HEADER HYDROLASE 22-FEB-19 5QP5
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF DCP2 (NUDT20)
TITLE 2 IN COMPLEX WITH Z2895259681
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DCP2 (NUDT20);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 95-260;
COMPND 5 SYNONYM: NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF 20, NUDIX MOTIF
COMPND 6 20, MRNA-DECAPPING ENZYME 2, HDPC, M7GPPPN-MRNA HYDROLASE;
COMPND 7 EC: 3.6.1.62;
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: DCP2, NUDT20;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SGC - DIAMOND I04-1 FRAGMENT SCREENING, PANDDA, XCHEMEXPLORER,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.R.NELSON,S.VELUPILLAI,R.TALON,P.M.COLLINS,T.KROJER,D.WANG,
AUTHOR 2 J.BRANDAO-NETO,A.DOUANGAMATH,N.BURGESS-BROWN,C.H.ARROWSMITH,
AUTHOR 3 C.BOUNTRA,K.HUBER,F.VON DELFT
REVDAT 3 06-MAR-24 5QP5 1 REMARK
REVDAT 2 20-NOV-19 5QP5 1 REMARK
REVDAT 1 08-MAY-19 5QP5 0
JRNL AUTH E.R.NELSON,S.VELUPILLAI,R.TALON,P.M.COLLINS,T.KROJER,D.WANG,
JRNL AUTH 2 J.BRANDAO-NETO,A.DOUANGAMATH,N.BURGESS-BROWN,C.H.ARROWSMITH,
JRNL AUTH 3 C.BOUNTRA,K.HUBER,F.VON DELFT
JRNL TITL PANDDA ANALYSIS GROUP DEPOSITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 14742
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 741
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1047
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 60
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.60000
REMARK 3 B22 (A**2) : -3.24000
REMARK 3 B33 (A**2) : -1.36000
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): 0.191
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.166
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2119 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1617 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2349 ; 1.825 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3734 ; 1.072 ; 2.976
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 217 ; 6.251 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;32.516 ;21.566
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 292 ;17.441 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;18.314 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 232 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2012 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 404 ; 0.002 ; 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): 1010 ; 4.596 ; 5.838
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 975 ; 4.606 ; 5.783
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1045 ; 7.117 ; 8.442
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 5QP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1001402230.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
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
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.32
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15514
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 28.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.78500
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 5MP0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M ACETATE, PH 4.5, 5-25% PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 23.90200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.88000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.52050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.88000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.90200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.52050
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 94
REMARK 465 MET A 95
REMARK 465 ASP A 245
