HEADER TRANSFERASE/INHIBITOR 01-MAY-18 6DA4
TITLE JAK3 WITH CYANAMIDE CP10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: JANUS KINASE 3,JAK-3,LEUKOCYTE JANUS KINASE,L-JAK;
COMPND 6 EC: 2.7.10.2;
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: JAK3;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF21
KEYWDS KINASE, COVALENT, TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.F.VAJDOS
REVDAT 2 01-MAY-19 6DA4 1 JRNL
REVDAT 1 28-NOV-18 6DA4 0
JRNL AUTH A.CASIMIRO-GARCIA,J.I.TRUJILLO,F.VAJDOS,B.JUBA,M.E.BANKER,
JRNL AUTH 2 A.AULABAUGH,P.BALBO,J.BAUMAN,J.CHRENCIK,J.W.COE,
JRNL AUTH 3 R.CZERWINSKI,M.DOWTY,J.D.KNAFELS,S.KWON,L.LEUNG,S.LIANG,
JRNL AUTH 4 R.P.ROBINSON,J.B.TELLIEZ,R.UNWALLA,X.YANG,A.THORARENSEN
JRNL TITL IDENTIFICATION OF CYANAMIDE-BASED JANUS KINASE 3 (JAK3)
JRNL TITL 2 COVALENT INHIBITORS.
JRNL REF J. MED. CHEM. V. 61 10665 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30423248
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01308
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 7165
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.750
REMARK 3 FREE R VALUE TEST SET COUNT : 340
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 : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.06
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1943
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2937
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1865
REMARK 3 BIN R VALUE (WORKING SET) : 0.2907
REMARK 3 BIN FREE R VALUE : 0.3623
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 78
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2215
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 18
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -20.74390
REMARK 3 B22 (A**2) : 11.22620
REMARK 3 B33 (A**2) : 9.51770
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) : 0.405
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.430
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.898
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2318 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3158 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 794 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 50 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 369 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2318 ; 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 : 276 ; 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 : 2574 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.85
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.33
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6DA4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50218
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.990
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
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 (%): 42.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M (NH4)2SO4, 2%
REMARK 280 PHENYLUREA, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 23.19200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.81050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.75800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.81050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.19200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.75800
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 MET A 804
REMARK 465 GLY A 805
REMARK 465 HIS A 806
REMARK 465 HIS A 807
REMARK 465 HIS A 808
REMARK 465 HIS A 809
REMARK 465 HIS A 810
REMARK 465 HIS A 811
REMARK 465 GLN A 812
REMARK 465 ASP A 813
REMARK 465 PRO A 814
REMARK 465 CYS A 1040
REMARK 465 GLU A 1041
REMARK 465 ARG A 1042
REMARK 465 ASP A 1043
REMARK 465 SER A 1100
REMARK 465 GLY A 1101
REMARK 465 SER A 1102
REMARK 465 ARG A 1103
REMARK 465 GLY A 1104
REMARK 465 CYS A 1105
REMARK 465 GLU A 1106
REMARK 465 THR A 1107
REMARK 465 HIS A 1108
REMARK 465 ALA A 1109
REMARK 465 PHE A 1110
REMARK 465 THR A 1111
REMARK 465 ALA A 1112
REMARK 465 HIS A 1113
REMARK 465 PRO A 1114
REMARK 465 GLU A 1115
REMARK 465 GLY A 1116
REMARK 465 LYS A 1117
REMARK 465 HIS A 1118
REMARK 465 HIS A 1119
REMARK 465 SER A 1120
REMARK 465 LEU A 1121
REMARK 465 SER A 1122
REMARK 465 PHE A 1123
REMARK 465 SER A 1124
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 823 CG CD CE NZ
REMARK 470 ARG A 895 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 896 CG CD OE1 NE2
REMARK 470 SER A 897 OG
REMARK 470 LEU A 898 CG CD1 CD2
REMARK 470 ARG A 920 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 984 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 985 CD OE1 OE2
