HEADER HYDROLASE 17-JUL-17 5OHI
TITLE CRYSTAL STRUCTURE OF AUTOTAXIN IN COMPLEX WITH BI-2545
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE FAMILY
COMPND 3 MEMBER 2;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: E-NPP 2,AUTOTAXIN,EXTRACELLULAR LYSOPHOSPHOLIPASE D,LYSOPLD;
COMPND 6 EC: 3.1.4.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ENPP2, NPPS2, PDNP2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293 GNT1;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDNA5/FRT
KEYWDS PHOSPHOLIPASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HOERER
REVDAT 4 17-JAN-24 5OHI 1 HETSYN
REVDAT 3 29-JUL-20 5OHI 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 03-OCT-18 5OHI 1 COMPND REMARK HET HETNAM
REVDAT 2 2 1 HETSYN FORMUL LINK SITE
REVDAT 2 3 1 ATOM
REVDAT 1 03-JAN-18 5OHI 0
JRNL AUTH C.A.KUTTRUFF,M.FERRARA,T.BRETSCHNEIDER,S.HOERER,S.HANDSCHUH,
JRNL AUTH 2 B.NOSSE,H.ROMIG,P.NICKLIN,G.J.ROTH
JRNL TITL DISCOVERY OF BI-2545: A NOVEL AUTOTAXIN INHIBITOR THAT
JRNL TITL 2 SIGNIFICANTLY REDUCES LPA LEVELS IN VIVO.
JRNL REF ACS MED CHEM LETT V. 8 1252 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 29259743
JRNL DOI 10.1021/ACSMEDCHEMLETT.7B00312
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 68.8
REMARK 3 NUMBER OF REFLECTIONS : 68935
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810
REMARK 3 FREE R VALUE TEST SET COUNT : 3319
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 1.89
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 188
REMARK 3 BIN R VALUE (WORKING SET) : 0.3176
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.33
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 11
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 : 6299
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 200
REMARK 3 SOLVENT ATOMS : 563
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42030
REMARK 3 B22 (A**2) : 1.67950
REMARK 3 B33 (A**2) : -1.25920
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.25310
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.220
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.137
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.118
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.133
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.117
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 : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6760 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9206 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2356 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 153 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 964 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6760 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 874 ; 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 : 8185 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.96
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.38
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.02
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2298 -23.1583 35.6996
REMARK 3 T TENSOR
REMARK 3 T11: -0.1390 T22: -0.1415
REMARK 3 T33: -0.1355 T12: 0.0078
REMARK 3 T13: -0.0207 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.0749 L22: 0.6942
REMARK 3 L33: 1.0349 L12: 0.3340
REMARK 3 L13: -0.2052 L23: -0.0408
REMARK 3 S TENSOR
REMARK 3 S11: -0.0834 S12: 0.0310 S13: -0.0140
REMARK 3 S21: -0.1099 S22: 0.0554 S23: 0.0463
REMARK 3 S31: 0.0419 S32: 0.0171 S33: 0.0280
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90996
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS MAY 1 2016
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 1.1.7, AIMLESS 0.5.31
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98475
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 75.417
