HEADER HYDROLASE/HYDROLASE INHIBITOR 22-APR-15 4ZG9
TITLE STRUCTURAL BASIS FOR INHIBITION OF HUMAN AUTOTAXIN BY FOUR NOVEL
TITLE 2 COMPOUNDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE FAMILY
COMPND 3 MEMBER 2;
COMPND 4 CHAIN: A, B;
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: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ENPP2, ATX, PDNP2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID
KEYWDS AUTOTAXIN, ENPP2, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.STEIN,G.BAIN,J.H.HUTCHINSON,J.F.EVANS
REVDAT 3 29-JUL-20 4ZG9 1 COMPND JRNL REMARK HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 11-NOV-15 4ZG9 1 JRNL
REVDAT 1 14-OCT-15 4ZG9 0
JRNL AUTH A.J.STEIN,G.BAIN,P.PRODANOVICH,A.M.SANTINI,J.DARLINGTON,
JRNL AUTH 2 N.M.STELZER,R.S.SIDHU,J.SCHAUB,L.GOULET,D.LONERGAN,
JRNL AUTH 3 I.CALDERON,J.F.EVANS,J.H.HUTCHINSON
JRNL TITL STRUCTURAL BASIS FOR INHIBITION OF HUMAN AUTOTAXIN BY FOUR
JRNL TITL 2 POTENT COMPOUNDS WITH DISTINCT MODES OF BINDING.
JRNL REF MOL.PHARMACOL. V. 88 982 2015
JRNL REFN ESSN 1521-0111
JRNL PMID 26371182
JRNL DOI 10.1124/MOL.115.100404
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 51193
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2752
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 213
REMARK 3 SOLVENT ATOMS : 51
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.05000
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): 1.254
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.357
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.253
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.434
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 4ZG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209212.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-325
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53975
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.81000
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3350, 4% TACSIMATE PH 6.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 94.09650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.09650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 63.73000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 104.99550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 63.73000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 104.99550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 94.09650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 63.73000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 104.99550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 94.09650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 63.73000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 104.99550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ARG A 3
REMARK 465 ARG A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 PHE A 7
REMARK 465 GLN A 8
REMARK 465 SER A 9
REMARK 465 CYS A 10
REMARK 465 GLN A 11
REMARK 465 ILE A 12
REMARK 465 ILE A 13
REMARK 465 SER A 14
REMARK 465 LEU A 15
REMARK 465 PHE A 16
REMARK 465 THR A 17
REMARK 465 PHE A 18
REMARK 465 ALA A 19
REMARK 465 VAL A 20
REMARK 465 GLY A 21
REMARK 465 VAL A 22
REMARK 465 ASN A 23
REMARK 465 ILE A 24
REMARK 465 CYS A 25
REMARK 465 LEU A 26
REMARK 465 GLY A 27
REMARK 465 PHE A 28
REMARK 465 THR A 29
REMARK 465 ALA A 30
REMARK 465 HIS A 31
REMARK 465 ARG A 32
REMARK 465 ILE A 33
REMARK 465 LYS A 34
REMARK 465 ARG A 35
REMARK 465 ALA A 36
REMARK 465 GLU A 37
REMARK 465 GLY A 38
REMARK 465 TRP A 39
REMARK 465 GLU A 40
REMARK 465 GLU A 41
REMARK 465 GLY A 42
REMARK 465 PRO A 43
REMARK 465 PRO A 44
REMARK 465 THR A 45
REMARK 465 VAL A 46
REMARK 465 LEU A 47
REMARK 465 SER A 48
REMARK 465 ASP A 49
REMARK 465 SER A 50
REMARK 465 PRO A 51
REMARK 465 TRP A 52
REMARK 465 THR A 53
REMARK 465 ASN A 54
REMARK 465 ILE A 55
REMARK 465 SER A 56
REMARK 465 GLY A 57
REMARK 465 GLU A 68
REMARK 465 ALA A 69
REMARK 465 GLY A 70
REMARK 465 PRO A 71
REMARK 465 ARG A 245
REMARK 465 GLY A 246
REMARK 465 ARG A 247
REMARK 465 GLU A 248
REMARK 465 LYS A 249
REMARK 465 LEU A 459
REMARK 465 ASP A 460
REMARK 465 VAL A 461
REMARK 465 TYR A 462
REMARK 465 LYS A 463
REMARK 465 LYS A 464
REMARK 465 PRO A 465
REMARK 465 SER A 466
REMARK 465 GLY A 467
REMARK 465 LYS A 468
