HEADER TRANSFERASE 24-AUG-17 5OUL
TITLE THE CRYSTAL STRUCTURE OF CK2ALPHA IN COMPLEX WITH COMPOUND 9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-329;
COMPND 5 SYNONYM: CK II ALPHA;
COMPND 6 EC: 2.7.11.1;
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: CSNK2A1, CK2A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHAT2
KEYWDS CK2ALPHA, CK2A, FRAGMENT BASED DRUG DISCOVERY, HIGH CONCENTRATION
KEYWDS 2 SCREENING, SELECTIVE ATP COMPETITIVE INHIBITORS, SURFACE ENTROPHY
KEYWDS 3 REDUCTION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BREAR,C.DE FUSCO,J.IEGRE,M.YOSHIDA,S.MITCHELL,M.ROSSMANN,L.CARRO,
AUTHOR 2 H.SORE,M.HYVONEN,D.SPRING
REVDAT 3 17-JAN-24 5OUL 1 REMARK
REVDAT 2 16-MAY-18 5OUL 1 JRNL
REVDAT 1 28-FEB-18 5OUL 0
JRNL AUTH J.IEGRE,P.BREAR,C.DE FUSCO,M.YOSHIDA,S.L.MITCHELL,
JRNL AUTH 2 M.ROSSMANN,L.CARRO,H.F.SORE,M.HYVONEN,D.R.SPRING
JRNL TITL SECOND-GENERATION CK2 ALPHA INHIBITORS TARGETING THE ALPHA D
JRNL TITL 2 POCKET.
JRNL REF CHEM SCI V. 9 3041 2018
JRNL REFN ISSN 2041-6520
JRNL PMID 29732088
JRNL DOI 10.1039/C7SC05122K
REMARK 2
REMARK 2 RESOLUTION. 1.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.1
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) : 1.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 68905
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3479
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.34
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.73
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4940
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3051
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4681
REMARK 3 BIN R VALUE (WORKING SET) : 0.3054
REMARK 3 BIN FREE R VALUE : 0.2988
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.24
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 259
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 : 2748
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.32170
REMARK 3 B22 (A**2) : -1.21270
REMARK 3 B33 (A**2) : -0.10910
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09090
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.202
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.064
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.064
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.063
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.064
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 : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3037 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4123 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1037 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 72 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 561 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3037 ; 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 : 352 ; 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 : 3691 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.95
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.51
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.87
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 5OUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-16
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
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 : AIMLESS 0.5.17, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69349
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
REMARK 200 RESOLUTION RANGE LOW (A) : 58.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.90900