REMARK 470 VAL A1044 CG1 CG2
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 825 -77.26 -111.40
REMARK 500 PHE A 833 -0.03 57.52
REMARK 500 ASN A 847 33.18 77.79
REMARK 500 SER A 897 84.84 -68.72
REMARK 500 ARG A 948 -5.72 68.24
REMARK 500 ASP A 949 43.67 -149.74
REMARK 500 ALA A 966 -166.51 -125.34
REMARK 500 ASP A 967 93.47 46.10
REMARK 500 ILE A 991 -19.91 -46.02
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 G4V A 1201
DBREF 6DA4 A 812 1124 UNP P52333 JAK3_HUMAN 812 1124
SEQADV 6DA4 MET A 804 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 GLY A 805 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 HIS A 806 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 HIS A 807 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 HIS A 808 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 HIS A 809 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 HIS A 810 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 HIS A 811 UNP P52333 EXPRESSION TAG
SEQADV 6DA4 SER A 1048 UNP P52333 CYS 1048 ENGINEERED MUTATION
SEQRES 1 A 321 MET GLY HIS HIS HIS HIS HIS HIS GLN ASP PRO THR ILE
SEQRES 2 A 321 PHE GLU GLU ARG HIS LEU LYS TYR ILE SER GLN LEU GLY
SEQRES 3 A 321 LYS GLY ASN PHE GLY SER VAL GLU LEU CYS ARG TYR ASP
SEQRES 4 A 321 PRO LEU GLY ASP ASN THR GLY ALA LEU VAL ALA VAL LYS
SEQRES 5 A 321 GLN LEU GLN HIS SER GLY PRO ASP GLN GLN ARG ASP PHE
SEQRES 6 A 321 GLN ARG GLU ILE GLN ILE LEU LYS ALA LEU HIS SER ASP
SEQRES 7 A 321 PHE ILE VAL LYS TYR ARG GLY VAL SER TYR GLY PRO GLY
SEQRES 8 A 321 ARG GLN SER LEU ARG LEU VAL MET GLU TYR LEU PRO SER
SEQRES 9 A 321 GLY CYS LEU ARG ASP PHE LEU GLN ARG HIS ARG ALA ARG
SEQRES 10 A 321 LEU ASP ALA SER ARG LEU LEU LEU TYR SER SER GLN ILE
SEQRES 11 A 321 CYS LYS GLY MET GLU TYR LEU GLY SER ARG ARG CYS VAL
SEQRES 12 A 321 HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU VAL GLU SER
SEQRES 13 A 321 GLU ALA HIS VAL LYS ILE ALA ASP PHE GLY LEU ALA LYS
SEQRES 14 A 321 LEU LEU PRO LEU ASP LYS ASP TYR TYR VAL VAL ARG GLU
SEQRES 15 A 321 PRO GLY GLN SER PRO ILE PHE TRP TYR ALA PRO GLU SER
SEQRES 16 A 321 LEU SER ASP ASN ILE PHE SER ARG GLN SER ASP VAL TRP
SEQRES 17 A 321 SER PHE GLY VAL VAL LEU TYR GLU LEU PHE THR TYR CYS
SEQRES 18 A 321 ASP LYS SER CYS SER PRO SER ALA GLU PHE LEU ARG MET
SEQRES 19 A 321 MET GLY CYS GLU ARG ASP VAL PRO ALA LEU SER ARG LEU
SEQRES 20 A 321 LEU GLU LEU LEU GLU GLU GLY GLN ARG LEU PRO ALA PRO
SEQRES 21 A 321 PRO ALA CYS PRO ALA GLU VAL HIS GLU LEU MET LYS LEU
SEQRES 22 A 321 CYS TRP ALA PRO SER PRO GLN ASP ARG PRO SER PHE SER
SEQRES 23 A 321 ALA LEU GLY PRO GLN LEU ASP MET LEU TRP SER GLY SER
SEQRES 24 A 321 ARG GLY CYS GLU THR HIS ALA PHE THR ALA HIS PRO GLU
SEQRES 25 A 321 GLY LYS HIS HIS SER LEU SER PHE SER
HET G4V A1201 27
HETNAM G4V (Z)-1-{2,2-DIFLUORO-6-[5-(2-METHOXYETHYL)-7H-PYRROLO[2,
HETNAM 2 G4V 3-D]PYRIMIDIN-4-YL]-2,3-DIHYDRO-4H-1,4-BENZOXAZIN-4-
HETNAM 3 G4V YL}METHANIMINE
FORMUL 2 G4V C18 H17 F2 N5 O2
FORMUL 3 HOH *18(H2 O)
HELIX 1 AA1 GLU A 818 ARG A 820 5 3
HELIX 2 AA2 ASP A 863 ALA A 877 1 15
HELIX 3 AA3 CYS A 909 ARG A 918 1 10
HELIX 4 AA4 ASP A 922 ARG A 943 1 22
HELIX 5 AA5 ALA A 951 ARG A 953 5 3
HELIX 6 AA6 PRO A 990 TYR A 994 5 5
HELIX 7 AA7 ALA A 995 ASN A 1002 1 8
HELIX 8 AA8 SER A 1005 THR A 1022 1 18
HELIX 9 AA9 SER A 1029 MET A 1038 1 10
HELIX 10 AB1 PRO A 1045 GLU A 1056 1 12
HELIX 11 AB2 PRO A 1067 TRP A 1078 1 12
HELIX 12 AB3 SER A 1081 ARG A 1085 5 5
HELIX 13 AB4 SER A 1087 TRP A 1099 1 13
SHEET 1 AA1 5 LEU A 822 GLY A 831 0
SHEET 2 AA1 5 GLY A 834 TYR A 841 -1 O LEU A 838 N ILE A 825
SHEET 3 AA1 5 ALA A 850 LEU A 857 -1 O VAL A 854 N GLU A 837
SHEET 4 AA1 5 ARG A 899 GLU A 903 -1 O MET A 902 N ALA A 853
SHEET 5 AA1 5 TYR A 886 SER A 890 -1 N GLY A 888 O VAL A 901
SHEET 1 AA2 2 CYS A 945 VAL A 946 0
SHEET 2 AA2 2 LYS A 972 LEU A 973 -1 O LYS A 972 N VAL A 946
SHEET 1 AA3 2 ILE A 955 SER A 959 0
SHEET 2 AA3 2 HIS A 962 ILE A 965 -1 O LYS A 964 N LEU A 956
SHEET 1 AA4 2 TYR A 981 VAL A 982 0
SHEET 2 AA4 2 ILE A1003 PHE A1004 -1 O PHE A1004 N TYR A 981
LINK SG CYS A 909 C13 G4V A1201 1555 1555 1.75
CISPEP 1 GLY A 894 ARG A 895 0 2.17
SITE 1 AC1 9 LEU A 828 GLY A 829 LYS A 830 ALA A 853
SITE 2 AC1 9 GLU A 903 TYR A 904 LEU A 905 CYS A 909
SITE 3 AC1 9 LEU A 956
CRYST1 46.384 75.516 89.621 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 0.021559 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011158 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