REMARK 465 SER A 246
REMARK 465 SER A 247
REMARK 465 ASP A 248
REMARK 465 SER A 249
REMARK 465 ASP A 250
REMARK 465 ASN A 251
REMARK 465 GLY A 252
REMARK 465 PHE A 253
REMARK 465 SER A 254
REMARK 465 SER A 255
REMARK 465 THR A 256
REMARK 465 GLY A 257
REMARK 465 SER A 258
REMARK 465 THR A 259
REMARK 465 PRO A 260
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 130 CE NZ
REMARK 470 LYS A 133 CG CD CE NZ
REMARK 470 GLU A 134 CG CD OE1 OE2
REMARK 470 LYS A 159 CD CE NZ
REMARK 470 ASP A 169 CG OD1 OD2
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 LYS A 185 CE NZ
REMARK 470 LYS A 215 CD CE NZ
REMARK 470 LYS A 217 CE NZ
REMARK 470 ARG A 241 CD NE CZ NH1 NH2
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 TYR A 156 CB TYR A 156 CG -0.091
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 LEU A 119 -110.72 57.23
REMARK 500 LYS A 121 40.82 -108.61
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LFY A 306
DBREF 5QP5 A 95 260 UNP Q8IU60 DCP2_HUMAN 95 260
SEQADV 5QP5 SER A 94 UNP Q8IU60 EXPRESSION TAG
SEQRES 1 A 167 SER MET GLY VAL PRO THR TYR GLY ALA ILE ILE LEU ASP
SEQRES 2 A 167 GLU THR LEU GLU ASN VAL LEU LEU VAL GLN GLY TYR LEU
SEQRES 3 A 167 ALA LYS SER GLY TRP GLY PHE PRO LYS GLY LYS VAL ASN
SEQRES 4 A 167 LYS GLU GLU ALA PRO HIS ASP CYS ALA ALA ARG GLU VAL
SEQRES 5 A 167 PHE GLU GLU THR GLY PHE ASP ILE LYS ASP TYR ILE CYS
SEQRES 6 A 167 LYS ASP ASP TYR ILE GLU LEU ARG ILE ASN ASP GLN LEU
SEQRES 7 A 167 ALA ARG LEU TYR ILE ILE PRO GLY ILE PRO LYS ASP THR
SEQRES 8 A 167 LYS PHE ASN PRO LYS THR ARG ARG GLU ILE ARG ASN ILE
SEQRES 9 A 167 GLU TRP PHE SER ILE GLU LYS LEU PRO CYS HIS ARG ASN
SEQRES 10 A 167 ASP MET THR PRO LYS SER LYS LEU GLY LEU ALA PRO ASN
SEQRES 11 A 167 LYS PHE PHE MET ALA ILE PRO PHE ILE ARG PRO LEU ARG
SEQRES 12 A 167 ASP TRP LEU SER ARG ARG PHE GLY ASP SER SER ASP SER
SEQRES 13 A 167 ASP ASN GLY PHE SER SER THR GLY SER THR PRO
HET EDO A 301 4
HET EDO A 302 4
HET DMS A 303 4
HET ACT A 304 4
HET ACT A 305 4
HET LFY A 306 18
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM ACT ACETATE ION
HETNAM LFY 1-ETHYL-N-[(4-FLUOROPHENYL)METHYL]-1H-IMIDAZOLE-4-
HETNAM 2 LFY CARBOXAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 2(C2 H6 O2)
FORMUL 4 DMS C2 H6 O S
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 7 LFY C13 H14 F N3 O
FORMUL 8 HOH *60(H2 O)
HELIX 1 AA1 LEU A 119 SER A 122 5 4
HELIX 2 AA2 ALA A 136 GLY A 150 1 15
HELIX 3 AA3 THR A 213 SER A 216 5 4
HELIX 4 AA4 ALA A 228 GLY A 244 1 17
SHEET 1 AA1 4 LYS A 128 LYS A 130 0
SHEET 2 AA1 4 THR A 99 ILE A 104 -1 N TYR A 100 O GLY A 129
SHEET 3 AA1 4 LEU A 171 ILE A 177 1 O ILE A 177 N ILE A 103
SHEET 4 AA1 4 TYR A 162 ARG A 166 -1 N ILE A 163 O LEU A 174
SHEET 1 AA2 3 TRP A 124 GLY A 125 0
SHEET 2 AA2 3 ASN A 111 GLY A 117 -1 N VAL A 115 O GLY A 125
SHEET 3 AA2 3 ILE A 194 SER A 201 -1 O PHE A 200 N VAL A 112
SHEET 1 AA3 2 ASP A 211 MET A 212 0
SHEET 2 AA3 2 LYS A 217 LEU A 220 -1 N LYS A 217 O MET A 212
SITE 1 AC1 4 ALA A 142 PHE A 146 ASP A 152 LYS A 154
SITE 1 AC2 4 ASN A 223 LYS A 224 HOH A 401 HOH A 412
SITE 1 AC3 2 ASN A 111 TRP A 199
SITE 1 AC4 5 LEU A 119 SER A 122 TYR A 156 ARG A 195
SITE 2 AC4 5 HOH A 408
SITE 1 AC5 3 ARG A 209 PRO A 222 ASN A 223
SITE 1 AC6 10 VAL A 115 GLY A 117 ALA A 120 LYS A 121
SITE 2 AC6 10 SER A 122 GLY A 123 GLY A 125 GLU A 148
SITE 3 AC6 10 ILE A 194 MET A 227
CRYST1 47.804 61.041 65.760 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 0.020919 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016382 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015207 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
