HEADER TRANSFERASE 22-DEC-16 5MRB
TITLE CRYSTAL STRUCTURE OF HUMAN MPS1 (TTK) IN COMPLEX WITH CPD-5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY PROTEIN KINASE TTK;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHOTYROSINE PICKED THREONINE-PROTEIN KINASE,PYT;
COMPND 5 EC: 2.7.12.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: TTK, MPS1, MPS1L1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MPS1, TTK, KINASE, INHIBITOR, CPD-5, COMPOUND 5, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.HIRUMA,R.P.JOOSTEN,A.PERRAKIS
REVDAT 6 17-JAN-24 5MRB 1 REMARK
REVDAT 5 13-SEP-17 5MRB 1 JRNL
REVDAT 4 23-AUG-17 5MRB 1 REMARK
REVDAT 3 09-AUG-17 5MRB 1 REMARK
REVDAT 2 02-AUG-17 5MRB 1
REVDAT 1 26-JUL-17 5MRB 0
JRNL AUTH Y.HIRUMA,A.KOCH,N.HAZRATY,F.TSAKOU,R.H.MEDEMA,R.P.JOOSTEN,
JRNL AUTH 2 A.PERRAKIS
JRNL TITL UNDERSTANDING INHIBITOR RESISTANCE IN MPS1 KINASE THROUGH
JRNL TITL 2 NOVEL BIOPHYSICAL ASSAYS AND STRUCTURES.
JRNL REF J. BIOL. CHEM. V. 292 14496 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28726638
JRNL DOI 10.1074/JBC.M117.783555
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 22011
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1214
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2164
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.81000
REMARK 3 B22 (A**2) : -2.12000
REMARK 3 B33 (A**2) : 2.94000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.158
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.558
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5MRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002891.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96771
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23225
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 41.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.86800
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 2.6.1
REMARK 200 STARTING MODEL: 3HMN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 200 UM (7.2 MG/ML)
REMARK 280 MPS1, 250 UM CPD-5. RESERVOIR SOLUTION: 15.5% (W/V) PEG 350 MME,
REMARK 280 10 MM MGCL2, AND 100 MM TRIS/HCL, PH 8.8, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.29100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.70950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.51250
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.29100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.70950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.51250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.29100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.70950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 57.51250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.29100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.70950
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 57.51250
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: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 25.0 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 MET A 496
REMARK 465 HIS A 497
REMARK 465 HIS A 498
REMARK 465 HIS A 499
REMARK 465 HIS A 500
REMARK 465 HIS A 501
REMARK 465 HIS A 502
REMARK 465 SER A 503
REMARK 465 SER A 504
REMARK 465 GLY A 505
REMARK 465 VAL A 506
REMARK 465 ASP A 507
REMARK 465 LEU A 508
REMARK 465 GLY A 509
REMARK 465 THR A 510