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 69.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 2.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 3.33400
REMARK 200 R SYM FOR SHELL (I) : 3.99500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.390
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 3NKM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 %W/V POLYVINYLPYROLIDINE (PVP K15)21
REMARK 280 %W/V POLYETHYLENE GLYCOL 3,350, 0.2 M ZNSO4, 0.5 M KSCN AND 0.1
REMARK 280 M BIS-TRIS AT PH8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 46.88950
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 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 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 569
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 586
REMARK 465 THR A 587
REMARK 465 SER A 856
REMARK 465 GLU A 857
REMARK 465 ILE A 858
REMARK 465 GLU A 859
REMARK 465 ASN A 860
REMARK 465 LEU A 861
REMARK 465 TYR A 862
REMARK 465 PHE A 863
REMARK 465 GLN A 864
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 94 60.83 -114.85
REMARK 500 ARG A 244 65.66 -119.20
REMARK 500 ARG A 368 62.13 -110.43
REMARK 500 PRO A 397 -62.14 -29.43
REMARK 500 ASN A 398 55.93 -107.75
REMARK 500 ASP A 403 77.18 -107.96
REMARK 500 ALA A 435 -36.38 -151.38
REMARK 500 ARG A 450 -4.43 84.43
REMARK 500 ASP A 477 126.81 -33.63
REMARK 500 ARG A 497 51.80 39.64
REMARK 500 LEU A 592 77.15 -114.31
REMARK 500 VAL A 652 -8.68 -59.68
REMARK 500 SER A 672 -160.03 -115.94
REMARK 500 ASN A 724 61.19 64.59
REMARK 500 LYS A 779 56.54 -146.57
REMARK 500 TRP A 810 -26.08 -148.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1562 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH A1563 DISTANCE = 9.53 ANGSTROMS
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 913 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 171 OD1
REMARK 620 2 ASP A 358 OD2 98.9
REMARK 620 3 HIS A 359 NE2 106.2 97.7
REMARK 620 4 HOH A1002 O 80.4 172.6 75.5
REMARK 620 N 1 2 3
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 311 OD1
REMARK 620 2 ASP A 311 OD2 56.2
REMARK 620 3 HIS A 315 NE2 102.4 91.2
REMARK 620 4 HIS A 474 NE2 95.9 151.9 98.8
REMARK 620 5 9V8 A 920 N29 136.8 92.4 107.5 109.3
REMARK 620 6 HOH A1002 O 71.9 86.2 174.3 81.4 77.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 919 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 374 O
REMARK 620 2 P3G A 917 O3 122.3
REMARK 620 3 P3G A 917 O3 118.2 9.3
REMARK 620 4 P3G A 917 O4 83.7 61.6 67.6
REMARK 620 5 P3G A 917 O4 89.3 53.1 59.1 8.5
REMARK 620 6 P3G A 917 O5 65.8 119.3 126.8 60.0 68.2
REMARK 620 7 P3G A 917 O5 77.6 106.0 114.1 50.3 57.8 14.7
REMARK 620 8 P3G A 917 O6 86.0 149.4 155.6 116.1 123.1 58.3 65.9
REMARK 620 9 HOH A1059 O 160.3 65.9 72.4 85.9 82.5 94.5 82.8 83.6
REMARK 620 N 1 2 3 4 5 6 7 8
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 88.2
REMARK 620 3 MET A 671 O 96.6 69.0
REMARK 620 4 HOH A1453 O 75.1 154.3 93.2
REMARK 620 5 HOH A1480 O 169.9 95.6 76.3 97.9
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 88.9
REMARK 620 3 ASN A 739 OD1 80.9 81.9
REMARK 620 4 LEU A 741 O 88.1 163.9 81.9
REMARK 620 5 ASP A 743 OD1 97.3 89.7 171.5 106.4
REMARK 620 6 HOH A1134 O 169.5 91.9 88.8 88.3 93.1
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 70.7
REMARK 620 3 SER A 803 OG 84.7 77.1
REMARK 620 4 HOH A1302 O 98.6 95.9 170.9
REMARK 620 5 HOH A1322 O 83.4 153.5 95.4 93.4
REMARK 620 6 HOH A1444 O 165.6 110.1 81.6 95.6 93.5
REMARK 620 N 1 2 3 4 5
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PROTEIN USED IN THIS STRUCTURE IS AN ISOFORM OF ANTOTAXIN FROM
REMARK 999 MOUSE, WHICH IS LACK OF RESIDUES KVEP (UNP RESDIUES 571-574 OF
REMARK 999 DATABASE ENPP2_MOUSE).
