HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-JUN-16 5KMN
TITLE TRKA JM-KINASE WITH 1-(2-METHYL-4-PHENYL-PYRIMIDIN-5-YL)-3-[[2-
TITLE 2 (TRIFLUOROMETHYL)PHENYL]METHYL]UREA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH AFFINITY NERVE GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN WITH JUXTAMEMBRANE REGION, UNP RESIDUES
COMPND 5 376-698;
COMPND 6 SYNONYM: NEUROTROPHIC TYROSINE KINASE RECEPTOR TYPE 1,TRK1-
COMPND 7 TRANSFORMING TYROSINE KINASE PROTEIN,TROPOMYOSIN-RELATED KINASE A,
COMPND 8 TYROSINE KINASE RECEPTOR,TYROSINE KINASE RECEPTOR A,TRK-A,GP140TRK,
COMPND 9 P140-TRKA;
COMPND 10 EC: 2.7.10.1;
COMPND 11 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: NTRK1, MTC, TRK, TRKA;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, JUXTAMEMBRANE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.SU
REVDAT 3 01-FEB-17 5KMN 1 JRNL
REVDAT 2 18-JAN-17 5KMN 1 JRNL
REVDAT 1 28-DEC-16 5KMN 0
JRNL AUTH H.P.SU,K.RICKERT,C.BURLEIN,K.NARAYAN,M.BUKHTIYAROVA,
JRNL AUTH 2 D.M.HURZY,C.A.STUMP,X.ZHANG,J.REID,A.KRASOWSKA-ZOLADEK,
JRNL AUTH 3 S.TUMMALA,J.M.SHIPMAN,M.KORNIENKO,P.A.LEMAIRE,D.KROSKY,
JRNL AUTH 4 A.HELLER,A.ACHAB,C.CHAMBERLIN,P.SARADJIAN,B.SAUVAGNAT,
JRNL AUTH 5 X.YANG,M.R.ZIEBELL,E.NICKBARG,J.M.SANDERS,M.T.BILODEAU,
JRNL AUTH 6 S.S.CARROLL,K.J.LUMB,S.M.SOISSON,D.A.HENZE,A.J.COOKE
JRNL TITL STRUCTURAL CHARACTERIZATION OF NONACTIVE SITE,
JRNL TITL 2 TRKA-SELECTIVE KINASE INHIBITORS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E297 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28039433
JRNL DOI 10.1073/PNAS.1611577114
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 20182
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1030
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2934
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2125
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2786
REMARK 3 BIN R VALUE (WORKING SET) : 0.2104
REMARK 3 BIN FREE R VALUE : 0.2546
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.04
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
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 : 2333
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.58580
REMARK 3 B22 (A**2) : -1.58580
REMARK 3 B33 (A**2) : 3.17160
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) : 0.260
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.202
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.164
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.200
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.165
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 : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2419 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3277 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 820 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 49 ; 8.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 376 ; 8.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2419 ; 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 : 295 ; 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 : 2768 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.21
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.19
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 5KMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222465.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20356
