HEADER TRANSFERASE/TRANSFERASE INHIBITOR 11-AUG-16 5SYS
TITLE C-SRC V281C BOUND TO N-[3-({6-[(1E)-2-CYANO-3-(METHYLAMINO)-3-OXOPROP-
TITLE 2 1-EN-1-YL]-7-(2-METHOXYETHYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-5-
TITLE 3 YL}ETHYNYL)-4-METHYLPHENYL]-3-(TRIFLUOROMETHYL)BENZAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTO-ONCOGENE C-SRC,PP60C-SRC,P60-SRC;
COMPND 5 EC: 2.7.10.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: SRC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DFG-OUT, COVALENTLY-LINKED INIHIBITOR, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.DIETER,E.A.MERRITT,D.J.MALY
REVDAT 5 04-OCT-23 5SYS 1 REMARK
REVDAT 4 25-DEC-19 5SYS 1 REMARK
REVDAT 3 27-FEB-19 5SYS 1 JRNL
REVDAT 2 17-JAN-18 5SYS 1 REMARK
REVDAT 1 16-AUG-17 5SYS 0
JRNL AUTH A.C.REGISTER,D.J.MALY
JRNL TITL A COMBINED APPROACH REVEALS A REGULATORY MECHANISM COUPLING
JRNL TITL 2 SRC'S KINASE ACTIVITY, LOCALIZATION, AND
JRNL TITL 3 PHOSPHOTRANSFERASE-INDEPENDENT FUNCTIONS
JRNL REF MOL.CELL V.2019
JRNL REFN ISSN 1097-2765
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 15434
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) : 0.288
REMARK 3 R VALUE (WORKING SET) : 0.286
REMARK 3 FREE R VALUE : 0.334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 827
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1050
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3900
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.61000
REMARK 3 B22 (A**2) : -2.41000
REMARK 3 B33 (A**2) : 3.25000
REMARK 3 B12 (A**2) : 0.24000
REMARK 3 B13 (A**2) : -0.06000
REMARK 3 B23 (A**2) : 1.23000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.527
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.544
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.468
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.819
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.792
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4342 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4084 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5886 ; 1.423 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9416 ; 0.965 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 516 ; 7.117 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 192 ;38.574 ;23.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 742 ;16.381 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;15.435 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 622 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5100 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 974 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2066 ; 3.853 ; 6.466
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2067 ; 3.852 ; 6.466
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2574 ; 6.592 ; 9.681
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 258 533 B 258 533 16560 0.050 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5SYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223295.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-16
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 : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16285
