HEADER HYDROLASE/HYDROLASE INHIBITOR 09-MAY-13 3WAW
TITLE CRYSTAL STRUCTURE OF AUTOTAXIN IN COMPLEX WITH 2BOA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE FAMILY
COMPND 3 MEMBER 2;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: ATX, E-NPP 2, AUTOTAXIN, EXTRACELLULAR LYSOPHOSPHOLIPASE D,
COMPND 6 LYSOPLD;
COMPND 7 EC: 3.1.4.39;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ENPP2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNT1-;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCD-CW
KEYWDS HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.NISHIMASU,R.ISHITANI,O.NUREKI
REVDAT 4 08-NOV-23 3WAW 1 HETSYN
REVDAT 3 29-JUL-20 3WAW 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 16-OCT-13 3WAW 1 JRNL
REVDAT 1 31-JUL-13 3WAW 0
JRNL AUTH M.KAWAGUCHI,T.OKABE,S.OKUDAIRA,H.NISHIMASU,R.ISHITANI,
JRNL AUTH 2 H.KOJIMA,O.NUREKI,J.AOKI,T.NAGANO
JRNL TITL SCREENING AND X-RAY CRYSTAL STRUCTURE-BASED OPTIMIZATION OF
JRNL TITL 2 AUTOTAXIN (ENPP2) INHIBITORS, USING A NEWLY DEVELOPED
JRNL TITL 3 FLUORESCENCE PROBE
JRNL REF ACS CHEM.BIOL. V. 8 1713 2013
JRNL REFN ISSN 1554-8929
JRNL PMID 23688339
JRNL DOI 10.1021/CB400150C
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.2_869
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.480
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 60975
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3081
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 47.1457 - 5.4711 1.00 2754 149 0.1897 0.2084
REMARK 3 2 5.4711 - 4.3436 1.00 2691 164 0.1515 0.1715
REMARK 3 3 4.3436 - 3.7948 1.00 2685 154 0.1565 0.1843
REMARK 3 4 3.7948 - 3.4479 0.99 2655 151 0.1715 0.2187
REMARK 3 5 3.4479 - 3.2009 0.99 2728 134 0.1872 0.2488
REMARK 3 6 3.2009 - 3.0122 0.99 2639 141 0.1940 0.2326
REMARK 3 7 3.0122 - 2.8613 0.99 2668 145 0.1997 0.2577
REMARK 3 8 2.8613 - 2.7368 0.99 2639 156 0.1953 0.2321
REMARK 3 9 2.7368 - 2.6315 0.99 2657 127 0.1836 0.2104
REMARK 3 10 2.6315 - 2.5407 0.99 2640 143 0.1869 0.2622
REMARK 3 11 2.5407 - 2.4612 0.99 2638 125 0.2031 0.2637
REMARK 3 12 2.4612 - 2.3909 0.98 2653 144 0.2097 0.2678
REMARK 3 13 2.3909 - 2.3279 0.98 2647 137 0.2077 0.2952
REMARK 3 14 2.3279 - 2.2711 0.98 2604 153 0.1998 0.2506
REMARK 3 15 2.2711 - 2.2195 0.98 2635 127 0.2074 0.2692
REMARK 3 16 2.2195 - 2.1723 0.97 2610 143 0.2310 0.2679
REMARK 3 17 2.1723 - 2.1288 0.97 2615 110 0.2340 0.2971
REMARK 3 18 2.1288 - 2.0887 0.98 2631 139 0.2511 0.3322
REMARK 3 19 2.0887 - 2.0513 0.97 2570 142 0.2626 0.2955
REMARK 3 20 2.0513 - 2.0166 0.97 2579 139 0.2700 0.3274
REMARK 3 21 2.0166 - 1.9840 0.97 2609 127 0.2876 0.3005
REMARK 3 22 1.9840 - 1.9535 0.88 2347 131 0.3132 0.3496
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 34.91
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.890
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.61120
REMARK 3 B22 (A**2) : 4.62610
REMARK 3 B33 (A**2) : -4.01490
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.35770
REMARK 3 B23 (A**2) : 0.00000
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 : 0.009 6703
REMARK 3 ANGLE : 1.071 9036
REMARK 3 CHIRALITY : 0.073 976
REMARK 3 PLANARITY : 0.005 1148
REMARK 3 DIHEDRAL : 18.471 2507
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3WAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000096105.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-11
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 : SPRING-8
REMARK 200 BEAMLINE : BL32XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60998
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: 3NKM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG3350, 0.15M NACL, 0.5M KSCN,
REMARK 280 0.2MM ZNSO4, 1% POLYVINYLPYRROLIDONE, VAPOR DIFFUSION, SITTING
REMARK 280 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 47.13200
REMARK 290 SMTRY3 2 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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ALA A 36
REMARK 465 GLU A 37
REMARK 465 TRP A 38
