HEADER HYDROLASE 07-SEP-16 5LTU
TITLE CRYSTAL STRUCTURE OF NUDT4A- DIPHOSPHOINOSITOL POLYPHOSPHATE
TITLE 2 PHOSPHOHYDROLASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPHOSPHOINOSITOL POLYPHOSPHATE PHOSPHOHYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPP-2,DIADENOSINE 5',5'''-P1,P6-HEXAPHOSPHATE HYDROLASE 2,
COMPND 5 NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF 4,NUDIX MOTIF 4;
COMPND 6 EC: 3.6.1.52,3.6.1.-;
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: NUDT4, DIPP2, KIAA0487, HDCMB47P;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS DIPHOSPHOINOSITOL POLYPHOSPHATE PHOSPHOHYDROLASE 2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.SRIKANNATHASAN,C.A.NUNEZ,C.TALLANT,P.SIEJKA,S.MATHEA,J.NEWMAN,
AUTHOR 2 C.STRAIN-DAMERELL,J.M.ELKINS,N.BURGESS-BROWN,C.H.ARROWSMITH,
AUTHOR 3 A.M.EDWARDS,C.BOUNTRA,F.VON DELFT,K.HUBER
REVDAT 3 17-JAN-24 5LTU 1 REMARK
REVDAT 2 07-FEB-18 5LTU 1 REMARK
REVDAT 1 20-SEP-17 5LTU 0
JRNL AUTH V.SRIKANNATHASAN,K.HUBER
JRNL TITL CRYSTAL STRUCTURE OF HUMAN NUDT4A- DIPHOSPHOINOSITOL
JRNL TITL 2 POLYPHOSPHATE PHOSPHOHYDROLASE 2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1682
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 17026
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.420
REMARK 3 FREE R VALUE TEST SET COUNT : 922
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 62.0212 - 4.2656 0.99 2360 154 0.2044 0.2220
REMARK 3 2 4.2656 - 3.3858 0.99 2271 142 0.1835 0.2126
REMARK 3 3 3.3858 - 2.9578 0.99 2304 133 0.2168 0.2365
REMARK 3 4 2.9578 - 2.6874 0.99 2313 124 0.2426 0.3147
REMARK 3 5 2.6874 - 2.4948 0.99 2281 120 0.2543 0.3103
REMARK 3 6 2.4948 - 2.3477 1.00 2295 119 0.2686 0.3364
REMARK 3 7 2.3477 - 2.2301 0.99 2280 130 0.2752 0.3122
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 2017
REMARK 3 ANGLE : 0.942 2707
REMARK 3 CHIRALITY : 0.039 297
REMARK 3 PLANARITY : 0.003 346
REMARK 3 DIHEDRAL : 14.747 722
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4488 3.5746 15.9172
REMARK 3 T TENSOR
REMARK 3 T11: 0.2748 T22: 0.1799
REMARK 3 T33: 0.2819 T12: 0.0119
REMARK 3 T13: 0.0650 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 3.8526 L22: 0.2577
REMARK 3 L33: 2.3123 L12: -0.3464
REMARK 3 L13: 2.9274 L23: -0.4025
REMARK 3 S TENSOR
REMARK 3 S11: -0.0830 S12: -0.0223 S13: 0.0853
REMARK 3 S21: -0.0145 S22: 0.0701 S23: -0.0827
REMARK 3 S31: -0.0660 S32: 0.0213 S33: 0.0182
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID AA
REMARK 3 SELECTION : CHAIN B AND SEGID BA
REMARK 3 ATOM PAIRS NUMBER : 1088
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5LTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001353.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92819
