HEADER TRANSFERASE/TRANSFERASE INHIBITOR 15-FEB-17 5UU1
TITLE CRYSTAL STRUCTURE OF HUMAN VACCINIA-RELATED KINASE 2 (VRK-2) BOUND TO
TITLE 2 BI-D1870
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE VRK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 14-335;
COMPND 5 SYNONYM: VACCINIA-RELATED KINASE 2;
COMPND 6 EC: 2.7.11.1;
COMPND 7 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: VRK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: R3
KEYWDS TRANSFERASE, PROTEIN KINASE DOMAIN, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.COUNAGO,C.BOUNTRA,P.ARRUDA,A.M.EDWARDS,O.GILEADI,STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (SGC)
REVDAT 5 04-OCT-23 5UU1 1 REMARK
REVDAT 4 01-JAN-20 5UU1 1 REMARK
REVDAT 3 17-APR-19 5UU1 1 REMARK
REVDAT 2 04-APR-18 5UU1 1 JRNL
REVDAT 1 01-MAR-17 5UU1 0
SPRSDE 01-MAR-17 5UU1 5TKX
JRNL AUTH R.M.COUNAGO,C.K.ALLERSTON,P.SAVITSKY,H.AZEVEDO,P.H.GODOI,
JRNL AUTH 2 C.I.WELLS,A.MASCARELLO,F.H.DE SOUZA GAMA,K.B.MASSIRER,
JRNL AUTH 3 W.J.ZUERCHER,C.R.W.GUIMARAES,O.GILEADI
JRNL TITL STRUCTURAL CHARACTERIZATION OF HUMAN VACCINIA-RELATED
JRNL TITL 2 KINASES (VRK) BOUND TO SMALL-MOLECULE INHIBITORS IDENTIFIES
JRNL TITL 3 DIFFERENT P-LOOP CONFORMATIONS.
JRNL REF SCI REP V. 7 7501 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28790404
JRNL DOI 10.1038/S41598-017-07755-Y
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 22467
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1100
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 : 11
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.10
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.06
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2932
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2144
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2795
REMARK 3 BIN R VALUE (WORKING SET) : 0.2136
REMARK 3 BIN FREE R VALUE : 0.2295
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.67
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 137
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 : 2391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.63750
REMARK 3 B22 (A**2) : -11.64520
REMARK 3 B33 (A**2) : 2.00780
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) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.173
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.151
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.167
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.150
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 : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2483 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3383 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 826 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 51 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 369 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2483 ; 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 : 312 ; 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 : 2947 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.36
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.91
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|14 - 82}
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2455 -18.4871 -2.9641
REMARK 3 T TENSOR
REMARK 3 T11: -0.0685 T22: -0.0126
REMARK 3 T33: -0.0307 T12: 0.0401
REMARK 3 T13: -0.0004 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 3.6769 L22: 0.6331
REMARK 3 L33: 1.7632 L12: 0.6761
REMARK 3 L13: -0.4849 L23: 0.2532
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: -0.0833 S13: -0.0157
REMARK 3 S21: 0.1651 S22: -0.0328 S23: 0.0324
REMARK 3 S31: 0.1754 S32: 0.1110 S33: 0.0393