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: PHASER
REMARK 200 STARTING MODEL: 5CVH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 112.5MM MES PH 6.5, 35% GLYCEROL
REMARK 280 ETHOXYLATE, 180 MM AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 23.04000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 SER A 2
REMARK 465 ARG A 330
REMARK 465 GLU A 331
REMARK 465 ALA A 332
REMARK 465 MET A 333
REMARK 465 GLU A 334
REMARK 465 HIS A 335
REMARK 465 PRO A 336
REMARK 465 TYR A 337
REMARK 465 PHE A 338
REMARK 465 TYR A 339
REMARK 465 THR A 340
REMARK 465 VAL A 341
REMARK 465 VAL A 342
REMARK 465 LYS A 343
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 ASN A 61 3.55 -153.94
REMARK 500 ASP A 156 43.55 -148.05
REMARK 500 ASP A 175 76.87 54.64
REMARK 500 ALA A 193 157.13 63.15
REMARK 500 ALA A 193 157.13 63.15
REMARK 500 MET A 208 54.74 -92.54
REMARK 500 ASP A 210 -159.20 -149.51
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 ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AWE A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AWE A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AWE A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AWE A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AWE A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AWE A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TFA A 409
DBREF 5OUL A 2 329 UNP P68400 CSK21_HUMAN 2 329
SEQADV 5OUL SER A 21 UNP P68400 ARG 21 ENGINEERED MUTATION
SEQADV 5OUL ALA A 74 UNP P68400 LYS 74 ENGINEERED MUTATION
SEQADV 5OUL ALA A 75 UNP P68400 LYS 75 ENGINEERED MUTATION
SEQADV 5OUL ALA A 76 UNP P68400 LYS 76 ENGINEERED MUTATION
SEQADV 5OUL ARG A 330 UNP P68400 EXPRESSION TAG
SEQADV 5OUL GLU A 331 UNP P68400 EXPRESSION TAG
SEQADV 5OUL ALA A 332 UNP P68400 EXPRESSION TAG
SEQADV 5OUL MET A 333 UNP P68400 EXPRESSION TAG
SEQADV 5OUL GLU A 334 UNP P68400 EXPRESSION TAG
SEQADV 5OUL HIS A 335 UNP P68400 EXPRESSION TAG
SEQADV 5OUL PRO A 336 UNP P68400 EXPRESSION TAG
SEQADV 5OUL TYR A 337 UNP P68400 EXPRESSION TAG
SEQADV 5OUL PHE A 338 UNP P68400 EXPRESSION TAG
SEQADV 5OUL TYR A 339 UNP P68400 EXPRESSION TAG
SEQADV 5OUL THR A 340 UNP P68400 EXPRESSION TAG
SEQADV 5OUL VAL A 341 UNP P68400 EXPRESSION TAG
SEQADV 5OUL VAL A 342 UNP P68400 EXPRESSION TAG
SEQADV 5OUL LYS A 343 UNP P68400 EXPRESSION TAG
SEQRES 1 A 342 SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR ASP
SEQRES 2 A 342 VAL ASN THR HIS ARG PRO SER GLU TYR TRP ASP TYR GLU
SEQRES 3 A 342 SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR GLN
SEQRES 4 A 342 LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU VAL
SEQRES 5 A 342 PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL VAL
SEQRES 6 A 342 VAL LYS ILE LEU LYS PRO VAL ALA ALA ALA LYS ILE LYS
SEQRES 7 A 342 ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY PRO
SEQRES 8 A 342 ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO VAL
SEQRES 9 A 342 SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN ASN
SEQRES 10 A 342 THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP TYR
SEQRES 11 A 342 ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA LEU
SEQRES 12 A 342 ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP VAL
SEQRES 13 A 342 LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG LYS
SEQRES 14 A 342 LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR HIS
SEQRES 15 A 342 PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG TYR
SEQRES 16 A 342 PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET TYR