REMARK 465 ASP A 39
REMARK 465 GLU A 40
REMARK 465 GLY A 41
REMARK 465 PRO A 42
REMARK 465 PRO A 43
REMARK 465 THR A 44
REMARK 465 VAL A 45
REMARK 465 LEU A 46
REMARK 465 SER A 47
REMARK 465 ASP A 48
REMARK 465 SER A 49
REMARK 465 PRO A 50
REMARK 465 LEU A 458
REMARK 465 ASP A 459
REMARK 465 VAL A 460
REMARK 465 TYR A 461
REMARK 465 LYS A 462
REMARK 465 LYS A 463
REMARK 465 PRO A 464
REMARK 465 SER A 465
REMARK 465 GLY A 466
REMARK 465 LYS A 467
REMARK 465 ASP A 570
REMARK 465 LYS A 571
REMARK 465 ASN A 572
REMARK 465 LYS A 573
REMARK 465 LEU A 574
REMARK 465 GLU A 575
REMARK 465 GLU A 576
REMARK 465 LEU A 577
REMARK 465 ASN A 578
REMARK 465 LYS A 579
REMARK 465 ARG A 580
REMARK 465 LEU A 581
REMARK 465 HIS A 582
REMARK 465 THR A 583
REMARK 465 LYS A 584
REMARK 465 GLY A 585
REMARK 465 SER A 856
REMARK 465 GLU A 857
REMARK 465 ILE A 858
REMARK 465 SER A 859
REMARK 465 ARG A 860
REMARK 465 GLU A 861
REMARK 465 ASN A 862
REMARK 465 LEU A 863
REMARK 465 TYR A 864
REMARK 465 PHE A 865
REMARK 465 GLN A 866
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 59 CG CD CE NZ
REMARK 470 GLU A 67 CG CD OE1 OE2
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 ARG A 244 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 246 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 549 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 559 CG CD OE1 NE2
REMARK 470 ASP A 569 CG OD1 OD2
REMARK 470 GLU A 589 CG CD OE1 OE2
REMARK 470 ARG A 602 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 642 CG CD OE1 OE2
REMARK 470 LYS A 666 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 PRO A 70 138.53 -39.15
REMARK 500 CYS A 75 18.39 -142.02
REMARK 500 LEU A 94 44.55 -106.18
REMARK 500 ARG A 111 109.12 -56.48
REMARK 500 ARG A 368 66.49 -109.28
REMARK 500 ALA A 435 -29.52 -153.71
REMARK 500 ARG A 450 -3.60 78.16
REMARK 500 ASP A 477 127.88 -33.70
REMARK 500 THR A 485 -168.97 -125.30
REMARK 500 MET A 556 -4.18 -143.28
REMARK 500 ASP A 563 74.28 -117.50
REMARK 500 SER A 672 -156.88 -107.46
REMARK 500 ARG A 742 123.81 -39.27
REMARK 500 SER A 755 -168.21 -124.02
REMARK 500 TRP A 810 -23.17 -150.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DWW A 937
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 912 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 171 OD1
REMARK 620 2 THR A 209 OG1 126.3
REMARK 620 3 ASP A 358 OD2 103.8 109.1
REMARK 620 4 HIS A 359 NE2 101.4 111.9 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 913 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 311 OD1
REMARK 620 2 ASP A 311 OD2 54.0
REMARK 620 3 HIS A 315 NE2 101.0 88.2
REMARK 620 4 HIS A 474 NE2 97.2 150.2 106.8
REMARK 620 5 SO4 A 917 O3 107.9 80.4 133.1 105.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 916 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 665 O
REMARK 620 2 ASP A 668 O 75.5
REMARK 620 3 MET A 671 O 92.2 71.5
REMARK 620 4 HOH A1372 O 83.3 152.8 92.9
REMARK 620 5 HOH A1373 O 174.7 100.1 83.6 100.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 914 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 735 OD1
REMARK 620 2 ASN A 737 OD1 82.9
REMARK 620 3 ASN A 739 OD1 81.4 87.6
REMARK 620 4 LEU A 741 O 91.7 170.9 84.3
REMARK 620 5 ASP A 743 OD1 98.7 83.8 171.3 104.4
REMARK 620 6 HOH A1327 O 166.9 92.3 86.3 91.4 92.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 915 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 797 O
REMARK 620 2 SER A 800 O 78.0
REMARK 620 3 SER A 803 OG 91.8 83.0
REMARK 620 4 HOH A1369 O 97.8 89.1 166.0
REMARK 620 5 HOH A1370 O 81.4 158.7 92.1 99.3
REMARK 620 6 HOH A1371 O 176.5 105.3 89.5 81.4 95.3
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WAV RELATED DB: PDB
REMARK 900 RELATED ID: 3WAX RELATED DB: PDB
REMARK 900 RELATED ID: 3WAY RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PROTEIN USED IN THIS STRUCTURE IS AN ISOFORM OF AUTOTAXIN FROM
REMARK 999 MOUSE, WHICH IS LACK OF RESIDUES KVEP (UNP RESDIUES 571-574 OF
REMARK 999 DATABASE ENPP2_MOUSE).