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R CDTE 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17028
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 62.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 1.05100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, MOLREP
REMARK 200 STARTING MODEL: 2DUK
REMARK 200
REMARK 200 REMARK: NEEDLE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULPHATE, 0.1M TRIS PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 67.85500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.51500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.85500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.51500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 1
REMARK 465 MET A 2
REMARK 465 LYS A 3
REMARK 465 PHE A 4
REMARK 465 LYS A 5
REMARK 465 PRO A 6
REMARK 465 ASN A 7
REMARK 465 GLN A 8
REMARK 465 SER A 40
REMARK 465 ARG A 41
REMARK 465 TYR A 42
REMARK 465 ASP A 106
REMARK 465 TRP A 107
REMARK 465 GLU A 108
REMARK 465 ASP A 109
REMARK 465 SER A 110
REMARK 465 VAL A 111
REMARK 465 ASN A 112
REMARK 465 ILE A 113
REMARK 465 CYS A 147
REMARK 465 SER A 148
REMARK 465 PRO A 149
REMARK 465 ALA A 150
REMARK 465 ASN A 151
REMARK 465 GLY A 152
REMARK 465 ASN A 153
REMARK 465 SER A 154
REMARK 465 THR A 155
REMARK 465 VAL A 156
REMARK 465 PRO A 157
REMARK 465 SER A 158
REMARK 465 LEU A 159
REMARK 465 PRO A 160
REMARK 465 ASP A 161
REMARK 465 ASN A 162
REMARK 465 ASN A 163
REMARK 465 ALA A 164
REMARK 465 LEU A 165
REMARK 465 PHE A 166
REMARK 465 VAL A 167
REMARK 465 THR A 168
REMARK 465 ALA A 169
REMARK 465 ALA A 170
REMARK 465 GLN A 171
REMARK 465 THR A 172
REMARK 465 SER A 173
REMARK 465 GLY A 174
REMARK 465 LEU A 175
REMARK 465 PRO A 176
REMARK 465 SER A 177
REMARK 465 SER A 178
REMARK 465 VAL A 179
REMARK 465 ARG A 180
REMARK 465 MET B 1
REMARK 465 MET B 2
REMARK 465 LYS B 3
REMARK 465 PHE B 4
REMARK 465 LYS B 5
REMARK 465 PRO B 6
REMARK 465 ASN B 7
REMARK 465 ARG B 41
REMARK 465 TYR B 42
REMARK 465 PRO B 43
REMARK 465 ASP B 44
REMARK 465 ASP B 109
REMARK 465 SER B 110
REMARK 465 VAL B 111
REMARK 465 ASN B 112
REMARK 465 ILE B 113
REMARK 465 GLY B 114
REMARK 465 SER B 148
REMARK 465 PRO B 149
REMARK 465 ALA B 150
REMARK 465 ASN B 151
REMARK 465 GLY B 152
REMARK 465 ASN B 153
REMARK 465 SER B 154
REMARK 465 THR B 155
REMARK 465 VAL B 156
REMARK 465 PRO B 157
REMARK 465 SER B 158
REMARK 465 LEU B 159
REMARK 465 PRO B 160
REMARK 465 ASP B 161
REMARK 465 ASN B 162
REMARK 465 ASN B 163
REMARK 465 ALA B 164
REMARK 465 LEU B 165
REMARK 465 PHE B 166
REMARK 465 VAL B 167
REMARK 465 THR B 168