REMARK 465 CYS A 567
REMARK 465 THR A 568
REMARK 465 CYS A 569
REMARK 465 ASP A 570
REMARK 465 ASP A 571
REMARK 465 LYS A 572
REMARK 465 VAL A 573
REMARK 465 GLU A 574
REMARK 465 PRO A 575
REMARK 465 LYS A 576
REMARK 465 ASN A 577
REMARK 465 LYS A 578
REMARK 465 LEU A 579
REMARK 465 ASP A 580
REMARK 465 GLU A 581
REMARK 465 LEU A 582
REMARK 465 ASN A 583
REMARK 465 LYS A 584
REMARK 465 ARG A 585
REMARK 465 LEU A 586
REMARK 465 HIS A 587
REMARK 465 THR A 588
REMARK 465 LYS A 589
REMARK 465 GLY A 590
REMARK 465 SER A 591
REMARK 465 THR A 592
REMARK 465 GLU A 593
REMARK 465 GLU A 594
REMARK 465 ALA A 640
REMARK 465 GLU A 641
REMARK 465 VAL A 642
REMARK 465 SER A 643
REMARK 465 SER A 644
REMARK 465 VAL A 645
REMARK 465 SER A 861
REMARK 465 GLU A 862
REMARK 465 ILE A 863
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ARG B 3
REMARK 465 ARG B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 PHE B 7
REMARK 465 GLN B 8
REMARK 465 SER B 9
REMARK 465 CYS B 10
REMARK 465 GLN B 11
REMARK 465 ILE B 12
REMARK 465 ILE B 13
REMARK 465 SER B 14
REMARK 465 LEU B 15
REMARK 465 PHE B 16
REMARK 465 THR B 17
REMARK 465 PHE B 18
REMARK 465 ALA B 19
REMARK 465 VAL B 20
REMARK 465 GLY B 21
REMARK 465 VAL B 22
REMARK 465 ASN B 23
REMARK 465 ILE B 24
REMARK 465 CYS B 25
REMARK 465 LEU B 26
REMARK 465 GLY B 27
REMARK 465 PHE B 28
REMARK 465 THR B 29
REMARK 465 ALA B 30
REMARK 465 HIS B 31
REMARK 465 ARG B 32
REMARK 465 ILE B 33
REMARK 465 LYS B 34
REMARK 465 ARG B 35
REMARK 465 ALA B 36
REMARK 465 GLU B 37
REMARK 465 GLY B 38
REMARK 465 TRP B 39
REMARK 465 GLU B 40
REMARK 465 GLU B 41
REMARK 465 GLY B 42
REMARK 465 PRO B 43
REMARK 465 PRO B 44
REMARK 465 THR B 45
REMARK 465 VAL B 46
REMARK 465 LEU B 47
REMARK 465 SER B 48
REMARK 465 ASP B 49
REMARK 465 SER B 50
REMARK 465 PRO B 51
REMARK 465 TRP B 52
REMARK 465 THR B 53
REMARK 465 ASN B 54
REMARK 465 ILE B 55
REMARK 465 SER B 56
REMARK 465 GLY B 57
REMARK 465 GLY B 70
REMARK 465 PRO B 71
REMARK 465 PRO B 72
REMARK 465 ARG B 127
REMARK 465 GLY B 128
REMARK 465 THR B 568
REMARK 465 CYS B 569
REMARK 465 ASP B 570
REMARK 465 ASP B 571
REMARK 465 LYS B 572
REMARK 465 VAL B 573
REMARK 465 GLU B 574
REMARK 465 PRO B 575
REMARK 465 LYS B 576
REMARK 465 ASN B 577
REMARK 465 LYS B 578
REMARK 465 LEU B 579
REMARK 465 ASP B 580
REMARK 465 GLU B 581
REMARK 465 LEU B 582
REMARK 465 ASN B 583
REMARK 465 LYS B 584
REMARK 465 ARG B 585
REMARK 465 LEU B 586
REMARK 465 HIS B 587
REMARK 465 THR B 588
REMARK 465 LYS B 589
REMARK 465 GLY B 590
REMARK 465 ALA B 640
REMARK 465 GLU B 641
REMARK 465 VAL B 642
REMARK 465 SER B 643
REMARK 465 SER B 644
REMARK 465 VAL B 645
REMARK 465 PRO B 646
REMARK 465 ASP B 647
REMARK 465 HIS B 648
REMARK 465 LEU B 649
REMARK 465 THR B 650
REMARK 465 SER B 651
REMARK 465 GLU B 862
REMARK 465 ILE B 863
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 60 CG CD CE NZ
REMARK 470 GLU A 65 CG CD OE1 OE2
REMARK 470 LEU A 66 CG CD1 CD2
REMARK 470 GLN A 67 CG CD OE1 NE2
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 LYS A 96 CG CD CE NZ
REMARK 470 ARG A 99 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 102 CG CD OE1 OE2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 ARG A 112 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 114 CG CD OE1 OE2
REMARK 470 GLU A 115 CG CD OE1 OE2
REMARK 470 GLU A 122 CG CD OE1 OE2
REMARK 470 ARG A 127 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 139 CG CD CE NZ
REMARK 470 GLU A 150 CG CD OE1 OE2
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 LYS A 181 CG CD CE NZ
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 GLU A 299 CG CD OE1 OE2
REMARK 470 LYS A 347 CG CD CE NZ
REMARK 470 ASN A 379 CG OD1 ND2
REMARK 470 ASN A 399 CG OD1 ND2
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 LYS A 406 CG CD CE NZ
REMARK 470 ASN A 411 CG OD1 ND2
REMARK 470 PHE A 470 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 520 CG CD CE NZ
REMARK 470 ARG A 541 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 550 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 565 CG CD1 CD2
REMARK 470 ASP A 647 CG OD1 OD2
REMARK 470 HIS A 648 CG ND1 CD2 CE1 NE2
REMARK 470 THR A 650 OG1 CG2
REMARK 470 SER A 651 OG
REMARK 470 LYS A 671 CG CD CE NZ
REMARK 470 LYS A 674 CG CD CE NZ
REMARK 470 GLU A 691 CG CD OE1 OE2