DBREF 5OHI A 36 858 UNP Q9R1E6 ENPP2_MOUSE 36 862
SEQADV 5OHI A UNP Q9R1E6 LYS 571 DELETION
SEQADV 5OHI A UNP Q9R1E6 VAL 572 DELETION
SEQADV 5OHI A UNP Q9R1E6 GLU 573 DELETION
SEQADV 5OHI A UNP Q9R1E6 PRO 574 DELETION
SEQADV 5OHI GLU A 859 UNP Q9R1E6 EXPRESSION TAG
SEQADV 5OHI ASN A 860 UNP Q9R1E6 EXPRESSION TAG
SEQADV 5OHI LEU A 861 UNP Q9R1E6 EXPRESSION TAG
SEQADV 5OHI TYR A 862 UNP Q9R1E6 EXPRESSION TAG
SEQADV 5OHI PHE A 863 UNP Q9R1E6 EXPRESSION TAG
SEQADV 5OHI GLN A 864 UNP Q9R1E6 EXPRESSION TAG
SEQRES 1 A 829 ALA GLU TRP ASP GLU GLY PRO PRO THR VAL LEU SER ASP
SEQRES 2 A 829 SER PRO TRP THR ASN THR SER GLY SER CYS LYS GLY ARG
SEQRES 3 A 829 CYS PHE GLU LEU GLN GLU VAL GLY PRO PRO ASP CYS ARG
SEQRES 4 A 829 CYS ASP ASN LEU CYS LYS SER TYR SER SER CYS CYS HIS
SEQRES 5 A 829 ASP PHE ASP GLU LEU CYS LEU LYS THR ALA ARG GLY TRP
SEQRES 6 A 829 GLU CYS THR LYS ASP ARG CYS GLY GLU VAL ARG ASN GLU
SEQRES 7 A 829 GLU ASN ALA CYS HIS CYS SER GLU ASP CYS LEU SER ARG
SEQRES 8 A 829 GLY ASP CYS CYS THR ASN TYR GLN VAL VAL CYS LYS GLY
SEQRES 9 A 829 GLU SER HIS TRP VAL ASP ASP ASP CYS GLU GLU ILE ARG
SEQRES 10 A 829 VAL PRO GLU CYS PRO ALA GLY PHE VAL ARG PRO PRO LEU
SEQRES 11 A 829 ILE ILE PHE SER VAL ASP GLY PHE ARG ALA SER TYR MET
SEQRES 12 A 829 LYS LYS GLY SER LYS VAL MET PRO ASN ILE GLU LYS LEU
SEQRES 13 A 829 ARG SER CYS GLY THR HIS ALA PRO TYR MET ARG PRO VAL
SEQRES 14 A 829 TYR PRO THR LYS THR PHE PRO ASN LEU TYR THR LEU ALA
SEQRES 15 A 829 THR GLY LEU TYR PRO GLU SER HIS GLY ILE VAL GLY ASN
SEQRES 16 A 829 SER MET TYR ASP PRO VAL PHE ASP ALA THR PHE HIS LEU
SEQRES 17 A 829 ARG GLY ARG GLU LYS PHE ASN HIS ARG TRP TRP GLY GLY
SEQRES 18 A 829 GLN PRO LEU TRP ILE THR ALA THR LYS GLN GLY VAL ARG
SEQRES 19 A 829 ALA GLY THR PHE PHE TRP SER VAL SER ILE PRO HIS GLU
SEQRES 20 A 829 ARG ARG ILE LEU THR ILE LEU GLN TRP LEU SER LEU PRO
SEQRES 21 A 829 ASP ASN GLU ARG PRO SER VAL TYR ALA PHE TYR SER GLU
SEQRES 22 A 829 GLN PRO ASP PHE SER GLY HIS LYS TYR GLY PRO PHE GLY
SEQRES 23 A 829 PRO GLU MET THR ASN PRO LEU ARG GLU ILE ASP LYS THR
SEQRES 24 A 829 VAL GLY GLN LEU MET ASP GLY LEU LYS GLN LEU LYS LEU
SEQRES 25 A 829 HIS ARG CYS VAL ASN VAL ILE PHE VAL GLY ASP HIS GLY
SEQRES 26 A 829 MET GLU ASP VAL THR CYS ASP ARG THR GLU PHE LEU SER
