HEADER TRANSFERASE/TRANSFERASE INHIBITOR 07-DEC-16 5U6C
TITLE CRYSTAL STRUCTURE OF THE MER KINASE DOMAIN IN COMPLEX WITH A
TITLE 2 MACROCYCLIC INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE MER;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 570-864;
COMPND 5 SYNONYM: PROTO-ONCOGENE C-MER,RECEPTOR TYROSINE KINASE MERTK;
COMPND 6 EC: 2.7.10.1;
COMPND 7 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: MERTK, MER;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.GAJIWALA,R.A.FERRE
REVDAT 4 04-OCT-23 5U6C 1 REMARK
REVDAT 3 04-OCT-17 5U6C 1 JRNL
REVDAT 2 02-AUG-17 5U6C 1 JRNL
REVDAT 1 26-JUL-17 5U6C 0
JRNL AUTH K.S.GAJIWALA,N.GRODSKY,B.BOLANOS,J.FENG,R.FERRE,
JRNL AUTH 2 S.TIMOFEEVSKI,M.XU,B.W.MURRAY,T.W.JOHNSON,A.STEWART
JRNL TITL THE AXL KINASE DOMAIN IN COMPLEX WITH A MACROCYCLIC
JRNL TITL 2 INHIBITOR OFFERS FIRST STRUCTURAL INSIGHTS INTO AN ACTIVE
JRNL TITL 3 TAM RECEPTOR KINASE.
JRNL REF J. BIOL. CHEM. V. 292 15705 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28724631
JRNL DOI 10.1074/JBC.M116.771485
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 35066
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1743
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.38
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2006
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2390
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1908
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.89
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 4253
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.02690
REMARK 3 B22 (A**2) : 4.51350
REMARK 3 B33 (A**2) : 8.51350
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.58930
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.300
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.228
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.194
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.231
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.197
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 : 0.875
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4422 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5983 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1575 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 107 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 675 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4422 ; 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 : 552 ; 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 : 5150 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.68
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.88
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 5U6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35110
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 92.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: 2P0C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 28-35% PEG
REMARK 280 600, 0.1 M TRIS (PH 8.7-9.0), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 46.16500
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 550
REMARK 465 GLY A 551
REMARK 465 SER A 552
REMARK 465 SER A 553
REMARK 465 HIS A 554
REMARK 465 HIS A 555
REMARK 465 HIS A 556
REMARK 465 HIS A 557
REMARK 465 HIS A 558
REMARK 465 HIS A 559
REMARK 465 SER A 560
REMARK 465 SER A 561
REMARK 465 GLY A 562
REMARK 465 GLU A 563
REMARK 465 ASN A 564
REMARK 465 LEU A 565
REMARK 465 TYR A 566
REMARK 465 PHE A 567
REMARK 465 GLN A 568
REMARK 465 GLY A 569
REMARK 465 SER A 570
REMARK 465 GLU A 571
REMARK 465 SER A 660
REMARK 465 SER A 661
REMARK 465 GLN A 662
REMARK 465 GLY A 663
REMARK 465 LYS A 746
REMARK 465 LYS A 747
REMARK 465 ILE A 748
REMARK 465 TYR A 749
REMARK 465 SER A 750