REMARK 470 LYS A 722 CG CD CE NZ
REMARK 470 LYS A 784 CG CD CE NZ
REMARK 470 LYS A 814 CG CD CE NZ
REMARK 470 LYS A 841 CG CD CE NZ
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 ASP B 73 CG OD1 OD2
REMARK 470 HIS B 88 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 92 CG CD OE1 OE2
REMARK 470 LYS B 96 CG CD CE NZ
REMARK 470 ARG B 99 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 VAL B 111 CG1 CG2
REMARK 470 ARG B 112 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 114 CG CD OE1 OE2
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 ASP B 123 CG OD1 OD2
REMARK 470 ASP B 129 CG OD1 OD2
REMARK 470 LYS B 180 CG CD CE NZ
REMARK 470 LYS B 181 CG CD CE NZ
REMARK 470 ARG B 245 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 248 CG CD OE1 OE2
REMARK 470 LYS B 347 CG CD CE NZ
REMARK 470 SER B 398 OG
REMARK 470 ASN B 399 CG OD1 ND2
REMARK 470 LYS B 402 CG CD CE NZ
REMARK 470 ASN B 411 CG OD1 ND2
REMARK 470 LYS B 416 CG CD CE NZ
REMARK 470 VAL B 461 CG1 CG2
REMARK 470 TYR B 462 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 463 CG CD CE NZ
REMARK 470 LYS B 464 CG CD CE NZ
REMARK 470 LYS B 468 CG CD CE NZ
REMARK 470 ARG B 541 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 593 CG CD OE1 OE2
REMARK 470 ARG B 607 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 671 CG CD CE NZ
REMARK 470 GLU B 691 CG CD OE1 OE2
REMARK 470 TYR B 694 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 722 CG CD CE NZ
REMARK 470 LYS B 841 CG CD CE NZ
REMARK 470 SER B 861 OG
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 LYS A 60 -89.20 30.05
REMARK 500 LEU A 95 41.50 -101.21
REMARK 500 ARG A 99 -8.66 75.38
REMARK 500 ARG A 112 46.98 -66.14
REMARK 500 CYS A 124 -75.29 1.60
REMARK 500 GLU A 156 66.46 -101.53
REMARK 500 LYS A 181 24.42 -75.75
REMARK 500 HIS A 360 -177.48 -175.60
REMARK 500 CYS A 414 65.67 13.89
REMARK 500 ALA A 436 -45.64 -158.91
REMARK 500 ARG A 450 135.17 -36.14
REMARK 500 ARG A 451 -4.15 77.75
REMARK 500 LYS A 457 149.72 -179.34
REMARK 500 ASP A 478 124.93 -27.07
REMARK 500 THR A 537 -157.72 -119.64
REMARK 500 ASN A 538 12.38 54.01
REMARK 500 MET A 544 129.24 -39.20
REMARK 500 ASP A 564 76.57 -111.58
REMARK 500 LEU A 565 -97.44 -93.03
REMARK 500 LEU A 597 55.81 -152.82
REMARK 500 ASP A 647 161.05 63.50
REMARK 500 HIS A 648 64.06 -101.96
REMARK 500 ASN A 729 54.27 76.51
REMARK 500 ASP A 740 54.69 -142.05
REMARK 500 HIS A 747 119.11 -35.10
REMARK 500 LYS A 784 47.97 -158.63
REMARK 500 PRO A 788 155.65 -46.04
REMARK 500 ASN A 802 42.12 -108.10
REMARK 500 TRP A 815 -29.57 -162.31
REMARK 500 TYR A 859 64.97 -113.33
REMARK 500 ASN B 78 -69.18 1.08
REMARK 500 LEU B 95 46.14 -94.39
REMARK 500 ARG B 112 102.68 -44.97
REMARK 500 GLU B 114 0.27 -66.79
REMARK 500 CYS B 124 -70.60 -12.81
REMARK 500 TYR B 134 -70.57 -47.54
REMARK 500 LYS B 180 -74.63 -66.34
REMARK 500 LYS B 181 69.67 -63.81
REMARK 500 ASP B 239 61.80 -118.85
REMARK 500 ARG B 245 55.22 -110.23
REMARK 500 GLU B 248 -113.28 -80.68
REMARK 500 HIS B 360 -175.93 -178.11
REMARK 500 SER B 374 -57.65 -18.55
REMARK 500 TYR B 376 -37.29 -134.97
REMARK 500 CYS B 414 71.55 28.44
REMARK 500 GLN B 419 135.27 -39.00
REMARK 500 ALA B 436 -41.42 -150.35
REMARK 500 ARG B 451 -12.32 86.33
REMARK 500 ARG B 456 -60.97 -90.92
REMARK 500 ASP B 478 136.06 -38.53
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR B 424 LEU B 425 149.45
REMARK 500
REMARK 500 REMARK: NULL
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 904 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 172 OD1
REMARK 620 2 THR A 210 OG1 101.1
REMARK 620 3 ASP A 359 OD2 98.6 121.4
REMARK 620 4 HIS A 360 NE2 116.7 96.5 121.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 903 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 312 OD1
REMARK 620 2 ASP A 312 OD2 52.5
REMARK 620 3 HIS A 316 NE2 79.7 83.6
REMARK 620 4 HIS A 475 NE2 91.1 140.5 106.5
REMARK 620 5 EDO A 910 O2 162.1 114.2 112.7 97.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 906 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 670 O
REMARK 620 2 ASP A 673 O 83.4
REMARK 620 3 MET A 676 O 102.3 73.0
REMARK 620 4 HOH A1008 O 158.1 74.7 71.2
REMARK 620 5 HOH A1018 O 147.6 128.8 92.6 54.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 905 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 740 OD1