DBREF 3WAW A 36 858 UNP Q9R1E6 ENPP2_MOUSE 36 862
SEQADV 3WAW A UNP Q9R1E6 LYS 571 SEE REMARK 999
SEQADV 3WAW A UNP Q9R1E6 VAL 572 SEE REMARK 999
SEQADV 3WAW A UNP Q9R1E6 GLU 573 SEE REMARK 999
SEQADV 3WAW A UNP Q9R1E6 PRO 574 SEE REMARK 999
SEQADV 3WAW SER A 859 UNP Q9R1E6 EXPRESSION TAG
SEQADV 3WAW ARG A 860 UNP Q9R1E6 EXPRESSION TAG
SEQADV 3WAW GLU A 861 UNP Q9R1E6 EXPRESSION TAG
SEQADV 3WAW ASN A 862 UNP Q9R1E6 EXPRESSION TAG
SEQADV 3WAW LEU A 863 UNP Q9R1E6 EXPRESSION TAG
SEQADV 3WAW TYR A 864 UNP Q9R1E6 EXPRESSION TAG
SEQADV 3WAW PHE A 865 UNP Q9R1E6 EXPRESSION TAG
SEQADV 3WAW GLN A 866 UNP Q9R1E6 EXPRESSION TAG
SEQRES 1 A 831 ALA GLU TRP ASP GLU GLY PRO PRO THR VAL LEU SER ASP
SEQRES 2 A 831 SER PRO TRP THR ASN THR SER GLY SER CYS LYS GLY ARG
SEQRES 3 A 831 CYS PHE GLU LEU GLN GLU VAL GLY PRO PRO ASP CYS ARG
SEQRES 4 A 831 CYS ASP ASN LEU CYS LYS SER TYR SER SER CYS CYS HIS
SEQRES 5 A 831 ASP PHE ASP GLU LEU CYS LEU LYS THR ALA ARG GLY TRP
SEQRES 6 A 831 GLU CYS THR LYS ASP ARG CYS GLY GLU VAL ARG ASN GLU
SEQRES 7 A 831 GLU ASN ALA CYS HIS CYS SER GLU ASP CYS LEU SER ARG
SEQRES 8 A 831 GLY ASP CYS CYS THR ASN TYR GLN VAL VAL CYS LYS GLY
SEQRES 9 A 831 GLU SER HIS TRP VAL ASP ASP ASP CYS GLU GLU ILE ARG
SEQRES 10 A 831 VAL PRO GLU CYS PRO ALA GLY PHE VAL ARG PRO PRO LEU
SEQRES 11 A 831 ILE ILE PHE SER VAL ASP GLY PHE ARG ALA SER TYR MET
SEQRES 12 A 831 LYS LYS GLY SER LYS VAL MET PRO ASN ILE GLU LYS LEU
SEQRES 13 A 831 ARG SER CYS GLY THR HIS ALA PRO TYR MET ARG PRO VAL
SEQRES 14 A 831 TYR PRO THR LYS THR PHE PRO ASN LEU TYR THR LEU ALA
SEQRES 15 A 831 THR GLY LEU TYR PRO GLU SER HIS GLY ILE VAL GLY ASN
SEQRES 16 A 831 SER MET TYR ASP PRO VAL PHE ASP ALA THR PHE HIS LEU
SEQRES 17 A 831 ARG GLY ARG GLU LYS PHE ASN HIS ARG TRP TRP GLY GLY
SEQRES 18 A 831 GLN PRO LEU TRP ILE THR ALA THR LYS GLN GLY VAL ARG
SEQRES 19 A 831 ALA GLY THR PHE PHE TRP SER VAL SER ILE PRO HIS GLU
SEQRES 20 A 831 ARG ARG ILE LEU THR ILE LEU GLN TRP LEU SER LEU PRO
SEQRES 21 A 831 ASP ASN GLU ARG PRO SER VAL TYR ALA PHE TYR SER GLU
SEQRES 22 A 831 GLN PRO ASP PHE SER GLY HIS LYS TYR GLY PRO PHE GLY
SEQRES 23 A 831 PRO GLU MET THR ASN PRO LEU ARG GLU ILE ASP LYS THR
SEQRES 24 A 831 VAL GLY GLN LEU MET ASP GLY LEU LYS GLN LEU LYS LEU
SEQRES 25 A 831 HIS ARG CYS VAL ASN VAL ILE PHE VAL GLY ASP HIS GLY