REMARK 465 GLY A 751
REMARK 465 ASP A 752
REMARK 465 TYR A 753
REMARK 465 TYR A 754
REMARK 465 ARG A 755
REMARK 465 GLN A 756
REMARK 465 GLY A 757
REMARK 465 ARG A 758
REMARK 465 ILE A 759
REMARK 465 ALA A 760
REMARK 465 LYS A 761
REMARK 465 MET A 762
REMARK 465 MET B 550
REMARK 465 GLY B 551
REMARK 465 SER B 552
REMARK 465 SER B 553
REMARK 465 HIS B 554
REMARK 465 HIS B 555
REMARK 465 HIS B 556
REMARK 465 HIS B 557
REMARK 465 HIS B 558
REMARK 465 HIS B 559
REMARK 465 SER B 560
REMARK 465 SER B 561
REMARK 465 GLY B 562
REMARK 465 GLU B 563
REMARK 465 ASN B 564
REMARK 465 LEU B 565
REMARK 465 TYR B 566
REMARK 465 PHE B 567
REMARK 465 GLN B 568
REMARK 465 GLY B 569
REMARK 465 SER B 570
REMARK 465 GLU B 571
REMARK 465 GLU B 572
REMARK 465 LEU B 573
REMARK 465 GLN B 574
REMARK 465 GLY B 596
REMARK 465 GLU B 597
REMARK 465 PHE B 598
REMARK 465 LYS B 622
REMARK 465 LEU B 623
REMARK 465 ASP B 624
REMARK 465 ASN B 625
REMARK 465 SER B 626
REMARK 465 SER B 627
REMARK 465 GLN B 628
REMARK 465 ARG B 629
REMARK 465 GLU B 630
REMARK 465 GLY B 743
REMARK 465 LEU B 744
REMARK 465 SER B 745
REMARK 465 LYS B 746
REMARK 465 LYS B 747
REMARK 465 ILE B 748
REMARK 465 TYR B 749
REMARK 465 SER B 750
REMARK 465 GLY B 751
REMARK 465 ASP B 752
REMARK 465 TYR B 753
REMARK 465 TYR B 754
REMARK 465 ARG B 755
REMARK 465 GLN B 756
REMARK 465 GLY B 757
REMARK 465 ARG B 758
REMARK 465 ILE B 759
REMARK 465 ALA B 760
REMARK 465 LYS B 761
REMARK 465 ASP B 863
REMARK 465 VAL B 864
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 ARG A 722 -5.13 77.64
REMARK 500 ASP A 723 42.02 -142.32
REMARK 500 ASP A 741 -58.25 73.14
REMARK 500 LEU A 744 90.85 -63.34
REMARK 500 ARG A 775 3.55 -62.03
REMARK 500 ARG B 722 -6.02 76.71
REMARK 500 ASP B 723 39.66 -148.06
REMARK 500 ASP B 774 -158.05 -91.09
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 7YS A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7YS B 9001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U6B RELATED DB: PDB
DBREF 5U6C A 570 864 UNP Q12866 MERTK_HUMAN 570 864
DBREF 5U6C B 570 864 UNP Q12866 MERTK_HUMAN 570 864
SEQADV 5U6C MET A 550 UNP Q12866 INITIATING METHIONINE
SEQADV 5U6C GLY A 551 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER A 552 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER A 553 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS A 554 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS A 555 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS A 556 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS A 557 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS A 558 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS A 559 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER A 560 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER A 561 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLY A 562 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLU A 563 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C ASN A 564 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C LEU A 565 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C TYR A 566 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C PHE A 567 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLN A 568 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLY A 569 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C MET A 650 UNP Q12866 ILE 650 CONFLICT
SEQADV 5U6C MET B 550 UNP Q12866 INITIATING METHIONINE