REMARK 620 2 ASP A 742 OD1 93.8
REMARK 620 3 ASP A 744 OD1 79.2 88.6
REMARK 620 4 LEU A 746 O 89.0 177.2 92.3
REMARK 620 5 ASP A 748 OD1 101.8 79.9 168.5 99.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 907 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 802 O
REMARK 620 2 SER A 805 O 68.4
REMARK 620 3 SER A 808 OG 95.5 87.1
REMARK 620 4 HOH A1004 O 85.6 148.9 112.9
REMARK 620 5 HOH A1006 O 80.4 69.6 156.3 90.1
REMARK 620 6 SER B 466 O 103.0 59.8 35.3 146.9 122.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 905 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 172 OD1
REMARK 620 2 THR B 210 OG1 107.1
REMARK 620 3 ASP B 359 OD2 72.0 106.4
REMARK 620 4 HIS B 360 NE2 163.9 87.4 97.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 904 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 312 OD1
REMARK 620 2 ASP B 312 OD2 53.3
REMARK 620 3 HIS B 316 NE2 81.9 87.4
REMARK 620 4 HIS B 475 NE2 126.2 72.9 98.4
REMARK 620 5 EDO B 911 O1 119.4 160.0 110.8 110.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 907 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 670 O
REMARK 620 2 ASP B 673 O 70.9
REMARK 620 3 MET B 676 O 82.6 64.1
REMARK 620 4 HOH B1006 O 140.7 88.6 58.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 906 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 740 OD1
REMARK 620 2 ASP B 742 OD1 87.0
REMARK 620 3 ASP B 744 OD2 129.8 91.7
REMARK 620 4 LEU B 746 O 78.2 164.7 100.5
REMARK 620 5 ASP B 748 OD1 88.6 82.9 141.0 93.1
REMARK 620 6 HOH B1001 O 173.9 92.6 56.3 101.8 85.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 908 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 802 O
REMARK 620 2 SER B 805 O 66.6
REMARK 620 3 SER B 808 OG 92.6 89.4
REMARK 620 4 HOH B1008 O 84.3 72.3 161.2
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZG6 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZG7 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZGA RELATED DB: PDB
DBREF 4ZG9 A 1 863 UNP Q13822 ENPP2_HUMAN 1 863
DBREF 4ZG9 B 1 863 UNP Q13822 ENPP2_HUMAN 1 863
SEQRES 1 A 863 MET ALA ARG ARG SER SER PHE GLN SER CYS GLN ILE ILE
SEQRES 2 A 863 SER LEU PHE THR PHE ALA VAL GLY VAL ASN ILE CYS LEU
SEQRES 3 A 863 GLY PHE THR ALA HIS ARG ILE LYS ARG ALA GLU GLY TRP
SEQRES 4 A 863 GLU GLU GLY PRO PRO THR VAL LEU SER ASP SER PRO TRP
SEQRES 5 A 863 THR ASN ILE SER GLY SER CYS LYS GLY ARG CYS PHE GLU
SEQRES 6 A 863 LEU GLN GLU ALA GLY PRO PRO ASP CYS ARG CYS ASP ASN
SEQRES 7 A 863 LEU CYS LYS SER TYR THR SER CYS CYS HIS ASP PHE ASP
SEQRES 8 A 863 GLU LEU CYS LEU LYS THR ALA ARG GLY TRP GLU CYS THR
SEQRES 9 A 863 LYS ASP ARG CYS GLY GLU VAL ARG ASN GLU GLU ASN ALA
SEQRES 10 A 863 CYS HIS CYS SER GLU ASP CYS LEU ALA ARG GLY ASP CYS
SEQRES 11 A 863 CYS THR ASN TYR GLN VAL VAL CYS LYS GLY GLU SER HIS
SEQRES 12 A 863 TRP VAL ASP ASP ASP CYS GLU GLU ILE LYS ALA ALA GLU
SEQRES 13 A 863 CYS PRO ALA GLY PHE VAL ARG PRO PRO LEU ILE ILE PHE
SEQRES 14 A 863 SER VAL ASP GLY PHE ARG ALA SER TYR MET LYS LYS GLY
SEQRES 15 A 863 SER LYS VAL MET PRO ASN ILE GLU LYS LEU ARG SER CYS
SEQRES 16 A 863 GLY THR HIS SER PRO TYR MET ARG PRO VAL TYR PRO THR
SEQRES 17 A 863 LYS THR PHE PRO ASN LEU TYR THR LEU ALA THR GLY LEU
SEQRES 18 A 863 TYR PRO GLU SER HIS GLY ILE VAL GLY ASN SER MET TYR
SEQRES 19 A 863 ASP PRO VAL PHE ASP ALA THR PHE HIS LEU ARG GLY ARG
SEQRES 20 A 863 GLU LYS PHE ASN HIS ARG TRP TRP GLY GLY GLN PRO LEU
SEQRES 21 A 863 TRP ILE THR ALA THR LYS GLN GLY VAL LYS ALA GLY THR
SEQRES 22 A 863 PHE PHE TRP SER VAL VAL ILE PRO HIS GLU ARG ARG ILE
SEQRES 23 A 863 LEU THR ILE LEU GLN TRP LEU THR LEU PRO ASP HIS GLU
SEQRES 24 A 863 ARG PRO SER VAL TYR ALA PHE TYR SER GLU GLN PRO ASP
SEQRES 25 A 863 PHE SER GLY HIS LYS TYR GLY PRO PHE GLY PRO GLU MET
SEQRES 26 A 863 THR ASN PRO LEU ARG GLU ILE ASP LYS ILE VAL GLY GLN
SEQRES 27 A 863 LEU MET ASP GLY LEU LYS GLN LEU LYS LEU HIS ARG CYS
SEQRES 28 A 863 VAL ASN VAL ILE PHE VAL GLY ASP HIS GLY MET GLU ASP
SEQRES 29 A 863 VAL THR CYS ASP ARG THR GLU PHE LEU SER ASN TYR LEU
SEQRES 30 A 863 THR ASN VAL ASP ASP ILE THR LEU VAL PRO GLY THR LEU
SEQRES 31 A 863 GLY ARG ILE ARG SER LYS PHE SER ASN ASN ALA LYS TYR
SEQRES 32 A 863 ASP PRO LYS ALA ILE ILE ALA ASN LEU THR CYS LYS LYS