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|83 - 139}
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8661 -13.2167 -12.4498
REMARK 3 T TENSOR
REMARK 3 T11: -0.0877 T22: -0.0896
REMARK 3 T33: 0.0235 T12: 0.0196
REMARK 3 T13: 0.0365 T23: -0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 0.9504 L22: 0.1607
REMARK 3 L33: 3.6979 L12: 0.1576
REMARK 3 L13: -0.3966 L23: -0.0209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0792 S12: -0.0901 S13: 0.1764
REMARK 3 S21: -0.1274 S22: 0.0304 S23: -0.1031
REMARK 3 S31: -0.0894 S32: -0.2169 S33: -0.1096
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|140 - 328}
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8938 -15.9375 -30.4453
REMARK 3 T TENSOR
REMARK 3 T11: -0.1270 T22: -0.0858
REMARK 3 T33: -0.1056 T12: 0.0049
REMARK 3 T13: -0.0142 T23: 0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 3.3110 L22: 1.1974
REMARK 3 L33: 2.9900 L12: 0.4105
REMARK 3 L13: -1.3475 L23: -0.6765
REMARK 3 S TENSOR
REMARK 3 S11: -0.1094 S12: 0.0039 S13: 0.1193
REMARK 3 S21: -0.1076 S22: 0.2146 S23: 0.1116
REMARK 3 S31: 0.1031 S32: -0.1485 S33: -0.1052
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226469.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.45869
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS MAY 1, 2016
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22504
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 28.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.69300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: 2V62
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 3350; 20 MM MAGNESIUM,
REMARK 280 CHLORIDE, 0.1M CHC BUFFER PH 7.5, STABILIZED WITH 20% (V/V)
REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 27.23850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.52100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.34150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.52100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.23850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.34150
REMARK 290 SMTRY3 4 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 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 12
REMARK 465 MET A 13
REMARK 465 GLY A 329
REMARK 465 GLN A 330
REMARK 465 SER A 331
REMARK 465 ILE A 332
REMARK 465 ASN A 333
REMARK 465 VAL A 334
REMARK 465 HIS A 335
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 25 CG CD OE1 OE2
REMARK 470 PHE A 40 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 GLU A 66 CG CD OE1 OE2
REMARK 470 ASN A 67 CG OD1 ND2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 LYS A 87 CG CD CE NZ
REMARK 470 LYS A 88 CG CD CE NZ
REMARK 470 ARG A 92 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 93 CG CD CE NZ
REMARK 470 GLN A 94 CG CD OE1 NE2
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 130 CG CD CE NZ
REMARK 470 GLN A 134 CG CD OE1 NE2
REMARK 470 ASN A 135 CG OD1 ND2
REMARK 470 LYS A 139 CG CD CE NZ
REMARK 470 GLU A 159 CG CD OE1 OE2
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 GLN A 203 CG CD OE1 NE2
REMARK 470 ARG A 207 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 LYS A 247 CG CD CE NZ
REMARK 470 GLU A 251 CG CD OE1 OE2
REMARK 470 GLN A 252 CG CD OE1 NE2
REMARK 470 ASN A 253 CG OD1 ND2
REMARK 470 LYS A 255 CG CD CE NZ
REMARK 470 GLN A 307 CG CD OE1 NE2
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 ASP A 324 CG OD1 OD2
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 67 -121.52 61.52
REMARK 500 ASP A 166 42.53 -151.15
REMARK 500 CYS A 285 41.32 -108.92
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 7DZ A 401
DBREF 5UU1 A 14 335 UNP Q86Y07 VRK2_HUMAN 14 335