SEQADV 5U6C GLY B 551 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER B 552 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER B 553 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS B 554 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS B 555 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS B 556 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS B 557 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS B 558 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C HIS B 559 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER B 560 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C SER B 561 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLY B 562 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLU B 563 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C ASN B 564 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C LEU B 565 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C TYR B 566 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C PHE B 567 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLN B 568 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C GLY B 569 UNP Q12866 EXPRESSION TAG
SEQADV 5U6C MET B 650 UNP Q12866 ILE 650 CONFLICT
SEQRES 1 A 315 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 315 GLU ASN LEU TYR PHE GLN GLY SER GLU GLU LEU GLN ASN
SEQRES 3 A 315 LYS LEU GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE
SEQRES 4 A 315 LEU GLY LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL
SEQRES 5 A 315 MET GLU GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU
SEQRES 6 A 315 LYS VAL ALA VAL LYS THR MET LYS LEU ASP ASN SER SER
SEQRES 7 A 315 GLN ARG GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS
SEQRES 8 A 315 MET LYS ASP PHE SER HIS PRO ASN VAL MET ARG LEU LEU
SEQRES 9 A 315 GLY VAL CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS
SEQRES 10 A 315 PRO MET VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU
SEQRES 11 A 315 HIS THR TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO
SEQRES 12 A 315 LYS HIS ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL
SEQRES 13 A 315 ASP ILE ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN
SEQRES 14 A 315 PHE LEU HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU
SEQRES 15 A 315 ARG ASP ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU
SEQRES 16 A 315 SER LYS LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY
SEQRES 17 A 315 ARG ILE ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU
SEQRES 18 A 315 SER LEU ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL
SEQRES 19 A 315 TRP ALA PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG
SEQRES 20 A 315 GLY MET THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET
SEQRES 21 A 315 TYR ASP TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO
SEQRES 22 A 315 GLU ASP CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER
SEQRES 23 A 315 CYS TRP ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER
SEQRES 24 A 315 VAL LEU ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU
SEQRES 25 A 315 PRO ASP VAL
SEQRES 1 B 315 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 315 GLU ASN LEU TYR PHE GLN GLY SER GLU GLU LEU GLN ASN
SEQRES 3 B 315 LYS LEU GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE
SEQRES 4 B 315 LEU GLY LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL
SEQRES 5 B 315 MET GLU GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU
SEQRES 6 B 315 LYS VAL ALA VAL LYS THR MET LYS LEU ASP ASN SER SER
SEQRES 7 B 315 GLN ARG GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS
SEQRES 8 B 315 MET LYS ASP PHE SER HIS PRO ASN VAL MET ARG LEU LEU
SEQRES 9 B 315 GLY VAL CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS
SEQRES 10 B 315 PRO MET VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU
SEQRES 11 B 315 HIS THR TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO
SEQRES 12 B 315 LYS HIS ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL
SEQRES 13 B 315 ASP ILE ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN
SEQRES 14 B 315 PHE LEU HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU
SEQRES 15 B 315 ARG ASP ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU
SEQRES 16 B 315 SER LYS LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY
SEQRES 17 B 315 ARG ILE ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU
SEQRES 18 B 315 SER LEU ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL
SEQRES 19 B 315 TRP ALA PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG
SEQRES 20 B 315 GLY MET THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET
SEQRES 21 B 315 TYR ASP TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO
SEQRES 22 B 315 GLU ASP CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER
SEQRES 23 B 315 CYS TRP ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER
SEQRES 24 B 315 VAL LEU ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU
SEQRES 25 B 315 PRO ASP VAL
HET 7YS A9001 32
HET 7YS B9001 32
HETNAM 7YS (10R)-7-AMINO-11-CHLORO-12-FLUORO-1-(2-HYDROXYETHYL)-3,
HETNAM 2 7YS 10,16-TRIMETHYL-16,17-DIHYDRO-1H-8,4-(AZENO)
HETNAM 3 7YS PYRAZOLO[4,3-H][2,5,11]BENZOXADIAZACYCLOTETRADECIN-
HETNAM 4 7YS 15(10H)-ONE
FORMUL 3 7YS 2(C21 H22 CL F N6 O3)
FORMUL 5 HOH *174(H2 O)
HELIX 1 AA1 GLN A 574 VAL A 581 1 8
HELIX 2 AA2 ASP A 583 ASN A 585 5 3
HELIX 3 AA3 GLN A 628 PHE A 644 1 17
HELIX 4 AA4 ASP A 678 SER A 686 1 9
HELIX 5 AA5 PRO A 696 ARG A 717 1 22
HELIX 6 AA6 ALA A 725 ARG A 727 5 3
HELIX 7 AA7 PRO A 763 ILE A 767 5 5
HELIX 8 AA8 ALA A 768 ASP A 774 1 7
HELIX 9 AA9 THR A 778 THR A 795 1 18
HELIX 10 AB1 GLN A 805 HIS A 807 5 3
HELIX 11 AB2 GLU A 808 HIS A 815 1 8
HELIX 12 AB3 LEU A 826 CYS A 836 1 11
HELIX 13 AB4 ASP A 840 ARG A 844 5 5
HELIX 14 AB5 THR A 846 SER A 860 1 15
HELIX 15 AB6 LYS B 576 VAL B 581 1 6
HELIX 16 AB7 ASP B 583 ASN B 585 5 3
HELIX 17 AB8 GLU B 632 ASP B 643 1 12
HELIX 18 AB9 ASP B 678 SER B 686 1 9
HELIX 19 AC1 PRO B 696 ARG B 717 1 22
HELIX 20 AC2 ALA B 725 ARG B 727 5 3
HELIX 21 AC3 PRO B 763 ILE B 767 5 5
HELIX 22 AC4 ALA B 768 ASP B 774 1 7
HELIX 23 AC5 THR B 778 THR B 795 1 18
HELIX 24 AC6 GLN B 805 HIS B 807 5 3
HELIX 25 AC7 GLU B 808 HIS B 815 1 8
HELIX 26 AC8 LEU B 826 CYS B 836 1 11
HELIX 27 AC9 ASP B 840 ARG B 844 5 5
HELIX 28 AD1 THR B 846 LEU B 861 1 16
SHEET 1 AA1 5 LEU A 587 GLY A 594 0
SHEET 2 AA1 5 VAL A 601 LYS A 607 -1 O VAL A 601 N GLY A 594
SHEET 3 AA1 5 SER A 613 THR A 620 -1 O VAL A 616 N GLY A 604
SHEET 4 AA1 5 LYS A 666 PRO A 672 -1 O LEU A 671 N ALA A 617
SHEET 5 AA1 5 GLY A 654 GLU A 658 -1 N GLY A 654 O ILE A 670
SHEET 1 AA2 2 CYS A 729 LEU A 731 0
SHEET 2 AA2 2 VAL A 737 VAL A 739 -1 O CYS A 738 N MET A 730
SHEET 1 AA3 5 LEU B 587 GLY B 594 0
SHEET 2 AA3 5 VAL B 601 LYS B 607 -1 O VAL B 601 N GLY B 594
SHEET 3 AA3 5 SER B 613 THR B 620 -1 O LEU B 614 N LEU B 606
SHEET 4 AA3 5 PRO B 665 PRO B 672 -1 O LEU B 671 N ALA B 617
SHEET 5 AA3 5 GLY B 654 MET B 659 -1 N GLU B 658 O LYS B 666
SHEET 1 AA4 2 CYS B 729 LEU B 731 0
SHEET 2 AA4 2 VAL B 737 VAL B 739 -1 O CYS B 738 N MET B 730
SITE 1 AC1 15 LEU A 593 VAL A 601 ALA A 617 MET A 650
SITE 2 AC1 15 LEU A 671 PRO A 672 PHE A 673 MET A 674
SITE 3 AC1 15 GLY A 677 ASP A 678 ARG A 727 ASN A 728
SITE 4 AC1 15 MET A 730 ALA A 740 HOH A9151
SITE 1 AC2 14 LEU B 593 VAL B 601 ALA B 617 MET B 650
SITE 2 AC2 14 PRO B 672 PHE B 673 MET B 674 GLY B 677
SITE 3 AC2 14 ASP B 678 ARG B 727 ASN B 728 MET B 730
SITE 4 AC2 14 ALA B 740 ASP B 741
CRYST1 51.692 92.330 69.269 90.00 100.80 90.00 P 1 21 1 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 0.019345 0.000000 0.003690 0.00000
SCALE2 0.000000 0.010831 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014697 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