SEQRES 27 A 829 ASN TYR LEU THR ASN VAL ASP ASP ILE THR LEU VAL PRO
SEQRES 28 A 829 GLY THR LEU GLY ARG ILE ARG PRO LYS ILE PRO ASN ASN
SEQRES 29 A 829 LEU LYS TYR ASP PRO LYS ALA ILE ILE ALA ASN LEU THR
SEQRES 30 A 829 CYS LYS LYS PRO ASP GLN HIS PHE LYS PRO TYR MET LYS
SEQRES 31 A 829 GLN HIS LEU PRO LYS ARG LEU HIS TYR ALA ASN ASN ARG
SEQRES 32 A 829 ARG ILE GLU ASP LEU HIS LEU LEU VAL GLU ARG ARG TRP
SEQRES 33 A 829 HIS VAL ALA ARG LYS PRO LEU ASP VAL TYR LYS LYS PRO
SEQRES 34 A 829 SER GLY LYS CYS PHE PHE GLN GLY ASP HIS GLY PHE ASP
SEQRES 35 A 829 ASN LYS VAL ASN SER MET GLN THR VAL PHE VAL GLY TYR
SEQRES 36 A 829 GLY PRO THR PHE LYS TYR ARG THR LYS VAL PRO PRO PHE
SEQRES 37 A 829 GLU ASN ILE GLU LEU TYR ASN VAL MET CYS ASP LEU LEU
SEQRES 38 A 829 GLY LEU LYS PRO ALA PRO ASN ASN GLY THR HIS GLY SER
SEQRES 39 A 829 LEU ASN HIS LEU LEU ARG THR ASN THR PHE ARG PRO THR
SEQRES 40 A 829 LEU PRO GLU GLU VAL SER ARG PRO ASN TYR PRO GLY ILE
SEQRES 41 A 829 MET TYR LEU GLN SER ASP PHE ASP LEU GLY CYS THR CYS
SEQRES 42 A 829 ASP ASP LYS ASN LYS LEU GLU GLU LEU ASN LYS ARG LEU
SEQRES 43 A 829 HIS THR LYS GLY SER THR GLU GLU ARG HIS LEU LEU TYR
SEQRES 44 A 829 GLY ARG PRO ALA VAL LEU TYR ARG THR SER TYR ASP ILE
SEQRES 45 A 829 LEU TYR HIS THR ASP PHE GLU SER GLY TYR SER GLU ILE
SEQRES 46 A 829 PHE LEU MET PRO LEU TRP THR SER TYR THR ILE SER LYS
SEQRES 47 A 829 GLN ALA GLU VAL SER SER ILE PRO GLU HIS LEU THR ASN
SEQRES 48 A 829 CYS VAL ARG PRO ASP VAL ARG VAL SER PRO GLY PHE SER
SEQRES 49 A 829 GLN ASN CYS LEU ALA TYR LYS ASN ASP LYS GLN MET SER
SEQRES 50 A 829 TYR GLY PHE LEU PHE PRO PRO TYR LEU SER SER SER PRO
SEQRES 51 A 829 GLU ALA LYS TYR ASP ALA PHE LEU VAL THR ASN MET VAL
SEQRES 52 A 829 PRO MET TYR PRO ALA PHE LYS ARG VAL TRP THR TYR PHE
SEQRES 53 A 829 GLN ARG VAL LEU VAL LYS LYS TYR ALA SER GLU ARG ASN
SEQRES 54 A 829 GLY VAL ASN VAL ILE SER GLY PRO ILE PHE ASP TYR ASN
SEQRES 55 A 829 TYR ASN GLY LEU ARG ASP ILE GLU ASP GLU ILE LYS GLN
SEQRES 56 A 829 TYR VAL GLU GLY SER SER ILE PRO VAL PRO THR HIS TYR
SEQRES 57 A 829 TYR SER ILE ILE THR SER CYS LEU ASP PHE THR GLN PRO
SEQRES 58 A 829 ALA ASP LYS CYS ASP GLY PRO LEU SER VAL SER SER PHE
SEQRES 59 A 829 ILE LEU PRO HIS ARG PRO ASP ASN ASP GLU SER CYS ASN
