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HEADER HYDROLASE 10-JUL-18 6H12
TITLE CRYSTAL STRUCTURE OF TCACHE COMPLEXED TO 1-(6-OXO-1,2,3,4,6,10B-
TITLE 2 HEXAHYDROPYRIDO[2,1-A]ISOINDOL-10-YL)-3-(4-(((1-(2-((1,2,3,4-
TITLE 3 TETRAHYDROACRIDIN-9-YL)AMINO)ETHYL)-1H-1,2,3-TRIAZOL-4-YL)METHOXY)
TITLE 4 METHYL)PYRIDIN-2-YL)UREA
CAVEAT 6H12 FJK A 626 HAS WRONG CHIRALITY AT ATOM CBR FJK A 626 HAS
CAVEAT 2 6H12 WRONG CHIRALITY AT ATOM CBT FJK B 619 HAS WRONG CHIRALITY
CAVEAT 3 6H12 AT ATOM CBR FJK B 619 HAS WRONG CHIRALITY AT ATOM CBT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS COMPLEX, INHIBITOR, ALZHEIMER, ACETYLCHOLINESTERASE, MULTI-TARGET-
KEYWDS 2 DIRECTED LIGANDS, MTDL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,J.P.COLLETIER
REVDAT 1 15-MAY-19 6H12 0
JRNL AUTH K.OUKOLOFF,N.COQUELLE,M.BARTOLINI,M.NALDI,R.LE GUEVEL,
JRNL AUTH 2 S.BACH,B.JOSSELIN,S.RUCHAUD,M.CATTO,L.PISANI,N.DENORA,
JRNL AUTH 3 R.M.IACOBAZZI,I.SILMAN,J.L.SUSSMAN,F.BURON,J.P.COLLETIER,
JRNL AUTH 4 L.JEAN,S.ROUTIER,P.Y.RENARD
JRNL TITL DESIGN, BIOLOGICAL EVALUATION AND X-RAY CRYSTALLOGRAPHY OF
JRNL TITL 2 NANOMOLAR MULTIFUNCTIONAL LIGANDS TARGETING SIMULTANEOUSLY
JRNL TITL 3 ACETYLCHOLINESTERASE AND GLYCOGEN SYNTHASE KINASE-3.
JRNL REF EUR.J.MED.CHEM. V. 168 58 2019
JRNL REFN ISSN 0223-5234
JRNL PMID 30798053
JRNL DOI 10.1016/J.EJMECH.2018.12.063
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 73462
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.720
REMARK 3 FREE R VALUE TEST SET COUNT : 1997
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 19.8851 - 5.2716 0.99 5360 150 0.1892 0.2092
REMARK 3 2 5.2716 - 4.1971 1.00 5189 146 0.1512 0.1960
REMARK 3 3 4.1971 - 3.6704 1.00 5151 142 0.1495 0.1739
REMARK 3 4 3.6704 - 3.3365 1.00 5119 144 0.1625 0.1957
REMARK 3 5 3.3365 - 3.0983 1.00 5084 142 0.1693 0.2155
REMARK 3 6 3.0983 - 2.9162 1.00 5101 143 0.1752 0.2113
REMARK 3 7 2.9162 - 2.7706 1.00 5053 142 0.1687 0.2305
REMARK 3 8 2.7706 - 2.6503 1.00 5110 142 0.1694 0.2154
REMARK 3 9 2.6503 - 2.5484 1.00 5074 142 0.1728 0.2408
REMARK 3 10 2.5484 - 2.4607 1.00 5025 141 0.1815 0.2342
REMARK 3 11 2.4607 - 2.3839 1.00 5082 142 0.1835 0.2472
REMARK 3 12 2.3839 - 2.3158 1.00 5038 139 0.1961 0.2307
REMARK 3 13 2.3158 - 2.2549 1.00 5049 142 0.1981 0.2899
REMARK 3 14 2.2549 - 2.2000 1.00 5030 140 0.2081 0.2389
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 9246
REMARK 3 ANGLE : 0.963 12521
REMARK 3 CHIRALITY : 0.052 1285
REMARK 3 PLANARITY : 0.006 1602
REMARK 3 DIHEDRAL : 13.452 5493
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 6H12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200010873.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.872600
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73534
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.58700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
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: 2XI4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 200/50 MM MES PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 45.63500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.84500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.84500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.63500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.54500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ASP A 538
REMARK 465 GLY A 539
REMARK 465 GLU A 540
REMARK 465 LEU A 541
REMARK 465 SER A 542
REMARK 465 SER A 543
REMARK 465 SER A 544
REMARK 465 GLY A 545
REMARK 465 THR A 546
REMARK 465 SER A 547
REMARK 465 SER A 548
REMARK 465 SER A 549
REMARK 465 LYS A 550
REMARK 465 GLY A 551
REMARK 465 ILE A 552
REMARK 465 ILE A 553
REMARK 465 PHE A 554
REMARK 465 TYR A 555
REMARK 465 VAL A 556
REMARK 465 LEU A 557
REMARK 465 PHE A 558
REMARK 465 SER A 559
REMARK 465 ILE A 560
REMARK 465 LEU A 561
REMARK 465 TYR A 562
REMARK 465 LEU A 563
REMARK 465 ILE A 564
REMARK 465 PHE A 565
REMARK 465 ASP B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 536
REMARK 465 CYS B 537
REMARK 465 ASP B 538
REMARK 465 GLY B 539
REMARK 465 GLU B 540
REMARK 465 LEU B 541
REMARK 465 SER B 542
REMARK 465 SER B 543
REMARK 465 SER B 544
REMARK 465 GLY B 545