REMARK 465 ALA B 169
REMARK 465 ALA B 170
REMARK 465 GLN B 171
REMARK 465 THR B 172
REMARK 465 SER B 173
REMARK 465 GLY B 174
REMARK 465 LEU B 175
REMARK 465 PRO B 176
REMARK 465 SER B 177
REMARK 465 SER B 178
REMARK 465 VAL B 179
REMARK 465 ARG B 180
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 THR A 9 OG1 CG2
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 SER A 39 OG
REMARK 470 ASP A 44 CG OD1 OD2
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 ASP A 88 CG OD1 OD2
REMARK 470 GLU A 102 CG CD OE1 OE2
REMARK 470 ILE A 103 CG1 CG2 CD1
REMARK 470 GLU A 105 CG CD OE1 OE2
REMARK 470 ARG A 115 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 GLU A 118 CG CD OE1 OE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 LYS A 127 CG CD CE NZ
REMARK 470 HIS A 132 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 ARG B 27 NE CZ NH1 NH2
REMARK 470 SER B 28 OG
REMARK 470 GLU B 29 CG CD OE1 OE2
REMARK 470 GLU B 56 CG CD OE1 OE2
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 ASP B 88 CG OD1 OD2
REMARK 470 GLU B 102 CG CD OE1 OE2
REMARK 470 ILE B 103 CG1 CG2 CD1
REMARK 470 ASP B 106 CG OD1 OD2
REMARK 470 GLU B 108 CG CD OE1 OE2
REMARK 470 LYS B 116 CG CD CE NZ
REMARK 470 GLU B 118 CG CD OE1 OE2
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 LYS B 127 CG CD CE NZ
REMARK 470 CYS B 131 SG
REMARK 470 HIS B 132 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 142 CG CD CE NZ
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 ASP A 44 44.69 -90.15
REMARK 500 GLU B 105 -145.88 22.23
REMARK 500 TRP B 107 -164.82 66.16
REMARK 500 HIS B 132 -16.61 82.46
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 203
DBREF 5LTU A 1 180 UNP Q9NZJ9 NUDT4_HUMAN 1 180
DBREF 5LTU B 1 180 UNP Q9NZJ9 NUDT4_HUMAN 1 180
SEQRES 1 A 180 MET MET LYS PHE LYS PRO ASN GLN THR ARG THR TYR ASP
SEQRES 2 A 180 ARG GLU GLY PHE LYS LYS ARG ALA ALA CYS LEU CYS PHE
SEQRES 3 A 180 ARG SER GLU GLN GLU ASP GLU VAL LEU LEU VAL SER SER
SEQRES 4 A 180 SER ARG TYR PRO ASP GLN TRP ILE VAL PRO GLY GLY GLY
SEQRES 5 A 180 MET GLU PRO GLU GLU GLU PRO GLY GLY ALA ALA VAL ARG
SEQRES 6 A 180 GLU VAL TYR GLU GLU ALA GLY VAL LYS GLY LYS LEU GLY
SEQRES 7 A 180 ARG LEU LEU GLY ILE PHE GLU ASN GLN ASP ARG LYS HIS
SEQRES 8 A 180 ARG THR TYR VAL TYR VAL LEU THR VAL THR GLU ILE LEU
SEQRES 9 A 180 GLU ASP TRP GLU ASP SER VAL ASN ILE GLY ARG LYS ARG
SEQRES 10 A 180 GLU TRP PHE LYS VAL GLU ASP ALA ILE LYS VAL LEU GLN
SEQRES 11 A 180 CYS HIS LYS PRO VAL HIS ALA GLU TYR LEU GLU LYS LEU
SEQRES 12 A 180 LYS LEU GLY CYS SER PRO ALA ASN GLY ASN SER THR VAL
SEQRES 13 A 180 PRO SER LEU PRO ASP ASN ASN ALA LEU PHE VAL THR ALA
SEQRES 14 A 180 ALA GLN THR SER GLY LEU PRO SER SER VAL ARG