SEQRES 60 A 829 SER SER GLU ASP GLU SER LYS TRP VAL GLU GLU LEU MET
SEQRES 61 A 829 LYS MET HIS THR ALA ARG VAL ARG ASP ILE GLU HIS LEU
SEQRES 62 A 829 THR GLY LEU ASP PHE TYR ARG LYS THR SER ARG SER TYR
SEQRES 63 A 829 SER GLU ILE LEU THR LEU LYS THR TYR LEU HIS THR TYR
SEQRES 64 A 829 GLU SER GLU ILE GLU ASN LEU TYR PHE GLN
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET MAN D 6 11
HET MAN D 7 11
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 P3G A 917 34
HET CL A 918 1
HET CA A 919 1
HET 9V8 A 920 37
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 P3G 3,6,9,12,15-PENTAOXAHEPTADECANE
HETNAM CL CHLORIDE ION
HETNAM 9V8 [3,5-BIS(TRIFLUOROMETHYL)PHENYL]METHYL (1~{S},5~{R})-6-
HETNAM 2 9V8 [(1~{H}-BENZOTRIAZOL-5-YLCARBONYLAMINO)METHYL]-3-
HETNAM 3 9V8 AZABICYCLO[3.1.0]HEXANE-3-CARBOXYLATE
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
FORMUL 2 NAG 6(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN 4(C6 H12 O6)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 CA 2(CA 2+)
FORMUL 8 NA NA 1+
FORMUL 9 K K 1+
FORMUL 10 P3G C12 H26 O5
FORMUL 11 CL CL 1-
FORMUL 13 9V8 C23 H19 F6 N5 O3
FORMUL 14 HOH *563(H2 O)
HELIX 1 AA1 ASP A 76 LYS A 80 5 5
HELIX 2 AA2 ASP A 88 LEU A 94 1 7
HELIX 3 AA3 THR A 103 CYS A 107 5 5
HELIX 4 AA4 ASP A 122 GLY A 127 1 6
HELIX 5 AA5 ASN A 132 GLY A 139 1 8
HELIX 6 AA6 HIS A 142 ASP A 146 5 5
HELIX 7 AA7 ARG A 174 VAL A 184 5 11
HELIX 8 AA8 MET A 185 GLY A 195 1 11
HELIX 9 AA9 LYS A 208 GLY A 219 1 12
HELIX 10 AB1 TYR A 221 GLY A 226 1 6
HELIX 11 AB2 ARG A 246 TRP A 254 5 9
HELIX 12 AB3 PRO A 258 GLN A 266 1 9
HELIX 13 AB4 PRO A 280 SER A 293 1 14
HELIX 14 AB5 ASP A 311 GLY A 318 1 8
HELIX 15 AB6 GLY A 321 GLU A 323 5 3
HELIX 16 AB7 MET A 324 LEU A 345 1 22
HELIX 17 AB8 SER A 373 TYR A 375 5 3
HELIX 18 AB9 ASP A 403 THR A 412 1 10
HELIX 19 AC1 GLN A 426 LEU A 428 5 3
HELIX 20 AC2 PRO A 429 HIS A 433 5 5
HELIX 21 AC3 VAL A 480 GLN A 484 5 5
HELIX 22 AC4 GLU A 507 LEU A 516 1 10
HELIX 23 AC5 LEU A 530 LEU A 534 5 5
HELIX 24 AC6 LEU A 558 PHE A 562 5 5
HELIX 25 AC7 PRO A 641 THR A 645 5 5
HELIX 26 AC8 SER A 655 SER A 659 5 5
HELIX 27 AC9 ASN A 661 ASP A 668 1 8
HELIX 28 AD1 PRO A 678 SER A 682 5 5
HELIX 29 AD2 SER A 684 PHE A 692 1 9
HELIX 30 AD3 LEU A 693 THR A 695 5 3
HELIX 31 AD4 TYR A 701 VAL A 714 1 14