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.136
REMARK 200 RESOLUTION RANGE LOW (A) : 44.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 0.51500
REMARK 200 R SYM FOR SHELL (I) : 0.51500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES PH 6.5, 150 MM NACL, 5MM
REMARK 280 TCEP, 0.1% BETA-OCTYLGLUCOSIDE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 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 -Y,-X,-Z+2/3
REMARK 290 5555 -X+Y,Y,-Z+1/3
REMARK 290 6555 X,X-Y,-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 -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 76.17667
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 152.35333
REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 152.35333
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 76.17667
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 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 TOTAL BURIED SURFACE AREA: 200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 GLU A 480
REMARK 465 GLY A 481
REMARK 465 LYS A 482
REMARK 465 GLY A 483
REMARK 465 SER A 484
REMARK 465 GLY A 485
REMARK 465 LEU A 486
REMARK 465 GLN A 487
REMARK 465 GLY A 488
REMARK 465 HIS A 489
REMARK 465 ILE A 490
REMARK 465 ILE A 491
REMARK 465 GLU A 492
REMARK 465 ASN A 493
REMARK 465 PRO A 494
REMARK 465 GLN A 495
REMARK 465 TYR A 496
REMARK 465 PHE A 497
REMARK 465 SER A 498
REMARK 465 GLU A 535
REMARK 465 GLN A 536
REMARK 465 ALA A 549
REMARK 465 LYS A 609
REMARK 465 LEU A 610
REMARK 465 LEU A 611
REMARK 465 ALA A 612
REMARK 465 GLY A 613
REMARK 465 HIS A 797
REMARK 465 HIS A 798
REMARK 465 HIS A 799
REMARK 465 HIS A 800
REMARK 465 HIS A 801
REMARK 465 HIS A 802
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 ASP A 499 CG OD1 OD2
REMARK 470 GLU A 548 CG CD OE1 OE2
REMARK 470 ARG A 559 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 568 CG CD OE1 NE2
REMARK 470 ARG A 686 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 761 CG CD NE CZ NH1 NH2
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 650 48.40 -142.64
REMARK 500 VAL A 683 -167.54 -129.43
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 6UK A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KMI RELATED DB: PDB
REMARK 900 RELATED ID: 5KMJ RELATED DB: PDB
REMARK 900 RELATED ID: 5KMK RELATED DB: PDB
REMARK 900 RELATED ID: 5KML RELATED DB: PDB
REMARK 900 RELATED ID: 5KMM RELATED DB: PDB
REMARK 900 RELATED ID: 5KMO RELATED DB: PDB
DBREF 5KMN A 474 796 UNP P04629 NTRK1_HUMAN 376 698
SEQADV 5KMN ACE A 0 UNP P04629 ACETYLATION
SEQADV 5KMN HIS A 797 UNP P04629 EXPRESSION TAG
SEQADV 5KMN HIS A 798 UNP P04629 EXPRESSION TAG
SEQADV 5KMN HIS A 799 UNP P04629 EXPRESSION TAG
SEQADV 5KMN HIS A 800 UNP P04629 EXPRESSION TAG
SEQADV 5KMN HIS A 801 UNP P04629 EXPRESSION TAG
SEQADV 5KMN HIS A 802 UNP P04629 EXPRESSION TAG
SEQRES 1 A 330 ACE SER SER LEU SER PRO THR GLU GLY LYS GLY SER GLY
SEQRES 2 A 330 LEU GLN GLY HIS ILE ILE GLU ASN PRO GLN TYR PHE SER
SEQRES 3 A 330 ASP ALA CYS VAL HIS HIS ILE LYS ARG ARG ASP ILE VAL
SEQRES 4 A 330 LEU LYS TRP GLU LEU GLY GLU GLY ALA PHE GLY LYS VAL
SEQRES 5 A 330 PHE LEU ALA GLU CYS HIS ASN LEU LEU PRO GLU GLN ASP
SEQRES 6 A 330 LYS MET LEU VAL ALA VAL LYS ALA LEU LYS GLU ALA SER
SEQRES 7 A 330 GLU SER ALA ARG GLN ASP PHE GLN ARG GLU ALA GLU LEU
