HEADER TRANSFERASE 07-JUN-18 6A1G
TITLE CRYSTAL STRUCTURE OF HUMAN DYRK1A IN COMPLEX WITH COMPOUND 32
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY TYROSINE-PHOSPHORYLATION-REGULATED KINASE
COMPND 3 1A;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: DUAL SPECIFICITY YAK1-RELATED KINASE,HP86,PROTEIN KINASE
COMPND 6 MINIBRAIN HOMOLOG,HMNB;
COMPND 7 EC: 2.7.12.1;
COMPND 8 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: DYRK1A, DYRK, MNB, MNBH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS DYRK1A, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BABA,H.HANZAWA
REVDAT 3 22-NOV-23 6A1G 1 REMARK
REVDAT 2 24-OCT-18 6A1G 1 JRNL
REVDAT 1 03-OCT-18 6A1G 0
JRNL AUTH T.FUKUDA,T.ISHIYAMA,T.KATAGIRI,K.UEDA,S.MURAMATSU,
JRNL AUTH 2 M.HASHIMOTO,A.AKI,D.BABA,K.WATANABE,N.TANAKA
JRNL TITL DISCOVERY OF DS42450411 AS A POTENT ORALLY ACTIVE HEPCIDIN
JRNL TITL 2 PRODUCTION INHIBITOR: DESIGN AND OPTIMIZATION OF NOVEL
JRNL TITL 3 4-AMINOPYRIMIDINE DERIVATIVES.
JRNL REF BIOORG. MED. CHEM. LETT. V. 28 3333 2018
JRNL REFN ESSN 1464-3405
JRNL PMID 30217414
JRNL DOI 10.1016/J.BMCL.2018.09.010
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 40680
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2097
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2850
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.4180
REMARK 3 BIN FREE R VALUE SET COUNT : 182
REMARK 3 BIN FREE R VALUE : 0.4360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5534
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.11000
REMARK 3 B22 (A**2) : 6.90000
REMARK 3 B33 (A**2) : -3.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.06000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.279
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.224
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.206
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.655
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5720 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7727 ; 1.413 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 671 ; 6.035 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 273 ;35.901 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1026 ;15.583 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;22.766 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 814 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4372 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 135 480 B 135 480 432 0.09 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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: NULL
REMARK 4
REMARK 4 6A1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1300008012.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-14
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42803
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.010
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: 2VX3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V POLYETHYLENE GLYCOL MONOMETHYL
REMARK 280 ETHER 2000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 34.68250
REMARK 290 SMTRY3 2 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 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 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 124