HELIX 32 AD5 VAL A 714 ASN A 724 1 11
HELIX 33 AD6 ILE A 744 ILE A 748 5 5
HELIX 34 AD7 PRO A 776 CYS A 780 5 5
HELIX 35 AD8 ASP A 806 LYS A 809 5 4
HELIX 36 AD9 TRP A 810 HIS A 818 1 9
HELIX 37 AE1 ARG A 821 GLY A 830 1 10
HELIX 38 AE2 SER A 840 TYR A 850 1 11
SHEET 1 AA1 6 VAL A 302 PRO A 310 0
SHEET 2 AA1 6 LEU A 165 ASP A 171 1 N ILE A 167 O PHE A 305
SHEET 3 AA1 6 ASN A 352 GLY A 357 1 O ILE A 354 N PHE A 168
SHEET 4 AA1 6 PHE A 487 TYR A 490 -1 O TYR A 490 N VAL A 353
SHEET 5 AA1 6 THR A 196 HIS A 197 -1 N THR A 196 O GLY A 489
SHEET 6 AA1 6 THR A 498 LYS A 499 1 O THR A 498 N HIS A 197
SHEET 1 AA2 2 MET A 201 ARG A 202 0
SHEET 2 AA2 2 PHE A 503 GLU A 504 1 O PHE A 503 N ARG A 202
SHEET 1 AA3 2 MET A 232 ASP A 234 0
SHEET 2 AA3 2 ALA A 239 PHE A 241 -1 O PHE A 241 N MET A 232
SHEET 1 AA4 2 GLU A 362 ASP A 363 0
SHEET 2 AA4 2 GLY A 472 ASP A 473 -1 O ASP A 473 N GLU A 362
SHEET 1 AA5 2 THR A 369 PHE A 371 0
SHEET 2 AA5 2 HIS A 452 ALA A 454 1 O HIS A 452 N GLU A 370
SHEET 1 AA6 4 ILE A 382 VAL A 385 0
SHEET 2 AA6 4 LEU A 389 PRO A 394 -1 O ARG A 393 N THR A 383
SHEET 3 AA6 4 LEU A 443 VAL A 447 -1 O LEU A 445 N GLY A 390
SHEET 4 AA6 4 PHE A 420 MET A 424 -1 N TYR A 423 O HIS A 444
SHEET 1 AA7 2 ALA A 598 VAL A 599 0
SHEET 2 AA7 2 LEU A 831 ASP A 832 -1 O ASP A 832 N ALA A 598
SHEET 1 AA8 7 TYR A 605 TYR A 609 0
SHEET 2 AA8 7 GLU A 614 SER A 618 -1 O TYR A 617 N ASP A 606
SHEET 3 AA8 7 MET A 623 ILE A 631 -1 O SER A 628 N GLU A 614
SHEET 4 AA8 7 VAL A 726 ILE A 733 -1 O VAL A 728 N TYR A 629
SHEET 5 AA8 7 HIS A 762 CYS A 770 -1 O THR A 768 N ASN A 727
SHEET 6 AA8 7 LEU A 784 PRO A 792 -1 O SER A 787 N ILE A 767
SHEET 7 AA8 7 THR A 819 ALA A 820 -1 O ALA A 820 N SER A 788
SHEET 1 AA9 2 SER A 672 PHE A 675 0
SHEET 2 AA9 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 2.04
SSBOND 2 CYS A 62 CYS A 93 1555 1555 2.04
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 2.03
SSBOND 9 CYS A 148 CYS A 194 1555 1555 2.03
SSBOND 10 CYS A 156 CYS A 350 1555 1555 2.03
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 2.04
LINK ND2 ASN A 53 C1 NAG B 1 1555 1555 1.43
LINK ND2 ASN A 410 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN A 524 C1 NAG D 1 1555 1555 1.43
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.42