SEQRES 33 A 863 PRO ASP GLN HIS PHE LYS PRO TYR LEU LYS GLN HIS LEU
SEQRES 34 A 863 PRO LYS ARG LEU HIS TYR ALA ASN ASN ARG ARG ILE GLU
SEQRES 35 A 863 ASP ILE HIS LEU LEU VAL GLU ARG ARG TRP HIS VAL ALA
SEQRES 36 A 863 ARG LYS PRO LEU ASP VAL TYR LYS LYS PRO SER GLY LYS
SEQRES 37 A 863 CYS PHE PHE GLN GLY ASP HIS GLY PHE ASP ASN LYS VAL
SEQRES 38 A 863 ASN SER MET GLN THR VAL PHE VAL GLY TYR GLY SER THR
SEQRES 39 A 863 PHE LYS TYR LYS THR LYS VAL PRO PRO PHE GLU ASN ILE
SEQRES 40 A 863 GLU LEU TYR ASN VAL MET CYS ASP LEU LEU GLY LEU LYS
SEQRES 41 A 863 PRO ALA PRO ASN ASN GLY THR HIS GLY SER LEU ASN HIS
SEQRES 42 A 863 LEU LEU ARG THR ASN THR PHE ARG PRO THR MET PRO GLU
SEQRES 43 A 863 GLU VAL THR ARG PRO ASN TYR PRO GLY ILE MET TYR LEU
SEQRES 44 A 863 GLN SER ASP PHE ASP LEU GLY CYS THR CYS ASP ASP LYS
SEQRES 45 A 863 VAL GLU PRO LYS ASN LYS LEU ASP GLU LEU ASN LYS ARG
SEQRES 46 A 863 LEU HIS THR LYS GLY SER THR GLU GLU ARG HIS LEU LEU
SEQRES 47 A 863 TYR GLY ARG PRO ALA VAL LEU TYR ARG THR ARG TYR ASP
SEQRES 48 A 863 ILE LEU TYR HIS THR ASP PHE GLU SER GLY TYR SER GLU
SEQRES 49 A 863 ILE PHE LEU MET PRO LEU TRP THR SER TYR THR VAL SER
SEQRES 50 A 863 LYS GLN ALA GLU VAL SER SER VAL PRO ASP HIS LEU THR
SEQRES 51 A 863 SER CYS VAL ARG PRO ASP VAL ARG VAL SER PRO SER PHE
SEQRES 52 A 863 SER GLN ASN CYS LEU ALA TYR LYS ASN ASP LYS GLN MET
SEQRES 53 A 863 SER TYR GLY PHE LEU PHE PRO PRO TYR LEU SER SER SER
SEQRES 54 A 863 PRO GLU ALA LYS TYR ASP ALA PHE LEU VAL THR ASN MET
SEQRES 55 A 863 VAL PRO MET TYR PRO ALA PHE LYS ARG VAL TRP ASN TYR
SEQRES 56 A 863 PHE GLN ARG VAL LEU VAL LYS LYS TYR ALA SER GLU ARG
SEQRES 57 A 863 ASN GLY VAL ASN VAL ILE SER GLY PRO ILE PHE ASP TYR
SEQRES 58 A 863 ASP TYR ASP GLY LEU HIS ASP THR GLU ASP LYS ILE LYS
SEQRES 59 A 863 GLN TYR VAL GLU GLY SER SER ILE PRO VAL PRO THR HIS
SEQRES 60 A 863 TYR TYR SER ILE ILE THR SER CYS LEU ASP PHE THR GLN
SEQRES 61 A 863 PRO ALA ASP LYS CYS ASP GLY PRO LEU SER VAL SER SER
SEQRES 62 A 863 PHE ILE LEU PRO HIS ARG PRO ASP ASN GLU GLU SER CYS
SEQRES 63 A 863 ASN SER SER GLU ASP GLU SER LYS TRP VAL GLU GLU LEU
SEQRES 64 A 863 MET LYS MET HIS THR ALA ARG VAL ARG ASP ILE GLU HIS
SEQRES 65 A 863 LEU THR SER LEU ASP PHE PHE ARG LYS THR SER ARG SER
SEQRES 66 A 863 TYR PRO GLU ILE LEU THR LEU LYS THR TYR LEU HIS THR
SEQRES 67 A 863 TYR GLU SER GLU ILE
SEQRES 1 B 863 MET ALA ARG ARG SER SER PHE GLN SER CYS GLN ILE ILE
SEQRES 2 B 863 SER LEU PHE THR PHE ALA VAL GLY VAL ASN ILE CYS LEU
SEQRES 3 B 863 GLY PHE THR ALA HIS ARG ILE LYS ARG ALA GLU GLY TRP
SEQRES 4 B 863 GLU GLU GLY PRO PRO THR VAL LEU SER ASP SER PRO TRP
SEQRES 5 B 863 THR ASN ILE SER GLY SER CYS LYS GLY ARG CYS PHE GLU
SEQRES 6 B 863 LEU GLN GLU ALA GLY PRO PRO ASP CYS ARG CYS ASP ASN
SEQRES 7 B 863 LEU CYS LYS SER TYR THR SER CYS CYS HIS ASP PHE ASP
SEQRES 8 B 863 GLU LEU CYS LEU LYS THR ALA ARG GLY TRP GLU CYS THR
SEQRES 9 B 863 LYS ASP ARG CYS GLY GLU VAL ARG ASN GLU GLU ASN ALA
SEQRES 10 B 863 CYS HIS CYS SER GLU ASP CYS LEU ALA ARG GLY ASP CYS
SEQRES 11 B 863 CYS THR ASN TYR GLN VAL VAL CYS LYS GLY GLU SER HIS
SEQRES 12 B 863 TRP VAL ASP ASP ASP CYS GLU GLU ILE LYS ALA ALA GLU
SEQRES 13 B 863 CYS PRO ALA GLY PHE VAL ARG PRO PRO LEU ILE ILE PHE
SEQRES 14 B 863 SER VAL ASP GLY PHE ARG ALA SER TYR MET LYS LYS GLY
SEQRES 15 B 863 SER LYS VAL MET PRO ASN ILE GLU LYS LEU ARG SER CYS
SEQRES 16 B 863 GLY THR HIS SER PRO TYR MET ARG PRO VAL TYR PRO THR
SEQRES 17 B 863 LYS THR PHE PRO ASN LEU TYR THR LEU ALA THR GLY LEU
SEQRES 18 B 863 TYR PRO GLU SER HIS GLY ILE VAL GLY ASN SER MET TYR
SEQRES 19 B 863 ASP PRO VAL PHE ASP ALA THR PHE HIS LEU ARG GLY ARG
SEQRES 20 B 863 GLU LYS PHE ASN HIS ARG TRP TRP GLY GLY GLN PRO LEU
SEQRES 21 B 863 TRP ILE THR ALA THR LYS GLN GLY VAL LYS ALA GLY THR
SEQRES 22 B 863 PHE PHE TRP SER VAL VAL ILE PRO HIS GLU ARG ARG ILE
SEQRES 23 B 863 LEU THR ILE LEU GLN TRP LEU THR LEU PRO ASP HIS GLU
SEQRES 24 B 863 ARG PRO SER VAL TYR ALA PHE TYR SER GLU GLN PRO ASP
SEQRES 25 B 863 PHE SER GLY HIS LYS TYR GLY PRO PHE GLY PRO GLU MET
SEQRES 26 B 863 THR ASN PRO LEU ARG GLU ILE ASP LYS ILE VAL GLY GLN
SEQRES 27 B 863 LEU MET ASP GLY LEU LYS GLN LEU LYS LEU HIS ARG CYS
SEQRES 28 B 863 VAL ASN VAL ILE PHE VAL GLY ASP HIS GLY MET GLU ASP