REMARK 465 PRO A 125
REMARK 465 MET A 126
REMARK 465 SER A 127
REMARK 465 SER A 128
REMARK 465 HIS A 129
REMARK 465 LYS A 130
REMARK 465 LYS A 131
REMARK 465 GLU A 132
REMARK 465 ARG A 133
REMARK 465 PRO A 298
REMARK 465 LYS A 299
REMARK 465 LYS A 407
REMARK 465 THR A 408
REMARK 465 LYS A 409
REMARK 465 ASP A 410
REMARK 465 GLY A 411
REMARK 465 LYS A 412
REMARK 465 ARG A 413
REMARK 465 LYS A 481
REMARK 465 THR A 482
REMARK 465 ALA A 483
REMARK 465 GLY B 124
REMARK 465 PRO B 125
REMARK 465 MET B 126
REMARK 465 SER B 127
REMARK 465 SER B 128
REMARK 465 HIS B 129
REMARK 465 LYS B 130
REMARK 465 LYS B 131
REMARK 465 GLU B 132
REMARK 465 ARG B 133
REMARK 465 LYS B 134
REMARK 465 LYS B 407
REMARK 465 THR B 408
REMARK 465 LYS B 409
REMARK 465 ASP B 410
REMARK 465 GLY B 411
REMARK 465 LYS B 412
REMARK 465 ARG B 413
REMARK 465 GLU B 414
REMARK 465 LYS B 481
REMARK 465 THR B 482
REMARK 465 ALA B 483
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 134 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 345 CE2 TRP A 345 CD2 0.078
REMARK 500 TRP B 345 CE2 TRP B 345 CD2 0.074
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 ARG A 158 -54.70 -124.94
REMARK 500 SER A 242 -153.22 -99.96
REMARK 500 LEU A 281 -65.11 -104.28
REMARK 500 CYS A 286 1.79 82.78
REMARK 500 ASP A 287 52.34 -158.99
REMARK 500 ASP A 307 74.46 62.52
REMARK 500 GLN A 323 148.51 76.44
REMARK 500 ASP A 339 -149.30 -138.79
REMARK 500 ARG B 158 -55.29 -133.28
REMARK 500 SER B 242 -156.64 -94.34
REMARK 500 CYS B 286 -3.90 83.60
REMARK 500 ASP B 287 57.70 -155.87
REMARK 500 ASP B 307 71.51 65.77
REMARK 500 ARG B 317 -177.06 156.08
REMARK 500 GLN B 323 145.62 74.32
REMARK 500 ASP B 339 -150.74 -144.59
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 9OL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9OL B 801
DBREF 6A1G A 127 483 UNP Q13627 DYR1A_HUMAN 127 483
DBREF 6A1G B 127 483 UNP Q13627 DYR1A_HUMAN 127 483
SEQADV 6A1G GLY A 124 UNP Q13627 EXPRESSION TAG
SEQADV 6A1G PRO A 125 UNP Q13627 EXPRESSION TAG
SEQADV 6A1G MET A 126 UNP Q13627 EXPRESSION TAG
SEQADV 6A1G GLY B 124 UNP Q13627 EXPRESSION TAG
SEQADV 6A1G PRO B 125 UNP Q13627 EXPRESSION TAG
SEQADV 6A1G MET B 126 UNP Q13627 EXPRESSION TAG
SEQRES 1 A 360 GLY PRO MET SER SER HIS LYS LYS GLU ARG LYS VAL TYR
SEQRES 2 A 360 ASN ASP GLY TYR ASP ASP ASP ASN TYR ASP TYR ILE VAL
SEQRES 3 A 360 LYS ASN GLY GLU LYS TRP MET ASP ARG TYR GLU ILE ASP
SEQRES 4 A 360 SER LEU ILE GLY LYS GLY SER PHE GLY GLN VAL VAL LYS
SEQRES 5 A 360 ALA TYR ASP ARG VAL GLU GLN GLU TRP VAL ALA ILE LYS
SEQRES 6 A 360 ILE ILE LYS ASN LYS LYS ALA PHE LEU ASN GLN ALA GLN
SEQRES 7 A 360 ILE GLU VAL ARG LEU LEU GLU LEU MET ASN LYS HIS ASP
SEQRES 8 A 360 THR GLU MET LYS TYR TYR ILE VAL HIS LEU LYS ARG HIS
SEQRES 9 A 360 PHE MET PHE ARG ASN HIS LEU CYS LEU VAL PHE GLU MET
SEQRES 10 A 360 LEU SER TYR ASN LEU TYR ASP LEU LEU ARG ASN THR ASN
SEQRES 11 A 360 PHE ARG GLY VAL SER LEU ASN LEU THR ARG LYS PHE ALA
SEQRES 12 A 360 GLN GLN MET CYS THR ALA LEU LEU PHE LEU ALA THR PRO
SEQRES 13 A 360 GLU LEU SER ILE ILE HIS CYS ASP LEU LYS PRO GLU ASN