SEQRES 26 A 831 MET GLU ASP VAL THR CYS ASP ARG THR GLU PHE LEU SER
SEQRES 27 A 831 ASN TYR LEU THR ASN VAL ASP ASP ILE THR LEU VAL PRO
SEQRES 28 A 831 GLY THR LEU GLY ARG ILE ARG PRO LYS ILE PRO ASN ASN
SEQRES 29 A 831 LEU LYS TYR ASP PRO LYS ALA ILE ILE ALA ASN LEU THR
SEQRES 30 A 831 CYS LYS LYS PRO ASP GLN HIS PHE LYS PRO TYR MET LYS
SEQRES 31 A 831 GLN HIS LEU PRO LYS ARG LEU HIS TYR ALA ASN ASN ARG
SEQRES 32 A 831 ARG ILE GLU ASP LEU HIS LEU LEU VAL GLU ARG ARG TRP
SEQRES 33 A 831 HIS VAL ALA ARG LYS PRO LEU ASP VAL TYR LYS LYS PRO
SEQRES 34 A 831 SER GLY LYS CYS PHE PHE GLN GLY ASP HIS GLY PHE ASP
SEQRES 35 A 831 ASN LYS VAL ASN SER MET GLN THR VAL PHE VAL GLY TYR
SEQRES 36 A 831 GLY PRO THR PHE LYS TYR ARG THR LYS VAL PRO PRO PHE
SEQRES 37 A 831 GLU ASN ILE GLU LEU TYR ASN VAL MET CYS ASP LEU LEU
SEQRES 38 A 831 GLY LEU LYS PRO ALA PRO ASN ASN GLY THR HIS GLY SER
SEQRES 39 A 831 LEU ASN HIS LEU LEU ARG THR ASN THR PHE ARG PRO THR
SEQRES 40 A 831 LEU PRO GLU GLU VAL SER ARG PRO ASN TYR PRO GLY ILE
SEQRES 41 A 831 MET TYR LEU GLN SER ASP PHE ASP LEU GLY CYS THR CYS
SEQRES 42 A 831 ASP ASP LYS ASN LYS LEU GLU GLU LEU ASN LYS ARG LEU
SEQRES 43 A 831 HIS THR LYS GLY SER THR GLU GLU ARG HIS LEU LEU TYR
SEQRES 44 A 831 GLY ARG PRO ALA VAL LEU TYR ARG THR SER TYR ASP ILE
SEQRES 45 A 831 LEU TYR HIS THR ASP PHE GLU SER GLY TYR SER GLU ILE
SEQRES 46 A 831 PHE LEU MET PRO LEU TRP THR SER TYR THR ILE SER LYS
SEQRES 47 A 831 GLN ALA GLU VAL SER SER ILE PRO GLU HIS LEU THR ASN
SEQRES 48 A 831 CYS VAL ARG PRO ASP VAL ARG VAL SER PRO GLY PHE SER
SEQRES 49 A 831 GLN ASN CYS LEU ALA TYR LYS ASN ASP LYS GLN MET SER
SEQRES 50 A 831 TYR GLY PHE LEU PHE PRO PRO TYR LEU SER SER SER PRO
SEQRES 51 A 831 GLU ALA LYS TYR ASP ALA PHE LEU VAL THR ASN MET VAL
SEQRES 52 A 831 PRO MET TYR PRO ALA PHE LYS ARG VAL TRP THR TYR PHE
SEQRES 53 A 831 GLN ARG VAL LEU VAL LYS LYS TYR ALA SER GLU ARG ASN
SEQRES 54 A 831 GLY VAL ASN VAL ILE SER GLY PRO ILE PHE ASP TYR ASN
SEQRES 55 A 831 TYR ASN GLY LEU ARG ASP ILE GLU ASP GLU ILE LYS GLN
SEQRES 56 A 831 TYR VAL GLU GLY SER SER ILE PRO VAL PRO THR HIS TYR
SEQRES 57 A 831 TYR SER ILE ILE THR SER CYS LEU ASP PHE THR GLN PRO
SEQRES 58 A 831 ALA ASP LYS CYS ASP GLY PRO LEU SER VAL SER SER PHE
SEQRES 59 A 831 ILE LEU PRO HIS ARG PRO ASP ASN ASP GLU SER CYS ASN
SEQRES 60 A 831 SER SER GLU ASP GLU SER LYS TRP VAL GLU GLU LEU MET