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.40
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.41
LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.40
LINK O3 BMA D 3 C1 MAN D 7 1555 1555 1.44
LINK O3 MAN D 4 C1 MAN D 5 1555 1555 1.44
LINK O2 MAN D 5 C1 MAN D 6 1555 1555 1.44
LINK OD1 ASP A 171 ZN ZN A 913 1555 1555 1.89
LINK OD1 ASP A 311 ZN ZN A 912 1555 1555 2.15
LINK OD2 ASP A 311 ZN ZN A 912 1555 1555 2.47
LINK NE2 HIS A 315 ZN ZN A 912 1555 1555 2.00
LINK OD2 ASP A 358 ZN ZN A 913 1555 1555 2.06
LINK NE2 HIS A 359 ZN ZN A 913 1555 1555 2.27
LINK O ASN A 374 CA CA A 919 1555 1555 2.65
LINK NE2 HIS A 474 ZN ZN A 912 1555 1555 2.09
LINK O TYR A 665 K K A 916 1555 1555 2.43
LINK O ASP A 668 K K A 916 1555 1555 2.63
LINK O MET A 671 K K A 916 1555 1555 2.68
LINK OD1 ASP A 735 CA CA A 914 1555 1555 2.34
LINK OD1 ASN A 737 CA CA A 914 1555 1555 2.30
LINK OD1 ASN A 739 CA CA A 914 1555 1555 2.36
LINK O LEU A 741 CA CA A 914 1555 1555 2.33
LINK OD1 ASP A 743 CA CA A 914 1555 1555 2.39
LINK O ASN A 797 NA NA A 915 1555 1555 2.66
LINK O SER A 800 NA NA A 915 1555 1555 2.64
LINK OG SER A 803 NA NA A 915 1555 1555 2.36
LINK ZN ZN A 912 N29 9V8 A 920 1555 1555 2.07
LINK ZN ZN A 912 O HOH A1002 1555 1555 2.48
LINK ZN ZN A 913 O HOH A1002 1555 1555 2.14
LINK CA CA A 914 O HOH A1134 1555 1555 2.49
LINK NA NA A 915 O HOH A1302 1555 1555 2.74
LINK NA NA A 915 O HOH A1322 1555 1555 2.47
LINK NA NA A 915 O HOH A1444 1555 1555 2.49
LINK K K A 916 O HOH A1453 1555 1555 2.87
LINK K K A 916 O HOH A1480 1555 1555 2.83
LINK O3 AP3G A 917 CA CA A 919 1555 1555 2.72
LINK O3 BP3G A 917 CA CA A 919 1555 1555 2.66
LINK O4 AP3G A 917 CA CA A 919 1555 1555 2.64
LINK O4 BP3G A 917 CA CA A 919 1555 1555 3.11
LINK O5 AP3G A 917 CA CA A 919 1555 1555 2.92
LINK O5 BP3G A 917 CA CA A 919 1555 1555 2.70
LINK O6 AP3G A 917 CA CA A 919 1555 1555 2.90
LINK CA CA A 919 O HOH A1059 1555 1655 2.68
CISPEP 1 PRO A 70 PRO A 71 0 2.12
CISPEP 2 TYR A 205 PRO A 206 0 -6.08
CISPEP 3 GLN A 309 PRO A 310 0 2.73
CRYST1 61.057 93.779 75.695 90.00 94.91 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 0.016378 0.000000 0.001407 0.00000
SCALE2 0.000000 0.010663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013260 0.00000
(ATOM LINES ARE NOT SHOWN.)
END