REMARK 465 THR B 546
REMARK 465 SER B 547
REMARK 465 SER B 548
REMARK 465 SER B 549
REMARK 465 LYS B 550
REMARK 465 GLY B 551
REMARK 465 ILE B 552
REMARK 465 ILE B 553
REMARK 465 PHE B 554
REMARK 465 TYR B 555
REMARK 465 VAL B 556
REMARK 465 LEU B 557
REMARK 465 PHE B 558
REMARK 465 SER B 559
REMARK 465 ILE B 560
REMARK 465 LEU B 561
REMARK 465 TYR B 562
REMARK 465 LEU B 563
REMARK 465 ILE B 564
REMARK 465 PHE B 565
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 454 CE NZ
REMARK 470 LYS B 454 CE NZ
REMARK 470 LYS B 511 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C1 PGE A 603 C2 GOL A 609 1.50
REMARK 500 ND2 ASN B 457 C1 NAG B 617 1.61
REMARK 500 O HOH A 798 O HOH A 1013 2.12
REMARK 500 OE1 GLU B 140 O HOH B 701 2.14
REMARK 500 O HOH A 702 O HOH A 759 2.16
REMARK 500 NH1 ARG A 468 O HOH A 701 2.17
REMARK 500 ND2 ASN B 9 O HOH B 702 2.17
REMARK 500 O HOH A 703 O HOH A 1009 2.17
REMARK 500 O HOH A 980 O HOH A 1047 2.18
REMARK 500 O HOH A 875 O HOH A 906 2.18
REMARK 500 ND2 ASN A 533 O HOH A 702 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 25 -156.05 -126.65
REMARK 500 PHE A 45 -5.78 76.47
REMARK 500 ALA A 60 52.72 -115.74
REMARK 500 SER A 108 79.47 -154.24
REMARK 500 PHE A 155 13.06 -140.41
REMARK 500 LEU A 158 79.77 -116.64
REMARK 500 SER A 200 -120.20 60.95
REMARK 500 GLU A 299 -69.38 -122.86
REMARK 500 ASP A 380 46.72 -160.48
REMARK 500 VAL A 400 -63.28 -126.86
REMARK 500 HIS A 486 -13.97 82.50
REMARK 500 ASN A 506 -166.03 -163.03
REMARK 500 ARG A 517 44.24 39.20
REMARK 500 GLN A 526 -53.66 -121.04
REMARK 500 LEU B 23 -124.58 53.08
REMARK 500 SER B 25 -157.44 -142.45
REMARK 500 PHE B 45 -5.66 77.67
REMARK 500 ALA B 60 56.72 -106.14
REMARK 500 PRO B 102 155.06 -49.69
REMARK 500 SER B 108 74.59 -162.51
REMARK 500 SER B 108 73.65 -162.06
REMARK 500 SER B 200 -119.78 59.67
REMARK 500 GLU B 299 -73.62 -123.47
REMARK 500 THR B 317 -159.32 -162.21
REMARK 500 ASP B 380 53.05 -163.23
REMARK 500 VAL B 400 -61.44 -129.49
REMARK 500 ARG B 517 46.42 36.87
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 A1062 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1083 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH B1084 DISTANCE = 8.84 ANGSTROMS
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 NAG B 617
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FJK A 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FJK B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 619 bound
REMARK 800 to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 620 bound
REMARK 800 to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 615 bound
REMARK 800 to ASN B 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 616 bound
REMARK 800 to ASN B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues PGE A 603 and GOL A
REMARK 800 609
DBREF 6H12 A 1 565 UNP P04058 ACES_TETCF 22 586
DBREF 6H12 B 1 565 UNP P04058 ACES_TETCF 22 586
SEQRES 1 A 565 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 565 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 565 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 565 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 565 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 565 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 565 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 565 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 565 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 565 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 565 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 565 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 565 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 565 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 565 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 565 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 565 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 565 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 565 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 565 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 565 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 565 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 565 