SEQRES 8 A 330 LEU THR MET LEU GLN HIS GLN HIS ILE VAL ARG PHE PHE
SEQRES 9 A 330 GLY VAL CYS THR GLU GLY ARG PRO LEU LEU MET VAL PHE
SEQRES 10 A 330 GLU TYR MET ARG HIS GLY ASP LEU ASN ARG PHE LEU ARG
SEQRES 11 A 330 SER HIS GLY PRO ASP ALA LYS LEU LEU ALA GLY GLY GLU
SEQRES 12 A 330 ASP VAL ALA PRO GLY PRO LEU GLY LEU GLY GLN LEU LEU
SEQRES 13 A 330 ALA VAL ALA SER GLN VAL ALA ALA GLY MET VAL TYR LEU
SEQRES 14 A 330 ALA GLY LEU HIS PHE VAL HIS ARG ASP LEU ALA THR ARG
SEQRES 15 A 330 ASN CYS LEU VAL GLY GLN GLY LEU VAL VAL LYS ILE GLY
SEQRES 16 A 330 ASP PHE GLY MET SER ARG ASP ILE TYR SER THR ASP TYR
SEQRES 17 A 330 TYR ARG VAL GLY GLY ARG THR MET LEU PRO ILE ARG TRP
SEQRES 18 A 330 MET PRO PRO GLU SER ILE LEU TYR ARG LYS PHE THR THR
SEQRES 19 A 330 GLU SER ASP VAL TRP SER PHE GLY VAL VAL LEU TRP GLU
SEQRES 20 A 330 ILE PHE THR TYR GLY LYS GLN PRO TRP TYR GLN LEU SER
SEQRES 21 A 330 ASN THR GLU ALA ILE ASP CYS ILE THR GLN GLY ARG GLU
SEQRES 22 A 330 LEU GLU ARG PRO ARG ALA CYS PRO PRO GLU VAL TYR ALA
SEQRES 23 A 330 ILE MET ARG GLY CYS TRP GLN ARG GLU PRO GLN GLN ARG
SEQRES 24 A 330 HIS SER ILE LYS ASP VAL HIS ALA ARG LEU GLN ALA LEU
SEQRES 25 A 330 ALA GLN ALA PRO PRO VAL TYR LEU ASP VAL LEU GLY HIS
SEQRES 26 A 330 HIS HIS HIS HIS HIS
HET ACE A 0 3
HET 6UK A 901 28
HETNAM ACE ACETYL GROUP
HETNAM 6UK 1-(2-METHYL-4-PHENYL-PYRIMIDIN-5-YL)-3-[[2-
HETNAM 2 6UK (TRIFLUOROMETHYL)PHENYL]METHYL]UREA
FORMUL 1 ACE C2 H4 O
FORMUL 2 6UK C20 H17 F3 N4 O
FORMUL 3 HOH *88(H2 O)
HELIX 1 AA1 LYS A 506 ARG A 508 5 3
HELIX 2 AA2 GLU A 551 LEU A 567 1 17
HELIX 3 AA3 ASP A 596 HIS A 604 1 9
HELIX 4 AA4 GLY A 623 LEU A 644 1 22
HELIX 5 AA5 ALA A 652 ARG A 654 5 3
HELIX 6 AA6 MET A 671 TYR A 676 1 6
HELIX 7 AA7 SER A 677 TYR A 680 5 4
HELIX 8 AA8 PRO A 690 MET A 694 5 5
HELIX 9 AA9 PRO A 695 ARG A 702 1 8
HELIX 10 AB1 THR A 705 THR A 722 1 18
HELIX 11 AB2 SER A 732 GLY A 743 1 12
HELIX 12 AB3 PRO A 753 TRP A 764 1 12
HELIX 13 AB4 GLU A 767 ARG A 771 5 5
HELIX 14 AB5 SER A 773 GLN A 786 1 14
HELIX 15 AB6 PRO A 788 VAL A 794 1 7
SHEET 1 AA1 2 LEU A 476 PRO A 478 0
SHEET 2 AA1 2 PHE A 646 HIS A 648 -1 O VAL A 647 N SER A 477
SHEET 1 AA2 5 ILE A 510 GLU A 518 0
SHEET 2 AA2 5 GLY A 522 HIS A 530 -1 O LEU A 526 N LYS A 513
SHEET 3 AA2 5 LYS A 538 LEU A 546 -1 O ALA A 545 N LYS A 523
SHEET 4 AA2 5 LEU A 586 GLU A 590 -1 O PHE A 589 N ALA A 542
SHEET 5 AA2 5 PHE A 575 CYS A 579 -1 N GLY A 577 O VAL A 588
SHEET 1 AA3 2 CYS A 656 GLY A 659 0
SHEET 2 AA3 2 VAL A 663 ILE A 666 -1 O LYS A 665 N LEU A 657
SHEET 1 AA4 2 TYR A 681 ARG A 682 0
SHEET 2 AA4 2 MET A 688 LEU A 689 -1 O LEU A 689 N TYR A 681
LINK C ACE A 0 N SER A 474 1555 1555 1.33
CISPEP 1 ARG A 583 PRO A 584 0 -3.01
SITE 1 AC1 12 ACE A 0 SER A 474 SER A 475 LEU A 476
SITE 2 AC1 12 LYS A 544 GLU A 560 LEU A 567 ILE A 572
SITE 3 AC1 12 HIS A 648 ILE A 666 ASP A 668 GLY A 670
CRYST1 52.150 52.150 228.530 90.00 90.00 120.00 P 31 1 2 6
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 0.019175 0.011071 0.000000 0.00000
SCALE2 0.000000 0.022142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004376 0.00000
HETATM 1 C ACE A 0 -18.712 -4.237 -27.849 1.00 32.51 C
HETATM 2 O ACE A 0 -18.658 -4.900 -28.883 1.00 33.59 O
HETATM 3 CH3 ACE A 0 -19.490 -4.757 -26.638 1.00 33.13 C
(ATOM LINES ARE NOT SHOWN.)
END