REMARK 465 GLU A 511
REMARK 465 ASN A 512
REMARK 465 LEU A 513
REMARK 465 VAL A 678
REMARK 465 VAL A 679
REMARK 465 LYS A 680
REMARK 465 ASP A 681
REMARK 465 SER A 682
REMARK 465 MET A 698
REMARK 465 SER A 699
REMARK 465 SER A 700
REMARK 465 SER A 701
REMARK 465 ARG A 702
REMARK 465 GLU A 703
REMARK 465 ASN A 704
REMARK 465 GLY A 705
REMARK 465 LYS A 706
REMARK 465 SER A 707
REMARK 465 LYS A 708
REMARK 465 SER A 709
REMARK 465 LYS A 710
REMARK 465 HIS A 796
REMARK 465 PRO A 797
REMARK 465 VAL A 798
REMARK 465 ASN A 799
REMARK 465 GLN A 800
REMARK 465 MET A 801
REMARK 465 ALA A 802
REMARK 465 LYS A 803
REMARK 465 GLY A 804
REMARK 465 THR A 805
REMARK 465 THR A 806
REMARK 465 GLU A 807
REMARK 465 GLU A 808
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 LYS A 617 -75.01 -74.38
REMARK 500 ASP A 647 44.13 -150.54
REMARK 500 ASP A 674 -65.68 59.34
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 C5N A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 912
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 913
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5LJJ RELATED DB: PDB
REMARK 900 5LJJ CONTAINS THE SAME PROTEIN BOUND TO REVERSINE
DBREF 5MRB A 519 808 UNP P33981 TTK_HUMAN 519 808
SEQADV 5MRB MET A 496 UNP P33981 INITIATING METHIONINE
SEQADV 5MRB HIS A 497 UNP P33981 EXPRESSION TAG
SEQADV 5MRB HIS A 498 UNP P33981 EXPRESSION TAG
SEQADV 5MRB HIS A 499 UNP P33981 EXPRESSION TAG
SEQADV 5MRB HIS A 500 UNP P33981 EXPRESSION TAG
SEQADV 5MRB HIS A 501 UNP P33981 EXPRESSION TAG
SEQADV 5MRB HIS A 502 UNP P33981 EXPRESSION TAG
SEQADV 5MRB SER A 503 UNP P33981 EXPRESSION TAG
SEQADV 5MRB SER A 504 UNP P33981 EXPRESSION TAG
SEQADV 5MRB GLY A 505 UNP P33981 EXPRESSION TAG
SEQADV 5MRB VAL A 506 UNP P33981 EXPRESSION TAG
SEQADV 5MRB ASP A 507 UNP P33981 EXPRESSION TAG
SEQADV 5MRB LEU A 508 UNP P33981 EXPRESSION TAG
SEQADV 5MRB GLY A 509 UNP P33981 EXPRESSION TAG
SEQADV 5MRB THR A 510 UNP P33981 EXPRESSION TAG
SEQADV 5MRB GLU A 511 UNP P33981 EXPRESSION TAG
SEQADV 5MRB ASN A 512 UNP P33981 EXPRESSION TAG
SEQADV 5MRB LEU A 513 UNP P33981 EXPRESSION TAG
SEQADV 5MRB TYR A 514 UNP P33981 EXPRESSION TAG
SEQADV 5MRB PHE A 515 UNP P33981 EXPRESSION TAG
SEQADV 5MRB GLN A 516 UNP P33981 EXPRESSION TAG
SEQADV 5MRB SER A 517 UNP P33981 EXPRESSION TAG
SEQADV 5MRB MET A 518 UNP P33981 EXPRESSION TAG
SEQADV 5MRB TYR A 604 UNP P33981 CYS 604 ENGINEERED MUTATION
SEQRES 1 A 313 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 313 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER VAL LYS
SEQRES 3 A 313 GLY ARG ILE TYR SER ILE LEU LYS GLN ILE GLY SER GLY
SEQRES 4 A 313 GLY SER SER LYS VAL PHE GLN VAL LEU ASN GLU LYS LYS
SEQRES 5 A 313 GLN ILE TYR ALA ILE LYS TYR VAL ASN LEU GLU GLU ALA
SEQRES 6 A 313 ASP ASN GLN THR LEU ASP SER TYR ARG ASN GLU ILE ALA
SEQRES 7 A 313 TYR LEU ASN LYS LEU GLN GLN HIS SER ASP LYS ILE ILE
SEQRES 8 A 313 ARG LEU TYR ASP TYR GLU ILE THR ASP GLN TYR ILE TYR
SEQRES 9 A 313 MET VAL MET GLU TYR GLY ASN ILE ASP LEU ASN SER TRP
SEQRES 10 A 313 LEU LYS LYS LYS LYS SER ILE ASP PRO TRP GLU ARG LYS
SEQRES 11 A 313 SER TYR TRP LYS ASN MET LEU GLU ALA VAL HIS THR ILE
SEQRES 12 A 313 HIS GLN HIS GLY ILE VAL HIS SER ASP LEU LYS PRO ALA
SEQRES 13 A 313 ASN PHE LEU ILE VAL ASP GLY MET LEU LYS LEU ILE ASP
SEQRES 14 A 313 PHE GLY ILE ALA ASN GLN MET GLN PRO ASP THR THR SER
