMARK 470 GLU A 762 CD OE1 OE2
REMARK 470 LYS A 806 CG CD CE NZ
REMARK 470 ASN A 808 CG OD1 ND2
REMARK 470 ARG A 832 CD NE CZ NH1 NH2
REMARK 470 VAL A 876 CG1 CG2
REMARK 470 GLU A 884 OE1 OE2
REMARK 470 LYS A 913 CG CD CE NZ
REMARK 470 GLU A 922 OE1 OE2
REMARK 470 GLU A 931 CG CD OE1 OE2
REMARK 470 THR A 940 OG1 CG2
REMARK 470 LYS A 960 CD CE NZ
REMARK 470 GLU A 967 CG CD OE1 OE2
REMARK 470 LYS A 970 CG CD CE NZ
REMARK 470 ILE A 981 CG1 CG2 CD1
REMARK 470 GLN A 982 CG CD OE1 NE2
REMARK 470 GLU A 985 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 GLU A 749 -166.54 -167.93
REMARK 500 THR A 783 -143.44 -151.08
REMARK 500 ARG A 836 -0.41 74.18
REMARK 500 ASP A 837 44.08 -156.60
REMARK 500 GLN A 982 -129.87 51.85
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 9LL A 1101
DBREF 5ZWJ A 675 1022 UNP P00533 EGFR_HUMAN 675 1022
SEQADV 5ZWJ GLY A 674 UNP P00533 EXPRESSION TAG
SEQADV 5ZWJ MET A 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5ZWJ SER A 797 UNP P00533 CYS 797 ENGINEERED MUTATION
SEQADV 5ZWJ ARG A 948 UNP P00533 VAL 948 ENGINEERED MUTATION
SEQADV 5ZWJ HIS A 1023 UNP P00533 EXPRESSION TAG
SEQADV 5ZWJ HIS A 1024 UNP P00533 EXPRESSION TAG
SEQADV 5ZWJ HIS A 1025 UNP P00533 EXPRESSION TAG
SEQADV 5ZWJ HIS A 1026 UNP P00533 EXPRESSION TAG
SEQADV 5ZWJ HIS A 1027 UNP P00533 EXPRESSION TAG
SEQADV 5ZWJ HIS A 1028 UNP P00533 EXPRESSION TAG
SEQRES 1 A 355 GLY ARG LYS ARG THR LEU ARG ARG LEU LEU GLN GLU ARG
SEQRES 2 A 355 GLU LEU VAL GLU PRO LEU THR PRO SER GLY GLU ALA PRO
SEQRES 3 A 355 ASN GLN ALA LEU LEU ARG ILE LEU LYS GLU THR GLU PHE
SEQRES 4 A 355 LYS LYS ILE LYS VAL LEU GLY SER GLY ALA PHE GLY THR
SEQRES 5 A 355 VAL TYR LYS GLY LEU TRP ILE PRO GLU GLY GLU LYS VAL
SEQRES 6 A 355 LYS ILE PRO VAL ALA ILE LYS GLU LEU ARG GLU ALA THR
SEQRES 7 A 355 SER PRO LYS ALA ASN LYS GLU ILE LEU ASP GLU ALA TYR
SEQRES 8 A 355 VAL MET ALA SER VAL ASP ASN PRO HIS VAL CYS ARG LEU
SEQRES 9 A 355 LEU GLY ILE CYS LEU THR SER THR VAL GLN LEU ILE MET
SEQRES 10 A 355 GLN LEU MET PRO PHE GLY SER LEU LEU ASP TYR VAL ARG
SEQRES 11 A 355 GLU HIS LYS ASP ASN ILE GLY SER GLN TYR LEU LEU ASN
SEQRES 12 A 355 TRP CYS VAL GLN ILE ALA LYS GLY MET ASN TYR LEU GLU
SEQRES 13 A 355 ASP ARG ARG LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 14 A 355 VAL LEU VAL LYS THR PRO GLN HIS VAL LYS ILE THR ASP