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 565 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 565 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 565 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 565 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 565 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 565 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 565 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 565 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 565 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 565 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 565 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 565 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 565 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 565 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 565 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 565 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 565 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 565 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 565 ALA THR ALA CYS ASP GLY GLU LEU SER SER SER GLY THR
SEQRES 43 A 565 SER SER SER LYS GLY ILE ILE PHE TYR VAL LEU PHE SER
SEQRES 44 A 565 ILE LEU TYR LEU ILE PHE
SEQRES 1 B 565 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 B 565 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 B 565 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 B 565 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 B 565 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 B 565 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 B 565 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 B 565 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 B 565 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 B 565 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 B 565 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 B 565 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 565 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 565 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 B 565 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 B 565 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 B 565 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 B 565 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 B 565 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 B 565 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 B 565 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 B 565 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 B 565 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 B 565 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 B 565 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 B 565 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 B 565 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 B 565 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 B 565 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 B 565 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 B 565 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 B 565 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 B 565 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 B 565 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 B 565 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 B 565 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 B 565 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 B 565 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 B 565 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 B 565 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 B 565 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 B 565 ALA THR ALA CYS ASP GLY GLU LEU SER SER SER GLY THR
SEQRES 43 B 565 SER SER SER LYS GLY ILE ILE PHE TYR VAL LEU PHE SER
SEQRES 44 B 565 ILE LEU TYR LEU ILE PHE
HET MES A 601 12
HET GOL A 602 6
HET PGE A 603 10
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET EDO A 607 4
HET EDO A 608 4
HET GOL A 609 6
HET EDO A 610 4
HET MES A 611 12
HET MES A 612 12
HET SO4 A 613 5
HET MES A 614 12
HET PEG A 615 7
HET PEG A 616 7
HET PEG A 617 7
HET PEG A 618 7
HET NAG A 619 14
HET NAG A 620 14