SEQRES 61 A 831 LYS MET HIS THR ALA ARG VAL ARG ASP ILE GLU HIS LEU
SEQRES 62 A 831 THR GLY LEU ASP PHE TYR ARG LYS THR SER ARG SER TYR
SEQRES 63 A 831 SER GLU ILE LEU THR LEU LYS THR TYR LEU HIS THR TYR
SEQRES 64 A 831 GLU SER GLU ILE SER ARG GLU ASN LEU TYR PHE GLN
MODRES 3WAW ASN A 524 ASN GLYCOSYLATION SITE
MODRES 3WAW ASN A 410 ASN GLYCOSYLATION SITE
MODRES 3WAW ASN A 53 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET MAN C 6 11
HET MAN C 7 11
HET NAG D 1 14
HET NAG D 2 14
HET ZN A 912 1
HET ZN A 913 1
HET CA A 914 1
HET NA A 915 1
HET K A 916 1
HET SO4 A 917 5
HET SCN A 918 3
HET SCN A 919 3
HET SCN A 920 3
HET EDO A 921 4
HET EDO A 922 4
HET EDO A 923 4
HET EDO A 924 4
HET EDO A 925 4
HET EDO A 926 4
HET EDO A 927 4
HET EDO A 928 4
HET EDO A 929 4
HET EDO A 930 4
HET EDO A 931 4
HET EDO A 932 4
HET EDO A 933 4
HET EDO A 934 4
HET EDO A 935 4
HET EDO A 936 4
HET DWW A 937 23
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM K POTASSIUM ION
HETNAM SO4 SULFATE ION
HETNAM SCN THIOCYANATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DWW [2-({4-[(5Z)-5-(3,4-DICHLOROBENZYLIDENE)-4-OXO-4,5-
HETNAM 2 DWW DIHYDRO-1,3-THIAZOL-2-YL]PIPERAZIN-1-YL}METHYL)
HETNAM 3 DWW PHENYL]BORONIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG 6(C8 H15 N O6)
FORMUL 3 BMA C6 H12 O6
FORMUL 3 MAN 4(C6 H12 O6)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 CA CA 2+
FORMUL 8 NA NA 1+
FORMUL 9 K K 1+
FORMUL 10 SO4 O4 S 2-
FORMUL 11 SCN 3(C N S 1-)
FORMUL 14 EDO 16(C2 H6 O2)
FORMUL 30 DWW C21 H20 B CL2 N3 O3 S
FORMUL 31 HOH *373(H2 O)
HELIX 1 1 CYS A 79 SER A 83 5 5
HELIX 2 2 ASP A 88 LEU A 94 1 7
HELIX 3 3 THR A 103 CYS A 107 5 5
HELIX 4 4 ASP A 122 GLY A 127 1 6
HELIX 5 5 ASN A 132 GLY A 139 1 8
HELIX 6 6 HIS A 142 ASP A 146 5 5
HELIX 7 7 ARG A 174 LYS A 179 5 6
HELIX 8 8 LYS A 180 MET A 185 1 6
HELIX 9 9 MET A 185 GLY A 195 1 11
HELIX 10 10 LYS A 208 GLY A 219 1 12
HELIX 11 11 TYR A 221 GLY A 226 1 6
HELIX 12 12 ARG A 246 TRP A 254 5 9
HELIX 13 13 PRO A 258 GLN A 266 1 9
HELIX 14 14 PRO A 280 SER A 293 1 14
HELIX 15 15 ASP A 311 GLY A 318 1 8
HELIX 16 16 GLY A 321 GLU A 323 5 3
HELIX 17 17 MET A 324 LEU A 345 1 22
HELIX 18 18 SER A 373 TYR A 375 5 3
HELIX 19 19 ASN A 378 ASP A 380 5 3
HELIX 20 20 ASP A 403 THR A 412 1 10
HELIX 21 21 GLN A 426 LEU A 428 5 3
HELIX 22 22 PRO A 429 HIS A 433 5 5