SEQRES 15 A 355 PHE GLY LEU ALA LYS LEU LEU GLY ALA GLU GLU LYS GLU
SEQRES 16 A 355 TYR HIS ALA GLU GLY GLY LYS VAL PRO ILE LYS TRP MET
SEQRES 17 A 355 ALA LEU GLU SER ILE LEU HIS ARG ILE TYR THR HIS GLN
SEQRES 18 A 355 SER ASP VAL TRP SER TYR GLY VAL THR VAL TRP GLU LEU
SEQRES 19 A 355 MET THR PHE GLY SER LYS PRO TYR ASP GLY ILE PRO ALA
SEQRES 20 A 355 SER GLU ILE SER SER ILE LEU GLU LYS GLY GLU ARG LEU
SEQRES 21 A 355 PRO GLN PRO PRO ILE CYS THR ILE ASP VAL TYR MET ILE
SEQRES 22 A 355 MET ARG LYS CYS TRP MET ILE ASP ALA ASP SER ARG PRO
SEQRES 23 A 355 LYS PHE ARG GLU LEU ILE ILE GLU PHE SER LYS MET ALA
SEQRES 24 A 355 ARG ASP PRO GLN ARG TYR LEU VAL ILE GLN GLY ASP GLU
SEQRES 25 A 355 ARG MET HIS LEU PRO SER PRO THR ASP SER ASN PHE TYR
SEQRES 26 A 355 ARG ALA LEU MET ASP GLU GLU ASP MET ASP ASP VAL VAL
SEQRES 27 A 355 ASP ALA ASP GLU TYR LEU ILE PRO GLN GLN GLY HIS HIS
SEQRES 28 A 355 HIS HIS HIS HIS
HET 9LL A1101 27
HETNAM 9LL (2R)-2-(5-FLUORO-2-HYDROXYPHENYL)-2-(1-OXO-1,3-DIHYDRO-
HETNAM 2 9LL 2H-ISOINDOL-2-YL)-N-(1,3-THIAZOL-2-YL)ACETAMIDE
FORMUL 2 9LL C19 H14 F N3 O3 S
FORMUL 3 HOH *24(H2 O)
HELIX 1 AA1 SER A 752 VAL A 769 1 18
HELIX 2 AA2 LEU A 798 HIS A 805 1 8
HELIX 3 AA3 GLY A 810 ARG A 831 1 22
HELIX 4 AA4 ALA A 882 ARG A 889 1 8
HELIX 5 AA5 THR A 892 THR A 909 1 18
HELIX 6 AA6 PRO A 919 GLY A 930 1 12
HELIX 7 AA7 THR A 940 TRP A 951 1 12
HELIX 8 AA8 LYS A 960 ASP A 974 1 15
HELIX 9 AA9 ASP A 974 LEU A 979 1 6
SHEET 1 AA1 6 ARG A 705 ILE A 706 0
SHEET 2 AA1 6 LEU A 777 LEU A 782 1 O ILE A 780 N ARG A 705
SHEET 3 AA1 6 VAL A 786 GLN A 791 -1 O ILE A 789 N GLY A 779
SHEET 4 AA1 6 ILE A 740 LEU A 747 -1 N ALA A 743 O MET A 790
SHEET 5 AA1 6 GLY A 724 TRP A 731 -1 N GLY A 729 O VAL A 742
SHEET 6 AA1 6 PHE A 712 SER A 720 -1 N LYS A 716 O LYS A 728
SHEET 1 AA2 3 GLY A 796 SER A 797 0
SHEET 2 AA2 3 VAL A 843 VAL A 845 -1 O VAL A 845 N GLY A 796
SHEET 3 AA2 3 VAL A 851 ILE A 853 -1 O LYS A 852 N LEU A 844
SITE 1 AC1 12 VAL A 726 ALA A 743 LYS A 745 ILE A 759
SITE 2 AC1 12 MET A 766 ARG A 776 LEU A 777 MET A 790
SITE 3 AC1 12 THR A 854 ASP A 855 PHE A 856 LEU A 858
CRYST1 79.586 79.586 215.075 90.00 90.00 120.00 P 61 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 0.012565 0.007254 0.000000 0.00000
SCALE2 0.000000 0.014509 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004650 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