SEQADV 5UU1 SER A 12 UNP Q86Y07 EXPRESSION TAG
SEQADV 5UU1 MET A 13 UNP Q86Y07 EXPRESSION TAG
SEQRES 1 A 324 SER MET PRO PHE PRO GLU GLY LYS VAL LEU ASP ASP MET
SEQRES 2 A 324 GLU GLY ASN GLN TRP VAL LEU GLY LYS LYS ILE GLY SER
SEQRES 3 A 324 GLY GLY PHE GLY LEU ILE TYR LEU ALA PHE PRO THR ASN
SEQRES 4 A 324 LYS PRO GLU LYS ASP ALA ARG HIS VAL VAL LYS VAL GLU
SEQRES 5 A 324 TYR GLN GLU ASN GLY PRO LEU PHE SER GLU LEU LYS PHE
SEQRES 6 A 324 TYR GLN ARG VAL ALA LYS LYS ASP CYS ILE LYS LYS TRP
SEQRES 7 A 324 ILE GLU ARG LYS GLN LEU ASP TYR LEU GLY ILE PRO LEU
SEQRES 8 A 324 PHE TYR GLY SER GLY LEU THR GLU PHE LYS GLY ARG SER
SEQRES 9 A 324 TYR ARG PHE MET VAL MET GLU ARG LEU GLY ILE ASP LEU
SEQRES 10 A 324 GLN LYS ILE SER GLY GLN ASN GLY THR PHE LYS LYS SER
SEQRES 11 A 324 THR VAL LEU GLN LEU GLY ILE ARG MET LEU ASP VAL LEU
SEQRES 12 A 324 GLU TYR ILE HIS GLU ASN GLU TYR VAL HIS GLY ASP ILE
SEQRES 13 A 324 LYS ALA ALA ASN LEU LEU LEU GLY TYR LYS ASN PRO ASP
SEQRES 14 A 324 GLN VAL TYR LEU ALA ASP TYR GLY LEU SER TYR ARG TYR
SEQRES 15 A 324 CYS PRO ASN GLY ASN HIS LYS GLN TYR GLN GLU ASN PRO
SEQRES 16 A 324 ARG LYS GLY HIS ASN GLY THR ILE GLU PHE THR SER LEU
SEQRES 17 A 324 ASP ALA HIS LYS GLY VAL ALA LEU SER ARG ARG SER ASP
SEQRES 18 A 324 VAL GLU ILE LEU GLY TYR CYS MET LEU ARG TRP LEU CYS
SEQRES 19 A 324 GLY LYS LEU PRO TRP GLU GLN ASN LEU LYS ASP PRO VAL
SEQRES 20 A 324 ALA VAL GLN THR ALA LYS THR ASN LEU LEU ASP GLU LEU
SEQRES 21 A 324 PRO GLN SER VAL LEU LYS TRP ALA PRO SER GLY SER SER
SEQRES 22 A 324 CYS CYS GLU ILE ALA GLN PHE LEU VAL CYS ALA HIS SER
SEQRES 23 A 324 LEU ALA TYR ASP GLU LYS PRO ASN TYR GLN ALA LEU LYS
SEQRES 24 A 324 LYS ILE LEU ASN PRO HIS GLY ILE PRO LEU GLY PRO LEU
SEQRES 25 A 324 ASP PHE SER THR LYS GLY GLN SER ILE ASN VAL HIS
HET 7DZ A 401 28
HETNAM 7DZ (7S)-2-[(3,5-DIFLUORO-4-HYDROXYPHENYL)AMINO]-5,7-
HETNAM 2 7DZ DIMETHYL-8-(3-METHYLBUTYL)-7,8-DIHYDROPTERIDIN-6(5H)-
HETNAM 3 7DZ ONE
HETSYN 7DZ BI-D1870
FORMUL 2 7DZ C19 H23 F2 N5 O2
FORMUL 3 HOH *137(H2 O)
HELIX 1 AA1 PRO A 69 ALA A 81 1 13
HELIX 2 AA2 LYS A 82 GLN A 94 1 13
HELIX 3 AA3 GLN A 129 SER A 132 5 4
HELIX 4 AA4 GLY A 133 THR A 137 5 5
HELIX 5 AA5 LYS A 139 ASN A 160 1 22
HELIX 6 AA6 LYS A 168 ALA A 170 5 3
HELIX 7 AA7 CYS A 194 ASN A 198 5 5
HELIX 8 AA8 ASN A 205 GLY A 209 5 5
HELIX 9 AA9 SER A 218 LYS A 223 1 6
HELIX 10 AB1 SER A 228 GLY A 246 1 19
HELIX 11 AB2 TRP A 250 LEU A 254 5 5
HELIX 12 AB3 ASP A 256 GLU A 270 1 15
HELIX 13 AB4 PRO A 272 ALA A 279 1 8
HELIX 14 AB5 CYS A 285 SER A 297 1 13
HELIX 15 AB6 ASN A 305 ASN A 314 1 10
SHEET 1 AA1 6 VAL A 20 ASP A 22 0
SHEET 2 AA1 6 GLN A 28 GLY A 38 -1 O TRP A 29 N LEU A 21
SHEET 3 AA1 6 GLY A 41 PRO A 48 -1 O LEU A 45 N GLY A 32
SHEET 4 AA1 6 HIS A 58 GLU A 63 -1 O VAL A 62 N LEU A 42
SHEET 5 AA1 6 ARG A 114 GLU A 122 -1 O MET A 119 N LYS A 61
SHEET 6 AA1 6 PHE A 103 PHE A 111 -1 N GLY A 105 O VAL A 120
SHEET 1 AA2 3 LEU A 124 ASP A 127 0
SHEET 2 AA2 3 LEU A 172 GLY A 175 -1 O LEU A 174 N GLY A 125
SHEET 3 AA2 3 VAL A 182 LEU A 184 -1 O TYR A 183 N LEU A 173
SHEET 1 AA3 2 TYR A 162 VAL A 163 0
SHEET 2 AA3 2 TYR A 191 ARG A 192 -1 O TYR A 191 N VAL A 163
CISPEP 1 LEU A 271 PRO A 272 0 -4.89
SITE 1 AC1 14 GLY A 38 ILE A 43 VAL A 59 LYS A 61
SITE 2 AC1 14 TYR A 77 PRO A 101 MET A 121 GLU A 122
SITE 3 AC1 14 LEU A 124 ALA A 170 LEU A 173 ALA A 185
SITE 4 AC1 14 HOH A 502 HOH A 510
CRYST1 54.477 72.683 83.042 90.00 90.00 90.00 P 21 21 21 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 0.018356 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013758 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012042 0.00000
(ATOM LINES ARE NOT SHOWN.)
END