SEQRES 29 B 863 VAL THR CYS ASP ARG THR GLU PHE LEU SER ASN TYR LEU
SEQRES 30 B 863 THR ASN VAL ASP ASP ILE THR LEU VAL PRO GLY THR LEU
SEQRES 31 B 863 GLY ARG ILE ARG SER LYS PHE SER ASN ASN ALA LYS TYR
SEQRES 32 B 863 ASP PRO LYS ALA ILE ILE ALA ASN LEU THR CYS LYS LYS
SEQRES 33 B 863 PRO ASP GLN HIS PHE LYS PRO TYR LEU LYS GLN HIS LEU
SEQRES 34 B 863 PRO LYS ARG LEU HIS TYR ALA ASN ASN ARG ARG ILE GLU
SEQRES 35 B 863 ASP ILE HIS LEU LEU VAL GLU ARG ARG TRP HIS VAL ALA
SEQRES 36 B 863 ARG LYS PRO LEU ASP VAL TYR LYS LYS PRO SER GLY LYS
SEQRES 37 B 863 CYS PHE PHE GLN GLY ASP HIS GLY PHE ASP ASN LYS VAL
SEQRES 38 B 863 ASN SER MET GLN THR VAL PHE VAL GLY TYR GLY SER THR
SEQRES 39 B 863 PHE LYS TYR LYS THR LYS VAL PRO PRO PHE GLU ASN ILE
SEQRES 40 B 863 GLU LEU TYR ASN VAL MET CYS ASP LEU LEU GLY LEU LYS
SEQRES 41 B 863 PRO ALA PRO ASN ASN GLY THR HIS GLY SER LEU ASN HIS
SEQRES 42 B 863 LEU LEU ARG THR ASN THR PHE ARG PRO THR MET PRO GLU
SEQRES 43 B 863 GLU VAL THR ARG PRO ASN TYR PRO GLY ILE MET TYR LEU
SEQRES 44 B 863 GLN SER ASP PHE ASP LEU GLY CYS THR CYS ASP ASP LYS
SEQRES 45 B 863 VAL GLU PRO LYS ASN LYS LEU ASP GLU LEU ASN LYS ARG
SEQRES 46 B 863 LEU HIS THR LYS GLY SER THR GLU GLU ARG HIS LEU LEU
SEQRES 47 B 863 TYR GLY ARG PRO ALA VAL LEU TYR ARG THR ARG TYR ASP
SEQRES 48 B 863 ILE LEU TYR HIS THR ASP PHE GLU SER GLY TYR SER GLU
SEQRES 49 B 863 ILE PHE LEU MET PRO LEU TRP THR SER TYR THR VAL SER
SEQRES 50 B 863 LYS GLN ALA GLU VAL SER SER VAL PRO ASP HIS LEU THR
SEQRES 51 B 863 SER CYS VAL ARG PRO ASP VAL ARG VAL SER PRO SER PHE
SEQRES 52 B 863 SER GLN ASN CYS LEU ALA TYR LYS ASN ASP LYS GLN MET
SEQRES 53 B 863 SER TYR GLY PHE LEU PHE PRO PRO TYR LEU SER SER SER
SEQRES 54 B 863 PRO GLU ALA LYS TYR ASP ALA PHE LEU VAL THR ASN MET
SEQRES 55 B 863 VAL PRO MET TYR PRO ALA PHE LYS ARG VAL TRP ASN TYR
SEQRES 56 B 863 PHE GLN ARG VAL LEU VAL LYS LYS TYR ALA SER GLU ARG
SEQRES 57 B 863 ASN GLY VAL ASN VAL ILE SER GLY PRO ILE PHE ASP TYR
SEQRES 58 B 863 ASP TYR ASP GLY LEU HIS ASP THR GLU ASP LYS ILE LYS
SEQRES 59 B 863 GLN TYR VAL GLU GLY SER SER ILE PRO VAL PRO THR HIS
SEQRES 60 B 863 TYR TYR SER ILE ILE THR SER CYS LEU ASP PHE THR GLN
SEQRES 61 B 863 PRO ALA ASP LYS CYS ASP GLY PRO LEU SER VAL SER SER
SEQRES 62 B 863 PHE ILE LEU PRO HIS ARG PRO ASP ASN GLU GLU SER CYS
SEQRES 63 B 863 ASN SER SER GLU ASP GLU SER LYS TRP VAL GLU GLU LEU
SEQRES 64 B 863 MET LYS MET HIS THR ALA ARG VAL ARG ASP ILE GLU HIS
SEQRES 65 B 863 LEU THR SER LEU ASP PHE PHE ARG LYS THR SER ARG SER
SEQRES 66 B 863 TYR PRO GLU ILE LEU THR LEU LYS THR TYR LEU HIS THR
SEQRES 67 B 863 TYR GLU SER GLU ILE
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 ZN A 903 1
HET ZN A 904 1
HET CA A 905 1
HET NA A 906 1
HET NA A 907 1
HET 4O2 A 908 31
HET 4O2 A 909 31
HET EDO A 910 4
HET EDO A 911 4
HET ZN B 904 1
HET ZN B 905 1
HET CA B 906 1
HET NA B 907 1
HET NA B 908 1
HET 4O2 B 909 31
HET 4O2 B 910 31
HET EDO B 911 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM 4O2 3-[(11AS)-6-(4-FLUOROBENZYL)-1,3-DIOXO-5,6,11,11A-
HETNAM 2 4O2 TETRAHYDRO-1H-IMIDAZO[1',5':1,6]PYRIDO[3,4-B]INDOL-
HETNAM 3 4O2 2(3H)-YL]PROPANOIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 5 ZN 4(ZN 2+)
FORMUL 7 CA 2(CA 2+)
FORMUL 8 NA 4(NA 1+)
FORMUL 10 4O2 4(C23 H20 F N3 O4)
FORMUL 12 EDO 3(C2 H6 O2)
FORMUL 22 HOH *51(H2 O)
HELIX 1 AA1 LEU A 79 THR A 84 1 6
HELIX 2 AA2 ASP A 89 CYS A 94 1 6
HELIX 3 AA3 ASP A 123 GLY A 128 1 6
HELIX 4 AA4 ASN A 133 LYS A 139 1 7
HELIX 5 AA5 ARG A 175 LYS A 180 5 6
HELIX 6 AA6 MET A 186 GLY A 196 1 11
HELIX 7 AA7 LYS A 209 GLY A 220 1 12
HELIX 8 AA8 TYR A 222 GLY A 227 1 6
HELIX 9 AA9 ASN A 251 TRP A 255 5 5
HELIX 10 AB1 PRO A 259 GLN A 267 1 9
HELIX 11 AB2 PRO A 281 LEU A 295 1 15
HELIX 12 AB3 PRO A 311 GLY A 319 1 9
HELIX 13 AB4 GLY A 322 GLU A 324 5 3
HELIX 14 AB5 MET A 325 GLN A 345 1 21
HELIX 15 AB6 SER A 374 TYR A 376 5 3
HELIX 16 AB7 ASN A 379 ASP A 381 5 3
HELIX 17 AB8 ASP A 404 THR A 413 1 10
HELIX 18 AB9 GLN A 427 LEU A 429 5 3
HELIX 19 AC1 PRO A 430 HIS A 434 5 5
HELIX 20 AC2 GLU A 508 LEU A 517 1 10
HELIX 21 AC3 LEU A 531 LEU A 535 5 5
HELIX 22 AC4 LEU A 559 PHE A 563 5 5
HELIX 23 AC5 SER A 660 SER A 664 5 5
HELIX 24 AC6 ASN A 666 ASN A 672 1 7
HELIX 25 AC7 PRO A 683 SER A 687 5 5
HELIX 26 AC8 ALA A 692 PHE A 697 1 6