SEQRES 17 A 342 ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET LEU
SEQRES 18 A 342 ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS GLY
SEQRES 19 A 342 HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS VAL
SEQRES 20 A 342 LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS TYR
SEQRES 21 A 342 ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU GLY
SEQRES 22 A 342 ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SER
SEQRES 23 A 342 GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP PHE
SEQRES 24 A 342 LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG LEU
SEQRES 25 A 342 THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR THR
SEQRES 26 A 342 VAL VAL LYS ARG GLU ALA MET GLU HIS PRO TYR PHE TYR
SEQRES 27 A 342 THR VAL VAL LYS
HET ACT A 401 4
HET ACT A 402 4
HET AWE A 403 32
HET AWE A 404 32
HET AWE A 405 16
HET AWE A 406 16
HET AWE A 407 16
HET AWE A 408 16
HET TFA A 409 7
HETNAM ACT ACETATE ION
HETNAM AWE [3-CHLORANYL-4-(3-FLUOROPHENYL)PHENYL]METHANAMINE
HETNAM TFA TRIFLUOROACETIC ACID
FORMUL 2 ACT 2(C2 H3 O2 1-)
FORMUL 4 AWE 6(C13 H11 CL F N)
FORMUL 10 TFA C2 H F3 O2
FORMUL 11 HOH *250(H2 O)
HELIX 1 AA1 ASP A 14 ARG A 19 1 6
HELIX 2 AA2 PRO A 20 ASP A 25 1 6
HELIX 3 AA3 TYR A 26 HIS A 29 5 4
HELIX 4 AA4 ASN A 35 ASP A 37 5 3
HELIX 5 AA5 LYS A 71 LYS A 77 1 7
HELIX 6 AA6 LYS A 77 ARG A 89 1 13
HELIX 7 AA7 ASP A 120 LEU A 128 1 9
HELIX 8 AA8 THR A 129 MET A 150 1 22
HELIX 9 AA9 LYS A 158 HIS A 160 5 3
HELIX 10 AB1 ASP A 175 ALA A 179 5 5
HELIX 11 AB2 SER A 194 LYS A 198 5 5
HELIX 12 AB3 GLY A 199 VAL A 204 1 6
HELIX 13 AB4 TYR A 211 ARG A 228 1 18
HELIX 14 AB5 ASP A 237 GLY A 250 1 14
HELIX 15 AB6 GLY A 250 TYR A 261 1 12
HELIX 16 AB7 ASP A 266 ILE A 272 5 7
HELIX 17 AB8 ARG A 280 VAL A 285 5 6
HELIX 18 AB9 ASN A 289 VAL A 293 5 5
HELIX 19 AC1 SER A 294 LEU A 305 1 12
HELIX 20 AC2 ASP A 308 ARG A 312 5 5
HELIX 21 AC3 THR A 314 GLU A 320 1 7
HELIX 22 AC4 HIS A 321 TYR A 325 5 5
SHEET 1 AA1 5 TYR A 39 ARG A 47 0
SHEET 2 AA1 5 SER A 51 ASN A 58 -1 O VAL A 53 N GLY A 46
SHEET 3 AA1 5 LYS A 64 LEU A 70 -1 O ILE A 69 N GLU A 52
SHEET 4 AA1 5 PRO A 109 GLU A 114 -1 O PHE A 113 N VAL A 66
SHEET 5 AA1 5 LEU A 97 LYS A 102 -1 N VAL A 101 O ALA A 110
SHEET 1 AA2 2 ILE A 152 MET A 153 0
SHEET 2 AA2 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153
SHEET 1 AA3 2 VAL A 162 ASP A 165 0
SHEET 2 AA3 2 LYS A 170 LEU A 173 -1 O ARG A 172 N MET A 163
CISPEP 1 GLU A 230 PRO A 231 0 -6.81
SITE 1 AC1 4 ASP A 103 ARG A 280 HOH A 507 HOH A 566
SITE 1 AC2 3 ARG A 80 ARG A 155 LEU A 178
SITE 1 AC3 13 PHE A 121 LEU A 124 ILE A 133 TYR A 136
SITE 2 AC3 13 MET A 137 PRO A 159 VAL A 162 ILE A 164
SITE 3 AC3 13 MET A 221 LEU A 222 MET A 225 HOH A 509
SITE 4 AC3 13 HOH A 527
SITE 1 AC4 8 GLN A 40 VAL A 285 GLN A 290 VAL A 293
SITE 2 AC4 8 SER A 294 PRO A 295 LEU A 298 AWE A 405
SITE 1 AC5 4 GLU A 282 ARG A 283 VAL A 285 AWE A 404
SITE 1 AC6 7 GLU A 52 ILE A 69 LYS A 71 PRO A 72
SITE 2 AC6 7 ASP A 103 SER A 106 ARG A 280
SITE 1 AC7 4 VAL A 116 ASN A 118 MET A 163 TFA A 409
SITE 1 AC8 5 HIS A 160 ASN A 161 MET A 163 ILE A 174
SITE 2 AC8 5 HOH A 509
SITE 1 AC9 6 LYS A 68 PHE A 113 ILE A 174 ASP A 175
SITE 2 AC9 6 AWE A 407 HOH A 597
CRYST1 58.703 46.080 63.369 90.00 112.39 90.00 P 1 21 1 2
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 0.017035 0.000000 0.007018 0.00000
SCALE2 0.000000 0.021701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017067 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