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 73.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 1.33400
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: 3UQG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6, 8% PEG 3350, 10 MM
REMARK 280 NAOAC, 14% GLYCEROL, 10 MM DTT, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLY A 248
REMARK 465 HIS A 249
REMARK 465 MET A 250
REMARK 465 GLN A 251
REMARK 465 THR A 252
REMARK 465 GLN A 253
REMARK 465 GLY A 254
REMARK 465 LEU A 255
REMARK 465 ALA A 256
REMARK 465 LYS A 257
REMARK 465 LEU A 407
REMARK 465 ALA A 408
REMARK 465 ARG A 409
REMARK 465 LEU A 410
REMARK 465 ILE A 411
REMARK 465 GLU A 412
REMARK 465 ASP A 413
REMARK 465 ASN A 414
REMARK 465 GLU A 415
REMARK 465 TYR A 416
REMARK 465 THR A 417
REMARK 465 ALA A 418
REMARK 465 ARG A 419
REMARK 465 GLN A 420
REMARK 465 GLY A 421
REMARK 465 ALA A 422
REMARK 465 LYS A 423
REMARK 465 PHE A 424
REMARK 465 GLY B 248
REMARK 465 HIS B 249
REMARK 465 MET B 250
REMARK 465 GLN B 251
REMARK 465 THR B 252
REMARK 465 GLN B 253
REMARK 465 GLY B 254
REMARK 465 LEU B 255
REMARK 465 ALA B 256
REMARK 465 LYS B 257
REMARK 465 LEU B 407
REMARK 465 ALA B 408
REMARK 465 ARG B 409
REMARK 465 LEU B 410
REMARK 465 ILE B 411
REMARK 465 GLU B 412
REMARK 465 ASP B 413
REMARK 465 ASN B 414
REMARK 465 GLU B 415
REMARK 465 TYR B 416
REMARK 465 THR B 417
REMARK 465 ALA B 418
REMARK 465 ARG B 419
REMARK 465 GLN B 420
REMARK 465 GLY B 421
REMARK 465 ALA B 422
REMARK 465 LYS B 423
REMARK 465 PHE B 424
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 GLU A 305 CG CD OE1 OE2
REMARK 470 ARG A 469 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 305 CG CD OE1 OE2
REMARK 470 ARG B 469 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 353 O HOH B 701 2.17
REMARK 500 O PHE B 515 O HOH B 702 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 261 156.32 -44.00
REMARK 500 GLU A 270 -75.25 -59.51
REMARK 500 LEU A 273 -50.78 -131.59
REMARK 500 ASP A 386 43.48 -170.90
REMARK 500 ASP A 404 115.62 -168.38
REMARK 500 LEU A 435 -74.42 -84.68
REMARK 500 TYR A 463 71.04 60.28
REMARK 500 GLU A 486 16.15 44.31
REMARK 500 TYR A 527 126.20 -30.61
REMARK 500 GLU B 261 156.68 -44.55
REMARK 500 GLU B 270 -74.91 -59.12
REMARK 500 LEU B 273 -50.62 -130.63
REMARK 500 GLN B 275 -159.85 -95.36
REMARK 500 ASP B 386 42.97 -171.45
REMARK 500 ASP B 404 115.77 -166.31
REMARK 500 LEU B 435 -73.87 -84.89
REMARK 500 TYR B 463 70.99 60.75
REMARK 500 ASN B 468 -39.09 -38.81
REMARK 500 GLU B 486 12.33 48.60
REMARK 500 TRP B 499 40.06 -105.76
REMARK 500 TYR B 527 126.53 -31.29
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 72F A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 72F B 600 and CYS B
REMARK 800 281
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5SWH RELATED DB: PDB
DBREF 5SYS A 251 533 UNP P00523 SRC_CHICK 251 533
DBREF 5SYS B 251 533 UNP P00523 SRC_CHICK 251 533
SEQADV 5SYS GLY A 248 UNP P00523 EXPRESSION TAG
SEQADV 5SYS HIS A 249 UNP P00523 EXPRESSION TAG
SEQADV 5SYS MET A 250 UNP P00523 EXPRESSION TAG
SEQADV 5SYS CYS A 281 UNP P00523 VAL 281 ENGINEERED MUTATION
SEQADV 5SYS GLY B 248 UNP P00523 EXPRESSION TAG
SEQADV 5SYS HIS B 249 UNP P00523 EXPRESSION TAG
SEQADV 5SYS MET B 250 UNP P00523 EXPRESSION TAG