SEQRES 14 A 360 ILE LEU LEU CYS ASN PRO LYS ARG SER ALA ILE LYS ILE
SEQRES 15 A 360 VAL ASP PHE GLY SER SER CYS GLN LEU GLY GLN ARG ILE
SEQRES 16 A 360 TYR GLN PTR ILE GLN SER ARG PHE TYR ARG SER PRO GLU
SEQRES 17 A 360 VAL LEU LEU GLY MET PRO TYR ASP LEU ALA ILE ASP MET
SEQRES 18 A 360 TRP SER LEU GLY CYS ILE LEU VAL GLU MET HIS THR GLY
SEQRES 19 A 360 GLU PRO LEU PHE SER GLY ALA ASN GLU VAL ASP GLN MET
SEQRES 20 A 360 ASN LYS ILE VAL GLU VAL LEU GLY ILE PRO PRO ALA HIS
SEQRES 21 A 360 ILE LEU ASP GLN ALA PRO LYS ALA ARG LYS PHE PHE GLU
SEQRES 22 A 360 LYS LEU PRO ASP GLY THR TRP ASN LEU LYS LYS THR LYS
SEQRES 23 A 360 ASP GLY LYS ARG GLU TYR LYS PRO PRO GLY THR ARG LYS
SEQRES 24 A 360 LEU HIS ASN ILE LEU GLY VAL GLU THR GLY GLY PRO GLY
SEQRES 25 A 360 GLY ARG ARG ALA GLY GLU SER GLY HIS THR VAL ALA ASP
SEQRES 26 A 360 TYR LEU LYS PHE LYS ASP LEU ILE LEU ARG MET LEU ASP
SEQRES 27 A 360 TYR ASP PRO LYS THR ARG ILE GLN PRO TYR TYR ALA LEU
SEQRES 28 A 360 GLN HIS SER PHE PHE LYS LYS THR ALA
SEQRES 1 B 360 GLY PRO MET SER SER HIS LYS LYS GLU ARG LYS VAL TYR
SEQRES 2 B 360 ASN ASP GLY TYR ASP ASP ASP ASN TYR ASP TYR ILE VAL
SEQRES 3 B 360 LYS ASN GLY GLU LYS TRP MET ASP ARG TYR GLU ILE ASP
SEQRES 4 B 360 SER LEU ILE GLY LYS GLY SER PHE GLY GLN VAL VAL LYS
SEQRES 5 B 360 ALA TYR ASP ARG VAL GLU GLN GLU TRP VAL ALA ILE LYS
SEQRES 6 B 360 ILE ILE LYS ASN LYS LYS ALA PHE LEU ASN GLN ALA GLN
SEQRES 7 B 360 ILE GLU VAL ARG LEU LEU GLU LEU MET ASN LYS HIS ASP
SEQRES 8 B 360 THR GLU MET LYS TYR TYR ILE VAL HIS LEU LYS ARG HIS
SEQRES 9 B 360 PHE MET PHE ARG ASN HIS LEU CYS LEU VAL PHE GLU MET
SEQRES 10 B 360 LEU SER TYR ASN LEU TYR ASP LEU LEU ARG ASN THR ASN
SEQRES 11 B 360 PHE ARG GLY VAL SER LEU ASN LEU THR ARG LYS PHE ALA
SEQRES 12 B 360 GLN GLN MET CYS THR ALA LEU LEU PHE LEU ALA THR PRO
SEQRES 13 B 360 GLU LEU SER ILE ILE HIS CYS ASP LEU LYS PRO GLU ASN
SEQRES 14 B 360 ILE LEU LEU CYS ASN PRO LYS ARG SER ALA ILE LYS ILE
SEQRES 15 B 360 VAL ASP PHE GLY SER SER CYS GLN LEU GLY GLN ARG ILE
SEQRES 16 B 360 TYR GLN PTR ILE GLN SER ARG PHE TYR ARG SER PRO GLU
SEQRES 17 B 360 VAL LEU LEU GLY MET PRO TYR ASP LEU ALA ILE ASP MET
SEQRES 18 B 360 TRP SER LEU GLY CYS ILE LEU VAL GLU MET HIS THR GLY
SEQRES 19 B 360 GLU PRO LEU PHE SER GLY ALA ASN GLU VAL ASP GLN MET
SEQRES 20 B 360 ASN LYS ILE VAL GLU VAL LEU GLY ILE PRO PRO ALA HIS
SEQRES 21 B 360 ILE LEU ASP GLN ALA PRO LYS ALA ARG LYS PHE PHE GLU
SEQRES 22 B 360 LYS LEU PRO ASP GLY THR TRP ASN LEU LYS LYS THR LYS
SEQRES 23 B 360 ASP GLY LYS ARG GLU TYR LYS PRO PRO GLY THR ARG LYS
SEQRES 24 B 360 LEU HIS ASN ILE LEU GLY VAL GLU THR GLY GLY PRO GLY
SEQRES 25 B 360 GLY ARG ARG ALA GLY GLU SER GLY HIS THR VAL ALA ASP
SEQRES 26 B 360 TYR LEU LYS PHE LYS ASP LEU ILE LEU ARG MET LEU ASP
SEQRES 27 B 360 TYR ASP PRO LYS THR ARG ILE GLN PRO TYR TYR ALA LEU
SEQRES 28 B 360 GLN HIS SER PHE PHE LYS LYS THR ALA
MODRES 6A1G PTR A 321 TYR MODIFIED RESIDUE
MODRES 6A1G PTR B 321 TYR MODIFIED RESIDUE
HET PTR A 321 16
HET PTR B 321 16
HET 9OL A 801 25
HET 9OL B 801 25
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 9OL 5,5-DIMETHYL-8-[1-(PIPERIDIN-4-YL)ETHENYL]-5,6-