SEQRES 1 B 180 MET MET LYS PHE LYS PRO ASN GLN THR ARG THR TYR ASP
SEQRES 2 B 180 ARG GLU GLY PHE LYS LYS ARG ALA ALA CYS LEU CYS PHE
SEQRES 3 B 180 ARG SER GLU GLN GLU ASP GLU VAL LEU LEU VAL SER SER
SEQRES 4 B 180 SER ARG TYR PRO ASP GLN TRP ILE VAL PRO GLY GLY GLY
SEQRES 5 B 180 MET GLU PRO GLU GLU GLU PRO GLY GLY ALA ALA VAL ARG
SEQRES 6 B 180 GLU VAL TYR GLU GLU ALA GLY VAL LYS GLY LYS LEU GLY
SEQRES 7 B 180 ARG LEU LEU GLY ILE PHE GLU ASN GLN ASP ARG LYS HIS
SEQRES 8 B 180 ARG THR TYR VAL TYR VAL LEU THR VAL THR GLU ILE LEU
SEQRES 9 B 180 GLU ASP TRP GLU ASP SER VAL ASN ILE GLY ARG LYS ARG
SEQRES 10 B 180 GLU TRP PHE LYS VAL GLU ASP ALA ILE LYS VAL LEU GLN
SEQRES 11 B 180 CYS HIS LYS PRO VAL HIS ALA GLU TYR LEU GLU LYS LEU
SEQRES 12 B 180 LYS LEU GLY CYS SER PRO ALA ASN GLY ASN SER THR VAL
SEQRES 13 B 180 PRO SER LEU PRO ASP ASN ASN ALA LEU PHE VAL THR ALA
SEQRES 14 B 180 ALA GLN THR SER GLY LEU PRO SER SER VAL ARG
HET EDO A 201 4
HET EDO A 202 4
HET EDO A 203 4
HET EDO A 204 4
HET EDO A 205 4
HET EDO B 201 4
HET EDO B 202 4
HET EDO B 203 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 8(C2 H6 O2)
FORMUL 11 HOH *88(H2 O)
HELIX 1 AA1 GLU A 58 GLY A 72 1 15
HELIX 2 AA2 VAL A 122 LYS A 133 1 12
HELIX 3 AA3 LYS A 133 GLY A 146 1 14
HELIX 4 AA4 GLU B 58 GLY B 72 1 15
HELIX 5 AA5 VAL B 122 GLN B 130 1 9
HELIX 6 AA6 LYS B 133 GLY B 146 1 14
SHEET 1 AA1 4 GLY A 50 GLY A 52 0
SHEET 2 AA1 4 LYS A 18 PHE A 26 -1 N ALA A 21 O GLY A 51
SHEET 3 AA1 4 HIS A 91 ILE A 103 1 O LEU A 98 N PHE A 26
SHEET 4 AA1 4 VAL A 73 ASN A 86 -1 N PHE A 84 O THR A 93
SHEET 1 AA2 3 TRP A 46 ILE A 47 0
SHEET 2 AA2 3 GLU A 33 SER A 38 -1 N VAL A 37 O ILE A 47
SHEET 3 AA2 3 ARG A 117 LYS A 121 -1 O PHE A 120 N VAL A 34
SHEET 1 AA3 4 GLY B 50 GLY B 52 0
SHEET 2 AA3 4 LYS B 18 PHE B 26 -1 N ALA B 21 O GLY B 51
SHEET 3 AA3 4 HIS B 91 ILE B 103 1 O LEU B 98 N PHE B 26
SHEET 4 AA3 4 VAL B 73 ASN B 86 -1 N GLY B 78 O VAL B 97
SHEET 1 AA4 3 TRP B 46 ILE B 47 0
SHEET 2 AA4 3 GLU B 33 SER B 38 -1 N VAL B 37 O ILE B 47
SHEET 3 AA4 3 ARG B 117 LYS B 121 -1 O PHE B 120 N VAL B 34
SITE 1 AC1 3 ARG A 20 GLY A 50 GLY A 51
SITE 1 AC2 2 GLU A 85 EDO A 203
SITE 1 AC3 3 ILE A 83 GLU A 85 EDO A 202
SITE 1 AC4 2 ALA A 71 ARG A 117
SITE 1 AC5 4 ARG B 20 ARG B 89 LYS B 133 HIS B 136
SITE 1 AC6 2 ARG B 115 HOH B 326
SITE 1 AC7 3 SER B 39 SER B 40 GLN B 45
CRYST1 135.710 41.030 74.320 90.00 122.55 90.00 C 1 2 1 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 0.007369 0.000000 0.004703 0.00000
SCALE2 0.000000 0.024372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015963 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