SEQADV 5SYS CYS B 281 UNP P00523 VAL 281 ENGINEERED MUTATION
SEQRES 1 A 286 GLY HIS MET GLN THR GLN GLY LEU ALA LYS ASP ALA TRP
SEQRES 2 A 286 GLU ILE PRO ARG GLU SER LEU ARG LEU GLU VAL LYS LEU
SEQRES 3 A 286 GLY GLN GLY CYS PHE GLY GLU CYS TRP MET GLY THR TRP
SEQRES 4 A 286 ASN GLY THR THR ARG VAL ALA ILE LYS THR LEU LYS PRO
SEQRES 5 A 286 GLY THR MET SER PRO GLU ALA PHE LEU GLN GLU ALA GLN
SEQRES 6 A 286 VAL MET LYS LYS LEU ARG HIS GLU LYS LEU VAL GLN LEU
SEQRES 7 A 286 TYR ALA VAL VAL SER GLU GLU PRO ILE TYR ILE VAL THR
SEQRES 8 A 286 GLU TYR MET SER LYS GLY SER LEU LEU ASP PHE LEU LYS
SEQRES 9 A 286 GLY GLU MET GLY LYS TYR LEU ARG LEU PRO GLN LEU VAL
SEQRES 10 A 286 ASP MET ALA ALA GLN ILE ALA SER GLY MET ALA TYR VAL
SEQRES 11 A 286 GLU ARG MET ASN TYR VAL HIS ARG ASP LEU ARG ALA ALA
SEQRES 12 A 286 ASN ILE LEU VAL GLY GLU ASN LEU VAL CYS LYS VAL ALA
SEQRES 13 A 286 ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR
SEQRES 14 A 286 THR ALA ARG GLN GLY ALA LYS PHE PRO ILE LYS TRP THR
SEQRES 15 A 286 ALA PRO GLU ALA ALA LEU TYR GLY ARG PHE THR ILE LYS
SEQRES 16 A 286 SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU LEU
SEQRES 17 A 286 THR THR LYS GLY ARG VAL PRO TYR PRO GLY MET VAL ASN
SEQRES 18 A 286 ARG GLU VAL LEU ASP GLN VAL GLU ARG GLY TYR ARG MET
SEQRES 19 A 286 PRO CYS PRO PRO GLU CYS PRO GLU SER LEU HIS ASP LEU
SEQRES 20 A 286 MET CYS GLN CYS TRP ARG LYS ASP PRO GLU GLU ARG PRO
SEQRES 21 A 286 THR PHE GLU TYR LEU GLN ALA PHE LEU GLU ASP TYR PHE
SEQRES 22 A 286 THR SER THR GLU PRO GLN TYR GLN PRO GLY GLU ASN LEU
SEQRES 1 B 286 GLY HIS MET GLN THR GLN GLY LEU ALA LYS ASP ALA TRP
SEQRES 2 B 286 GLU ILE PRO ARG GLU SER LEU ARG LEU GLU VAL LYS LEU
SEQRES 3 B 286 GLY GLN GLY CYS PHE GLY GLU CYS TRP MET GLY THR TRP
SEQRES 4 B 286 ASN GLY THR THR ARG VAL ALA ILE LYS THR LEU LYS PRO
SEQRES 5 B 286 GLY THR MET SER PRO GLU ALA PHE LEU GLN GLU ALA GLN
SEQRES 6 B 286 VAL MET LYS LYS LEU ARG HIS GLU LYS LEU VAL GLN LEU
SEQRES 7 B 286 TYR ALA VAL VAL SER GLU GLU PRO ILE TYR ILE VAL THR
SEQRES 8 B 286 GLU TYR MET SER LYS GLY SER LEU LEU ASP PHE LEU LYS
SEQRES 9 B 286 GLY GLU MET GLY LYS TYR LEU ARG LEU PRO GLN LEU VAL
SEQRES 10 B 286 ASP MET ALA ALA GLN ILE ALA SER GLY MET ALA TYR VAL
SEQRES 11 B 286 GLU ARG MET ASN TYR VAL HIS ARG ASP LEU ARG ALA ALA
SEQRES 12 B 286 ASN ILE LEU VAL GLY GLU ASN LEU VAL CYS LYS VAL ALA
SEQRES 13 B 286 ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR
SEQRES 14 B 286 THR ALA ARG GLN GLY ALA LYS PHE PRO ILE LYS TRP THR
SEQRES 15 B 286 ALA PRO GLU ALA ALA LEU TYR GLY ARG PHE THR ILE LYS
SEQRES 16 B 286 SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU LEU
SEQRES 17 B 286 THR THR LYS GLY ARG VAL PRO TYR PRO GLY MET VAL ASN
SEQRES 18 B 286 ARG GLU VAL LEU ASP GLN VAL GLU ARG GLY TYR ARG MET
SEQRES 19 B 286 PRO CYS PRO PRO GLU CYS PRO GLU SER LEU HIS ASP LEU
SEQRES 20 B 286 MET CYS GLN CYS TRP ARG LYS ASP PRO GLU GLU ARG PRO
SEQRES 21 B 286 THR PHE GLU TYR LEU GLN ALA PHE LEU GLU ASP TYR PHE
SEQRES 22 B 286 THR SER THR GLU PRO GLN TYR GLN PRO GLY GLU ASN LEU
HET 72F A 600 43
HET 72F B 600 43
HETNAM 72F N-[3-({6-[(2S)-2-CYANO-3-(METHYLAMINO)-3-OXOPROPYL]-7-