HELIX 23 23 VAL A 480 GLN A 484 5 5
HELIX 24 24 GLU A 507 GLY A 517 1 11
HELIX 25 25 LEU A 530 LEU A 534 5 5
HELIX 26 26 LEU A 558 PHE A 562 5 5
HELIX 27 27 THR A 587 LEU A 592 1 6
HELIX 28 28 PRO A 641 THR A 645 5 5
HELIX 29 29 SER A 655 SER A 659 5 5
HELIX 30 30 ASN A 661 ASP A 668 1 8
HELIX 31 31 PRO A 678 SER A 682 5 5
HELIX 32 32 SER A 684 PHE A 692 1 9
HELIX 33 33 TYR A 701 VAL A 714 1 14
HELIX 34 34 VAL A 714 ARG A 723 1 10
HELIX 35 35 ILE A 744 ILE A 748 5 5
HELIX 36 36 PRO A 776 CYS A 780 5 5
HELIX 37 37 ASP A 806 LYS A 809 5 4
HELIX 38 38 TRP A 810 HIS A 818 1 9
HELIX 39 39 ARG A 821 GLY A 830 1 10
HELIX 40 40 SER A 840 TYR A 850 1 11
SHEET 1 A 6 VAL A 302 PRO A 310 0
SHEET 2 A 6 LEU A 165 ASP A 171 1 N ILE A 167 O TYR A 303
SHEET 3 A 6 ASN A 352 GLY A 357 1 O ILE A 354 N PHE A 168
SHEET 4 A 6 PHE A 487 TYR A 490 -1 O TYR A 490 N VAL A 353
SHEET 5 A 6 THR A 196 HIS A 197 -1 N THR A 196 O GLY A 489
SHEET 6 A 6 THR A 498 LYS A 499 1 O THR A 498 N HIS A 197
SHEET 1 B 2 MET A 201 ARG A 202 0
SHEET 2 B 2 PHE A 503 GLU A 504 1 O PHE A 503 N ARG A 202
SHEET 1 C 2 MET A 232 ASP A 234 0
SHEET 2 C 2 ALA A 239 PHE A 241 -1 O PHE A 241 N MET A 232
SHEET 1 D 2 GLU A 362 ASP A 363 0
SHEET 2 D 2 GLY A 472 ASP A 473 -1 O ASP A 473 N GLU A 362
SHEET 1 E 2 THR A 369 PHE A 371 0
SHEET 2 E 2 HIS A 452 ALA A 454 1 O HIS A 452 N GLU A 370
SHEET 1 F 4 ILE A 382 VAL A 385 0
SHEET 2 F 4 LEU A 389 PRO A 394 -1 O ARG A 391 N VAL A 385
SHEET 3 F 4 LEU A 443 VAL A 447 -1 O LEU A 445 N GLY A 390
SHEET 4 F 4 PHE A 420 MET A 424 -1 N TYR A 423 O HIS A 444
SHEET 1 G 2 ALA A 598 VAL A 599 0
SHEET 2 G 2 LEU A 831 ASP A 832 -1 O ASP A 832 N ALA A 598
SHEET 1 H 7 TYR A 605 TYR A 609 0
SHEET 2 H 7 GLU A 614 SER A 618 -1 O TYR A 617 N ASP A 606
SHEET 3 H 7 PRO A 624 ILE A 631 -1 O SER A 628 N GLU A 614
SHEET 4 H 7 VAL A 726 ILE A 733 -1 O VAL A 728 N TYR A 629
SHEET 5 H 7 HIS A 762 CYS A 770 -1 O THR A 768 N ASN A 727
SHEET 6 H 7 LEU A 784 PRO A 792 -1 O SER A 787 N ILE A 767
SHEET 7 H 7 THR A 819 ALA A 820 -1 O ALA A 820 N SER A 788
SHEET 1 I 2 SER A 672 PHE A 675 0
SHEET 2 I 2 MET A 697 MET A 700 -1 O VAL A 698 N GLY A 674
SSBOND 1 CYS A 58 CYS A 75 1555 1555 2.03
SSBOND 2 CYS A 62 CYS A 93 1555 1555 2.03
SSBOND 3 CYS A 73 CYS A 86 1555 1555 2.04
SSBOND 4 CYS A 79 CYS A 85 1555 1555 2.04
SSBOND 5 CYS A 102 CYS A 119 1555 1555 2.04