HELIX 27 AC9 TYR A 706 VAL A 719 1 14
HELIX 28 AD1 VAL A 719 ASN A 729 1 11
HELIX 29 AD2 THR A 749 ILE A 753 5 5
HELIX 30 AD3 PRO A 781 CYS A 785 5 5
HELIX 31 AD4 ASP A 811 LYS A 814 5 4
HELIX 32 AD5 TRP A 815 HIS A 823 1 9
HELIX 33 AD6 ARG A 826 SER A 835 1 10
HELIX 34 AD7 SER A 845 TYR A 855 1 11
HELIX 35 AD8 LEU B 79 THR B 84 1 6
HELIX 36 AD9 ASP B 89 LEU B 95 1 7
HELIX 37 AE1 THR B 104 CYS B 108 5 5
HELIX 38 AE2 ASN B 133 CYS B 138 1 6
HELIX 39 AE3 HIS B 143 ASP B 147 5 5
HELIX 40 AE4 ARG B 175 LYS B 180 5 6
HELIX 41 AE5 MET B 186 GLY B 196 1 11
HELIX 42 AE6 LYS B 209 GLY B 220 1 12
HELIX 43 AE7 TYR B 222 GLY B 227 1 6
HELIX 44 AE8 ASN B 251 TRP B 255 5 5
HELIX 45 AE9 PRO B 259 GLN B 267 1 9
HELIX 46 AF1 PRO B 281 LEU B 293 1 13
HELIX 47 AF2 PRO B 311 GLY B 319 1 9
HELIX 48 AF3 GLY B 322 GLU B 324 5 3
HELIX 49 AF4 MET B 325 LEU B 346 1 22
HELIX 50 AF5 SER B 374 TYR B 376 5 3
HELIX 51 AF6 ASN B 379 ASP B 381 5 3
HELIX 52 AF7 ASP B 404 THR B 413 1 10
HELIX 53 AF8 GLN B 427 LEU B 429 5 3
HELIX 54 AF9 PRO B 430 HIS B 434 5 5
HELIX 55 AG1 VAL B 481 GLN B 485 5 5
HELIX 56 AG2 GLU B 508 LEU B 517 1 10
HELIX 57 AG3 LEU B 531 LEU B 535 5 5
HELIX 58 AG4 LEU B 559 PHE B 563 5 5
HELIX 59 AG5 THR B 592 LEU B 597 1 6
HELIX 60 AG6 SER B 660 SER B 664 5 5
HELIX 61 AG7 ASN B 666 ASP B 673 1 8
HELIX 62 AG8 PRO B 683 SER B 687 5 5
HELIX 63 AG9 PRO B 690 THR B 700 5 11
HELIX 64 AH1 TYR B 706 VAL B 719 1 14
HELIX 65 AH2 VAL B 719 ARG B 728 1 10
HELIX 66 AH3 THR B 749 ILE B 753 5 5
HELIX 67 AH4 ASP B 811 LYS B 814 5 4
HELIX 68 AH5 TRP B 815 HIS B 823 1 9
HELIX 69 AH6 ARG B 826 SER B 835 1 10
HELIX 70 AH7 SER B 845 TYR B 855 1 11
SHEET 1 AA1 6 VAL A 303 SER A 308 0
SHEET 2 AA1 6 LEU A 166 VAL A 171 1 N ILE A 168 O PHE A 306
SHEET 3 AA1 6 ASN A 353 GLY A 358 1 O ILE A 355 N PHE A 169
SHEET 4 AA1 6 PHE A 488 TYR A 491 -1 O TYR A 491 N VAL A 354
SHEET 5 AA1 6 THR A 197 HIS A 198 -1 N THR A 197 O GLY A 490
SHEET 6 AA1 6 THR A 499 LYS A 500 1 O THR A 499 N HIS A 198
SHEET 1 AA2 2 MET A 202 ARG A 203 0
SHEET 2 AA2 2 PHE A 504 GLU A 505 1 O PHE A 504 N ARG A 203
SHEET 1 AA3 2 SER A 232 ASP A 235 0
SHEET 2 AA3 2 ALA A 240 HIS A 243 -1 O ALA A 240 N ASP A 235
SHEET 1 AA4 2 GLU A 363 ASP A 364 0
SHEET 2 AA4 2 GLY A 473 ASP A 474 -1 O ASP A 474 N GLU A 363
SHEET 1 AA5 2 THR A 370 PHE A 372 0
SHEET 2 AA5 2 HIS A 453 ALA A 455 1 O ALA A 455 N GLU A 371
SHEET 1 AA6 4 ILE A 383 VAL A 386 0
SHEET 2 AA6 4 LEU A 390 SER A 395 -1 O ARG A 394 N THR A 384
SHEET 3 AA6 4 ILE A 444 VAL A 448 -1 O LEU A 446 N GLY A 391
SHEET 4 AA6 4 PHE A 421 LEU A 425 -1 N TYR A 424 O HIS A 445
SHEET 1 AA7 7 TYR A 610 TYR A 614 0
SHEET 2 AA7 7 GLU A 619 SER A 623 -1 O TYR A 622 N ASP A 611
SHEET 3 AA7 7 MET A 628 VAL A 636 -1 O LEU A 630 N GLY A 621
SHEET 4 AA7 7 VAL A 731 ILE A 738 -1 O VAL A 731 N VAL A 636
SHEET 5 AA7 7 HIS A 767 CYS A 775 -1 O THR A 773 N ASN A 732
SHEET 6 AA7 7 LEU A 789 PRO A 797 -1 O SER A 790 N SER A 774
SHEET 7 AA7 7 THR A 824 ALA A 825 -1 O ALA A 825 N SER A 793
SHEET 1 AA8 2 SER A 677 PHE A 680 0
SHEET 2 AA8 2 MET A 702 MET A 705 -1 O MET A 705 N SER A 677
SHEET 1 AA9 6 VAL B 303 SER B 308 0
SHEET 2 AA9 6 LEU B 166 VAL B 171 1 N ILE B 168 O PHE B 306
SHEET 3 AA9 6 ASN B 353 GLY B 358 1 O ILE B 355 N PHE B 169
SHEET 4 AA9 6 PHE B 488 TYR B 491 -1 O TYR B 491 N VAL B 354
SHEET 5 AA9 6 THR B 197 HIS B 198 -1 N THR B 197 O GLY B 490
SHEET 6 AA9 6 THR B 499 LYS B 500 1 O THR B 499 N HIS B 198
SHEET 1 AB1 2 MET B 202 ARG B 203 0
SHEET 2 AB1 2 PHE B 504 GLU B 505 1 O PHE B 504 N ARG B 203
SHEET 1 AB2 2 SER B 232 ASP B 235 0
SHEET 2 AB2 2 ALA B 240 HIS B 243 -1 O ALA B 240 N ASP B 235
SHEET 1 AB3 2 GLU B 363 ASP B 364 0
SHEET 2 AB3 2 GLY B 473 ASP B 474 -1 O ASP B 474 N GLU B 363
SHEET 1 AB4 2 THR B 370 PHE B 372 0
SHEET 2 AB4 2 HIS B 453 ALA B 455 1 O ALA B 455 N GLU B 371
SHEET 1 AB5 4 ILE B 383 VAL B 386 0
SHEET 2 AB5 4 LEU B 390 SER B 395 -1 O ARG B 394 N THR B 384
SHEET 3 AB5 4 ILE B 444 VAL B 448 -1 O LEU B 446 N GLY B 391
SHEET 4 AB5 4 PHE B 421 LEU B 425 -1 N LYS B 422 O LEU B 447
SHEET 1 AB6 2 ALA B 603 VAL B 604 0
SHEET 2 AB6 2 LEU B 836 ASP B 837 -1 O ASP B 837 N ALA B 603
SHEET 1 AB7 7 TYR B 610 LEU B 613 0
SHEET 2 AB7 7 GLU B 619 SER B 623 -1 O SER B 620 N LEU B 613
SHEET 3 AB7 7 PRO B 629 VAL B 636 -1 O LEU B 630 N GLY B 621