HETNAM 2 9OL DIHYDROBENZO[H]QUINAZOLIN-4-AMINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 3 9OL 2(C21 H26 N4)
FORMUL 5 HOH *151(H2 O)
HELIX 1 AA1 TYR A 136 TYR A 140 5 5
HELIX 2 AA2 LYS A 193 LYS A 212 1 20
HELIX 3 AA3 GLU A 216 ILE A 221 5 6
HELIX 4 AA4 ASN A 244 ASN A 251 1 8
HELIX 5 AA5 SER A 258 ALA A 277 1 20
HELIX 6 AA6 LYS A 289 GLU A 291 5 3
HELIX 7 AA7 SER A 324 ARG A 328 5 5
HELIX 8 AA8 SER A 329 LEU A 334 1 6
HELIX 9 AA9 LEU A 340 GLY A 357 1 18
HELIX 10 AB1 ASN A 365 GLY A 378 1 14
HELIX 11 AB2 PRO A 381 ASP A 386 1 6
HELIX 12 AB3 LYS A 390 PHE A 394 1 5
HELIX 13 AB4 LYS A 422 LEU A 427 1 6
HELIX 14 AB5 GLY A 433 ARG A 437 5 5
HELIX 15 AB6 THR A 445 LEU A 460 1 16
HELIX 16 AB7 GLN A 469 HIS A 476 1 8
HELIX 17 AB8 TYR B 136 TYR B 140 5 5
HELIX 18 AB9 LYS B 193 LYS B 212 1 20
HELIX 19 AC1 THR B 215 ILE B 221 5 7
HELIX 20 AC2 ASN B 244 ASN B 251 1 8
HELIX 21 AC3 SER B 258 ALA B 277 1 20
HELIX 22 AC4 LYS B 289 GLU B 291 5 3
HELIX 23 AC5 SER B 324 ARG B 328 5 5
HELIX 24 AC6 SER B 329 LEU B 334 1 6
HELIX 25 AC7 LEU B 340 GLY B 357 1 18
HELIX 26 AC8 ASN B 365 GLY B 378 1 14
HELIX 27 AC9 PRO B 381 ASP B 386 1 6
HELIX 28 AD1 LYS B 390 PHE B 394 1 5
HELIX 29 AD2 LYS B 422 LEU B 427 1 6
HELIX 30 AD3 GLY B 433 ARG B 437 5 5
HELIX 31 AD4 THR B 445 LEU B 460 1 16
HELIX 32 AD5 GLN B 469 LEU B 474 1 6
HELIX 33 AD6 GLN B 475 LYS B 480 5 6
SHEET 1 AA1 6 LYS A 154 TRP A 155 0
SHEET 2 AA1 6 TYR A 159 GLY A 168 -1 O TYR A 159 N TRP A 155
SHEET 3 AA1 6 GLY A 171 ASP A 178 -1 O GLY A 171 N GLY A 168
SHEET 4 AA1 6 GLU A 183 ILE A 190 -1 O ILE A 189 N GLN A 172
SHEET 5 AA1 6 HIS A 233 GLU A 239 -1 O PHE A 238 N ALA A 186
SHEET 6 AA1 6 LEU A 224 PHE A 230 -1 N PHE A 228 O CYS A 235
SHEET 1 AA2 2 ILE A 283 ILE A 284 0
SHEET 2 AA2 2 CYS A 312 GLN A 313 -1 O CYS A 312 N ILE A 284
SHEET 1 AA3 2 ILE A 293 LEU A 295 0
SHEET 2 AA3 2 ILE A 303 ILE A 305 -1 O LYS A 304 N LEU A 294
SHEET 1 AA4 2 PHE A 395 LYS A 397 0
SHEET 2 AA4 2 TRP A 403 LEU A 405 -1 O ASN A 404 N GLU A 396
SHEET 1 AA5 6 LYS B 154 TRP B 155 0
SHEET 2 AA5 6 TYR B 159 GLY B 168 -1 O TYR B 159 N TRP B 155
SHEET 3 AA5 6 GLY B 171 ASP B 178 -1 O GLY B 171 N GLY B 168
SHEET 4 AA5 6 GLU B 183 ILE B 190 -1 O ILE B 189 N GLN B 172
SHEET 5 AA5 6 HIS B 233 GLU B 239 -1 O PHE B 238 N ALA B 186
SHEET 6 AA5 6 LEU B 224 PHE B 230 -1 N ARG B 226 O VAL B 237
SHEET 1 AA6 2 ILE B 283 ILE B 284 0
SHEET 2 AA6 2 CYS B 312 GLN B 313 -1 O CYS B 312 N ILE B 284
SHEET 1 AA7 2 ILE B 293 LEU B 295 0
SHEET 2 AA7 2 ILE B 303 ILE B 305 -1 O LYS B 304 N LEU B 294
SHEET 1 AA8 2 PHE B 395 LYS B 397 0
SHEET 2 AA8 2 TRP B 403 LEU B 405 -1 O ASN B 404 N GLU B 396
LINK C GLN A 320 N PTR A 321 1555 1555 1.33
LINK C PTR A 321 N ILE A 322 1555 1555 1.33
LINK C GLN B 320 N PTR B 321 1555 1555 1.33
LINK C PTR B 321 N ILE B 322 1555 1555 1.33
SITE 1 AC1 7 GLY A 166 LYS A 167 VAL A 173 ALA A 186
SITE 2 AC1 7 GLU A 239 LEU A 241 GLU A 291
SITE 1 AC2 4 GLY B 166 GLU B 239 LEU B 241 GLU B 291
CRYST1 67.841 69.365 89.150 90.00 108.81 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 0.014740 0.000000 0.005021 0.00000
SCALE2 0.000000 0.014416 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011850 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