SEQRES 15 A 313 VAL VAL LYS ASP SER GLN VAL GLY THR VAL ASN TYR MET
SEQRES 16 A 313 PRO PRO GLU ALA ILE LYS ASP MET SER SER SER ARG GLU
SEQRES 17 A 313 ASN GLY LYS SER LYS SER LYS ILE SER PRO LYS SER ASP
SEQRES 18 A 313 VAL TRP SER LEU GLY CYS ILE LEU TYR TYR MET THR TYR
SEQRES 19 A 313 GLY LYS THR PRO PHE GLN GLN ILE ILE ASN GLN ILE SER
SEQRES 20 A 313 LYS LEU HIS ALA ILE ILE ASP PRO ASN HIS GLU ILE GLU
SEQRES 21 A 313 PHE PRO ASP ILE PRO GLU LYS ASP LEU GLN ASP VAL LEU
SEQRES 22 A 313 LYS CYS CYS LEU LYS ARG ASP PRO LYS GLN ARG ILE SER
SEQRES 23 A 313 ILE PRO GLU LEU LEU ALA HIS PRO TYR VAL GLN ILE GLN
SEQRES 24 A 313 THR HIS PRO VAL ASN GLN MET ALA LYS GLY THR THR GLU
SEQRES 25 A 313 GLU
HET C5N A 901 43
HET EDO A 902 4
HET EDO A 903 4
HET EDO A 904 4
HET EDO A 905 4
HET EDO A 906 4
HET EDO A 907 4
HET EDO A 908 4
HET EDO A 909 4
HET EDO A 910 4
HET EDO A 911 4
HET EDO A 912 4
HET EDO A 913 4
HET CL A 914 1
HETNAM C5N ~{N}-(2,6-DIETHYLPHENYL)-8-[[2-METHOXY-4-(4-
HETNAM 2 C5N METHYLPIPERAZIN-1-YL)PHENYL]AMINO]-1-METHYL-4,5-
HETNAM 3 C5N DIHYDROPYRAZOLO[4,3-H]QUINAZOLINE-3-CARBOXAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 C5N C33 H40 N8 O2
FORMUL 3 EDO 12(C2 H6 O2)
FORMUL 15 CL CL 1-
FORMUL 16 HOH *70(H2 O)
HELIX 1 AA1 ASP A 561 GLN A 579 1 19
HELIX 2 AA2 LEU A 609 LYS A 616 1 8
HELIX 3 AA3 ASP A 620 HIS A 641 1 22
HELIX 4 AA4 LYS A 649 ALA A 651 5 3
HELIX 5 AA5 PRO A 691 LYS A 696 1 6
HELIX 6 AA6 SER A 712 GLY A 730 1 19
HELIX 7 AA7 ASN A 739 ASP A 749 1 11
HELIX 8 AA8 GLU A 761 LEU A 772 1 12
HELIX 9 AA9 SER A 781 ALA A 787 1 7
HELIX 10 AB1 HIS A 788 ILE A 793 1 6
SHEET 1 AA1 6 GLN A 516 VAL A 520 0
SHEET 2 AA1 6 ARG A 523 GLY A 534 -1 O TYR A 525 N MET A 518
SHEET 3 AA1 6 SER A 537 LEU A 543 -1 O GLN A 541 N LYS A 529
SHEET 4 AA1 6 ILE A 549 ASN A 556 -1 O TYR A 554 N LYS A 538
SHEET 5 AA1 6 TYR A 597 MET A 602 -1 O MET A 602 N ALA A 551
SHEET 6 AA1 6 LEU A 588 ILE A 593 -1 N ASP A 590 O VAL A 601
SHEET 1 AA2 3 ILE A 607 ASP A 608 0
SHEET 2 AA2 3 PHE A 653 VAL A 656 -1 O ILE A 655 N ILE A 607
SHEET 3 AA2 3 MET A 659 LEU A 662 -1 O MET A 659 N VAL A 656
SITE 1 AC1 16 ILE A 531 SER A 533 GLY A 534 SER A 537
SITE 2 AC1 16 ALA A 551 LYS A 553 GLU A 603 TYR A 604
SITE 3 AC1 16 GLY A 605 ASN A 606 ASP A 608 SER A 611
SITE 4 AC1 16 ALA A 651 LEU A 654 ILE A 663 GLN A 670
SITE 1 AC2 6 SER A 526 LYS A 547 TYR A 604 ASN A 606
SITE 2 AC2 6 ASP A 657 HOH A1004
SITE 1 AC3 2 GLN A 579 ARG A 587
SITE 1 AC4 6 LYS A 547 ILE A 549 TYR A 550 TYR A 589
SITE 2 AC4 6 GLU A 603 TYR A 604
SITE 1 AC5 3 TRP A 622 LYS A 625 LYS A 629
SITE 1 AC6 3 LYS A 529 GLN A 541 TYR A 604
SITE 1 AC7 1 LEU A 528
SITE 1 AC8 5 LYS A 521 LYS A 777 ARG A 779 GLU A 784
SITE 2 AC8 5 HOH A1019
SITE 1 AC9 3 TRP A 622 TYR A 627 GLY A 658
SITE 1 AD1 5 PRO A 760 GLU A 761 LYS A 762 ASP A 763
SITE 2 AD1 5 HOH A1020
SITE 1 AD2 2 SER A 626 ASN A 630
SITE 1 AD3 5 HIS A 581 SER A 582 GLU A 633 THR A 637
SITE 2 AD3 5 GLN A 640
SITE 1 AD4 4 ARG A 523 TYR A 525 ASN A 544 TYR A 550
CRYST1 70.582 111.419 115.025 90.00 90.00 90.00 I 2 2 2 8
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 0.014168 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008975 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008694 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