SHEET 4 AB7 7 VAL B 731 ILE B 738 -1 O VAL B 733 N TYR B 634
SHEET 5 AB7 7 HIS B 767 CYS B 775 -1 O THR B 773 N ASN B 732
SHEET 6 AB7 7 LEU B 789 PRO B 797 -1 O SER B 792 N ILE B 772
SHEET 7 AB7 7 THR B 824 ALA B 825 -1 O ALA B 825 N SER B 793
SHEET 1 AB8 2 SER B 677 PHE B 680 0
SHEET 2 AB8 2 MET B 702 MET B 705 -1 O VAL B 703 N GLY B 679
SSBOND 1 CYS A 59 CYS A 76 1555 1555 2.03
SSBOND 2 CYS A 63 CYS A 94 1555 1555 2.03
SSBOND 3 CYS A 74 CYS A 87 1555 1555 2.04
SSBOND 4 CYS A 80 CYS A 86 1555 1555 2.09
SSBOND 5 CYS A 103 CYS A 120 1555 1555 2.05
SSBOND 6 CYS A 108 CYS A 138 1555 1555 2.01
SSBOND 7 CYS A 118 CYS A 131 1555 1555 2.03
SSBOND 8 CYS A 124 CYS A 130 1555 1555 2.02
SSBOND 9 CYS A 149 CYS A 195 1555 1555 2.07
SSBOND 10 CYS A 157 CYS A 351 1555 1555 2.07
SSBOND 11 CYS A 367 CYS A 469 1555 1555 2.04
SSBOND 12 CYS A 414 CYS A 806 1555 1555 2.06
SSBOND 13 CYS A 775 CYS A 785 1555 1555 2.07
SSBOND 14 CYS B 59 CYS B 76 1555 1555 2.04
SSBOND 15 CYS B 63 CYS B 94 1555 1555 2.06
SSBOND 16 CYS B 74 CYS B 87 1555 1555 2.05
SSBOND 17 CYS B 80 CYS B 86 1555 1555 2.07
SSBOND 18 CYS B 103 CYS B 120 1555 1555 2.05
SSBOND 19 CYS B 108 CYS B 138 1555 1555 2.04
SSBOND 20 CYS B 118 CYS B 131 1555 1555 2.01
SSBOND 21 CYS B 124 CYS B 130 1555 1555 2.03
SSBOND 22 CYS B 149 CYS B 195 1555 1555 2.08
SSBOND 23 CYS B 157 CYS B 351 1555 1555 2.10
SSBOND 24 CYS B 367 CYS B 469 1555 1555 2.05
SSBOND 25 CYS B 414 CYS B 806 1555 1555 2.09
SSBOND 26 CYS B 567 CYS B 667 1555 1555 2.06
SSBOND 27 CYS B 775 CYS B 785 1555 1555 2.07
LINK ND2 ASN A 525 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN B 525 C1 NAG D 1 1555 1555 1.42
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK OD1 ASP A 172 ZN ZN A 904 1555 1555 1.77
LINK OG1 THR A 210 ZN ZN A 904 1555 1555 2.17
LINK OD1 ASP A 312 ZN ZN A 903 1555 1555 2.05
LINK OD2 ASP A 312 ZN ZN A 903 1555 1555 2.68
LINK NE2 HIS A 316 ZN ZN A 903 1555 1555 2.06
LINK OD2 ASP A 359 ZN ZN A 904 1555 1555 2.01
LINK NE2 HIS A 360 ZN ZN A 904 1555 1555 2.28
LINK NE2 HIS A 475 ZN ZN A 903 1555 1555 2.20
LINK O TYR A 670 NA NA A 906 1555 1555 2.44
LINK O ASP A 673 NA NA A 906 1555 1555 2.76
LINK O MET A 676 NA NA A 906 1555 1555 2.48
LINK OD1 ASP A 740 CA CA A 905 1555 1555 2.31
LINK OD1 ASP A 742 CA CA A 905 1555 1555 2.07
LINK OD1 ASP A 744 CA CA A 905 1555 1555 2.27
LINK O LEU A 746 CA CA A 905 1555 1555 2.47
LINK OD1 ASP A 748 CA CA A 905 1555 1555 2.24
LINK O ASN A 802 NA NA A 907 1555 1555 2.64
LINK O SER A 805 NA NA A 907 1555 1555 2.78
LINK OG SER A 808 NA NA A 907 1555 1555 2.11
LINK ZN ZN A 903 O2 EDO A 910 1555 1555 2.43
LINK NA NA A 906 O HOH A1008 1555 1555 3.12
LINK NA NA A 906 O HOH A1018 1555 1555 2.82
LINK NA NA A 907 O HOH A1004 1555 1555 2.57
LINK NA NA A 907 O HOH A1006 1555 1555 2.27
LINK NA NA A 907 O SER B 466 3554 1555 3.10
LINK OD1 ASP B 172 ZN ZN B 905 1555 1555 2.28
LINK OG1 THR B 210 ZN ZN B 905 1555 1555 2.49
LINK OD1 ASP B 312 ZN ZN B 904 1555 1555 2.66
LINK OD2 ASP B 312 ZN ZN B 904 1555 1555 1.95
LINK NE2 HIS B 316 ZN ZN B 904 1555 1555 2.28
LINK OD2 ASP B 359 ZN ZN B 905 1555 1555 2.40
LINK NE2 HIS B 360 ZN ZN B 905 1555 1555 2.40
LINK NE2 HIS B 475 ZN ZN B 904 1555 1555 1.94
LINK O TYR B 670 NA NA B 907 1555 1555 2.31
LINK O ASP B 673 NA NA B 907 1555 1555 2.77
LINK O MET B 676 NA NA B 907 1555 1555 2.95
LINK OD1 ASP B 740 CA CA B 906 1555 1555 2.29
LINK OD1 ASP B 742 CA CA B 906 1555 1555 2.18
LINK OD2 ASP B 744 CA CA B 906 1555 1555 2.90
LINK O LEU B 746 CA CA B 906 1555 1555 2.33
LINK OD1 ASP B 748 CA CA B 906 1555 1555 2.17
LINK O ASN B 802 NA NA B 908 1555 1555 2.72
LINK O SER B 805 NA NA B 908 1555 1555 2.42
LINK OG SER B 808 NA NA B 908 1555 1555 2.28
LINK ZN ZN B 904 O1 EDO B 911 1555 1555 2.12
LINK CA CA B 906 O HOH B1001 1555 1555 2.29
LINK NA NA B 907 O HOH B1006 1555 1555 2.58
LINK NA NA B 908 O HOH B1008 1555 1555 2.21
CISPEP 1 TYR A 206 PRO A 207 0 -2.34
CISPEP 2 GLN A 310 PRO A 311 0 13.58
CISPEP 3 TYR B 206 PRO B 207 0 -9.16
CISPEP 4 GLN B 310 PRO B 311 0 5.99
CRYST1 127.460 209.991 188.193 90.00 90.00 90.00 C 2 2 21 16
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 0.007846 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005314 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