HETNAM 2 72F (2-METHOXYETHYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-5-
HETNAM 3 72F YL}ETHYNYL)-4-METHYLPHENYL]-3-(TRIFLUOROMETHYL)
HETNAM 4 72F BENZAMIDE
HETSYN 72F N-[3-({6-[(1E)-2-CYANO-3-(METHYLAMINO)-3-OXOPROP-1-EN-
HETSYN 2 72F 1-YL]-7-(2-METHOXYETHYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-5-
HETSYN 3 72F YL}ETHYNYL)-4-METHYLPHENYL]-3-(TRIFLUOROMETHYL)
HETSYN 4 72F BENZAMIDE INHIBITOR, BOUND FORM
FORMUL 3 72F 2(C31 H27 F3 N6 O3)
FORMUL 5 HOH *67(H2 O)
HELIX 1 AA1 PRO A 263 GLU A 265 5 3
HELIX 2 AA2 SER A 303 LEU A 308 1 6
HELIX 3 AA3 LEU A 308 LYS A 316 1 9
HELIX 4 AA4 SER A 345 GLY A 352 1 8
HELIX 5 AA5 GLU A 353 LYS A 356 5 4
HELIX 6 AA6 ARG A 359 MET A 380 1 22
HELIX 7 AA7 ARG A 388 ALA A 390 5 3
HELIX 8 AA8 GLU A 396 LEU A 398 5 3
HELIX 9 AA9 PRO A 425 THR A 429 5 5
HELIX 10 AB1 ALA A 430 GLY A 437 1 8
HELIX 11 AB2 THR A 440 THR A 456 1 17
HELIX 12 AB3 VAL A 467 GLY A 478 1 12
HELIX 13 AB4 PRO A 488 TRP A 499 1 12
HELIX 14 AB5 ASP A 502 ARG A 506 5 5
HELIX 15 AB6 THR A 508 THR A 523 1 16
HELIX 16 AB7 PRO B 263 GLU B 265 5 3
HELIX 17 AB8 SER B 303 LEU B 308 1 6
HELIX 18 AB9 LEU B 308 LYS B 316 1 9
HELIX 19 AC1 SER B 345 GLY B 352 1 8
HELIX 20 AC2 GLU B 353 LYS B 356 5 4
HELIX 21 AC3 ARG B 359 MET B 380 1 22
HELIX 22 AC4 ARG B 388 ALA B 390 5 3
HELIX 23 AC5 GLU B 396 LEU B 398 5 3
HELIX 24 AC6 PRO B 425 THR B 429 5 5
HELIX 25 AC7 ALA B 430 GLY B 437 1 8
HELIX 26 AC8 THR B 440 THR B 456 1 17
HELIX 27 AC9 VAL B 467 GLY B 478 1 12
HELIX 28 AD1 PRO B 488 TRP B 499 1 12
HELIX 29 AD2 ASP B 502 ARG B 506 5 5
HELIX 30 AD3 THR B 508 THR B 523 1 16
SHEET 1 AA1 5 LEU A 267 GLY A 274 0
SHEET 2 AA1 5 CYS A 281 TRP A 286 -1 O THR A 285 N ARG A 268
SHEET 3 AA1 5 ARG A 291 THR A 296 -1 O VAL A 292 N GLY A 284
SHEET 4 AA1 5 TYR A 335 GLU A 339 -1 O ILE A 336 N LYS A 295
SHEET 5 AA1 5 LEU A 325 VAL A 329 -1 N TYR A 326 O VAL A 337
SHEET 1 AA2 2 ILE A 392 VAL A 394 0
SHEET 2 AA2 2 CYS A 400 VAL A 402 -1 O LYS A 401 N LEU A 393
SHEET 1 AA3 5 LEU B 267 GLY B 274 0
SHEET 2 AA3 5 CYS B 281 TRP B 286 -1 O THR B 285 N ARG B 268
SHEET 3 AA3 5 ARG B 291 THR B 296 -1 O VAL B 292 N GLY B 284
SHEET 4 AA3 5 TYR B 335 GLU B 339 -1 O ILE B 336 N LYS B 295
SHEET 5 AA3 5 LEU B 325 VAL B 329 -1 N TYR B 326 O VAL B 337
SHEET 1 AA4 2 ILE B 392 VAL B 394 0
SHEET 2 AA4 2 CYS B 400 VAL B 402 -1 O LYS B 401 N LEU B 393
LINK SG CYS A 281 C26 72F A 600 1555 1555 1.82
LINK SG CYS B 281 C26 72F B 600 1555 1555 1.84
CISPEP 1 GLU A 332 PRO A 333 0 -2.12
CISPEP 2 GLU B 332 PRO B 333 0 -2.09
SITE 1 AC1 17 CYS A 281 ALA A 293 ILE A 294 LYS A 295
SITE 2 AC1 17 GLU A 310 MET A 314 LEU A 317 LEU A 322
SITE 3 AC1 17 ILE A 336 TYR A 340 MET A 341 HIS A 384
SITE 4 AC1 17 VAL A 402 ALA A 403 ASP A 404 PHE A 405
SITE 5 AC1 17 HOH A 716
SITE 1 AC2 16 LEU B 273 GLY B 274 GLU B 280 TRP B 282
SITE 2 AC2 16 ALA B 293 ILE B 294 LYS B 295 GLU B 310
SITE 3 AC2 16 MET B 314 THR B 338 TYR B 340 MET B 341
SITE 4 AC2 16 VAL B 402 ALA B 403 ASP B 404 PHE B 405
CRYST1 41.813 63.857 75.625 77.87 90.10 89.83 P 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 0.023916 -0.000069 0.000055 0.00000
SCALE2 0.000000 0.015660 -0.003366 0.00000
SCALE3 0.000000 0.000000 0.013525 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