SSBOND 6 CYS A 107 CYS A 137 1555 1555 2.04
SSBOND 7 CYS A 117 CYS A 130 1555 1555 2.04
SSBOND 8 CYS A 123 CYS A 129 1555 1555 2.04
SSBOND 9 CYS A 148 CYS A 194 1555 1555 2.03
SSBOND 10 CYS A 156 CYS A 350 1555 1555 2.02
SSBOND 11 CYS A 366 CYS A 468 1555 1555 2.04
SSBOND 12 CYS A 413 CYS A 801 1555 1555 2.04
SSBOND 13 CYS A 566 CYS A 662 1555 1555 2.04
SSBOND 14 CYS A 568 CYS A 647 1555 1555 2.04
SSBOND 15 CYS A 770 CYS A 780 1555 1555 2.03
LINK ND2 ASN A 53 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 410 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 524 C1 NAG C 1 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O6 BMA C 3 C1 MAN C 4 1555 1555 1.45
LINK O3 BMA C 3 C1 MAN C 7 1555 1555 1.44
LINK O3 MAN C 4 C1 MAN C 5 1555 1555 1.44
LINK O2 MAN C 5 C1 MAN C 6 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK OD1 ASP A 171 ZN ZN A 912 1555 1555 1.97
LINK OG1 THR A 209 ZN ZN A 912 1555 1555 2.02
LINK OD1 ASP A 311 ZN ZN A 913 1555 1555 2.20
LINK OD2 ASP A 311 ZN ZN A 913 1555 1555 2.56
LINK NE2 HIS A 315 ZN ZN A 913 1555 1555 2.00
LINK OD2 ASP A 358 ZN ZN A 912 1555 1555 2.16
LINK NE2 HIS A 359 ZN ZN A 912 1555 1555 2.14
LINK NE2 HIS A 474 ZN ZN A 913 1555 1555 1.97
LINK O TYR A 665 K K A 916 1555 1555 2.58
LINK O ASP A 668 K K A 916 1555 1555 2.64
LINK O MET A 671 K K A 916 1555 1555 2.82
LINK OD1 ASP A 735 CA CA A 914 1555 1555 2.38
LINK OD1 ASN A 737 CA CA A 914 1555 1555 2.34
LINK OD1 ASN A 739 CA CA A 914 1555 1555 2.42
LINK O LEU A 741 CA CA A 914 1555 1555 2.36
LINK OD1 ASP A 743 CA CA A 914 1555 1555 2.23
LINK O ASN A 797 NA NA A 915 1555 1555 2.55
LINK O SER A 800 NA NA A 915 1555 1555 2.41
LINK OG SER A 803 NA NA A 915 1555 1555 2.28
LINK ZN ZN A 913 O3 SO4 A 917 1555 1555 2.24
LINK CA CA A 914 O HOH A1327 1555 1555 2.42
LINK NA NA A 915 O HOH A1369 1555 1555 2.42
LINK NA NA A 915 O HOH A1370 1555 1555 2.40
LINK NA NA A 915 O HOH A1371 1555 1555 2.51
LINK K K A 916 O HOH A1372 1555 1555 2.93
LINK K K A 916 O HOH A1373 1555 1555 2.96
CISPEP 1 PRO A 70 PRO A 71 0 9.24
CISPEP 2 TYR A 205 PRO A 206 0 -2.06
CISPEP 3 GLN A 309 PRO A 310 0 5.44
CRYST1 61.648 94.264 75.358 90.00 94.73 90.00 P 1 21 1 2
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 0.016221 0.000000 0.001342 0.00000
SCALE2 0.000000 0.010609 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END