HET CL A 621 1
HET CL A 622 1
HET CL A 623 1
HET CL A 624 1
HET CL A 625 1
HET FJK A 626 49
HET SO4 A 627 5
HET EDO B 601 4
HET EDO B 602 4
HET EDO B 603 4
HET GOL B 604 6
HET PGE B 605 10
HET EDO B 606 4
HET EDO B 607 4
HET SO4 B 608 5
HET EDO B 609 4
HET EDO B 610 4
HET PEG B 611 7
HET PEG B 612 7
HET PEG B 613 7
HET PEG B 614 7
HET NAG B 615 14
HET NAG B 616 14
HET NAG B 617 14
HET CL B 618 1
HET FJK B 619 49
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CL CHLORIDE ION
HETNAM FJK 1-[4-[[1-[2-(1,2,3,4,4~{A},9~{A}-HEXAHYDROACRIDIN-9-
HETNAM 2 FJK YLAMINO)ETHYL]-1,2,3-TRIAZOL-4-
HETNAM 3 FJK YL]METHOXYMETHYL]PYRIDIN-2-YL]-3-[(10~{B}~{R})-6-
HETNAM 4 FJK OXIDANYLIDENE-2,3,4,10~{B}-TETRAHYDRO-1~{H}-PYRIDO[2,
HETNAM 5 FJK 1-A]ISOINDOL-10-YL]UREA
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 MES 4(C6 H13 N O4 S)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 PGE 2(C6 H14 O4)
FORMUL 6 EDO 13(C2 H6 O2)
FORMUL 15 SO4 3(O4 S 2-)
FORMUL 17 PEG 8(C4 H10 O3)
FORMUL 21 NAG 5(C8 H15 N O6)
FORMUL 23 CL 6(CL 1-)
FORMUL 28 FJK 2(C37 H41 N9 O3)
FORMUL 49 HOH *746(H2 O)
HELIX 1 AA1 VAL A 40 ARG A 44 5 5
HELIX 2 AA2 PHE A 78 MET A 83 1 6
HELIX 3 AA3 LEU A 127 ASN A 131 5 5
HELIX 4 AA4 GLY A 132 GLU A 140 1 9
HELIX 5 AA5 VAL A 150 LEU A 156 1 7
HELIX 6 AA6 ASN A 167 ILE A 184 1 18
HELIX 7 AA7 GLN A 185 PHE A 187 5 3
HELIX 8 AA8 SER A 200 SER A 212 1 13
HELIX 9 AA9 PRO A 213 PHE A 219 5 7
HELIX 10 AB1 VAL A 238 LEU A 252 1 15
HELIX 11 AB2 SER A 258 GLU A 268 1 11
HELIX 12 AB3 LYS A 270 GLU A 278 1 9
HELIX 13 AB4 TRP A 279 LEU A 282 5 4
HELIX 14 AB5 SER A 304 GLY A 312 1 9
HELIX 15 AB6 GLY A 328 ALA A 336 1 9
HELIX 16 AB7 PRO A 337 LYS A 341 5 5
HELIX 17 AB8 SER A 348 VAL A 360 1 13
HELIX 18 AB9 ASN A 364 THR A 376 1 13
HELIX 19 AC1 ASN A 383 VAL A 400 1 18
HELIX 20 AC2 VAL A 400 GLY A 415 1 16
HELIX 21 AC3 PRO A 433 GLY A 437 5 5
HELIX 22 AC4 GLU A 443 PHE A 448 1 6
HELIX 23 AC5 GLY A 449 ASN A 457 5 9
HELIX 24 AC6 THR A 459 GLY A 480 1 22
HELIX 25 AC7 ARG A 517 GLN A 526 1 10
HELIX 26 AC8 GLN A 526 THR A 535 1 10
HELIX 27 AC9 VAL B 40 ARG B 44 5 5
HELIX 28 AD1 PHE B 78 MET B 83 1 6
HELIX 29 AD2 LEU B 127 ASN B 131 5 5
HELIX 30 AD3 GLY B 132 GLU B 140 1 9
HELIX 31 AD4 VAL B 150 LEU B 156 1 7
HELIX 32 AD5 ASN B 167 ILE B 184 1 18
HELIX 33 AD6 GLN B 185 PHE B 187 5 3
HELIX 34 AD7 SER B 200 SER B 212 1 13
HELIX 35 AD8 SER B 215 PHE B 219 5 5
HELIX 36 AD9 SER B 237 LEU B 252 1 16
HELIX 37 AE1 SER B 258 LYS B 269 1 12
HELIX 38 AE2 LYS B 270 GLU B 278 1 9
HELIX 39 AE3 TRP B 279 LEU B 282 5 4
HELIX 40 AE4 SER B 304 GLY B 312 1 9
HELIX 41 AE5 GLY B 328 ALA B 336 1 9
HELIX 42 AE6 PRO B 337 LYS B 341 5 5
HELIX 43 AE7 SER B 348 VAL B 360 1 13
HELIX 44 AE8 ASN B 364 THR B 376 1 13
HELIX 45 AE9 ASN B 383 VAL B 400 1 18
HELIX 46 AF1 VAL B 400 GLY B 415 1 16
HELIX 47 AF2 PRO B 433 GLY B 437 5 5
HELIX 48 AF3 GLU B 443 PHE B 448 1 6
HELIX 49 AF4 GLY B 449 ASN B 457 5 9
HELIX 50 AF5 THR B 459 GLY B 480 1 22
HELIX 51 AF6 ARG B 517 GLN B 526 1 10
HELIX 52 AF7 GLN B 526 THR B 535 1 10
SHEET 1 AA1 3 LEU A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 MET A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 AA1 3 VAL A 57 ASN A 59 1 O TRP A 58 N LYS A 14
SHEET 1 AA211 THR A 18 VAL A 22 0
SHEET 2 AA211 SER A 25 PRO A 34 -1 O ILE A 27 N VAL A 20
SHEET 3 AA211 TYR A 96 VAL A 101 -1 O ILE A 99 N PHE A 30
SHEET 4 AA211 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AA211 THR A 109 ILE A 115 1 N TRP A 114 O VAL A 144
SHEET 6 AA211 GLY A 189 GLU A 199 1 O THR A 195 N VAL A 113
SHEET 7 AA211 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
SHEET 8 AA211 ILE A 319 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AA211 THR A 418 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 AA211 LYS A 501 LEU A 505 1 O LEU A 505 N PHE A 422
SHEET 11 AA211 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AA3 2 VAL A 236 SER A 237 0
SHEET 2 AA3 2 VAL A 295 ILE A 296 1 O ILE A 296 N VAL A 236
SHEET 1 AA4 3 LEU B 7 THR B 10 0
SHEET 2 AA4 3 GLY B 13 MET B 16 -1 O VAL B 15 N VAL B 8
SHEET 3 AA4 3 VAL B 57 ASN B 59 1 O TRP B 58 N LYS B 14
SHEET 1 AA511 THR B 18 VAL B 22 0
SHEET 2 AA511 SER B 25 PRO B 34 -1 O ILE B 27 N VAL B 20
SHEET 3 AA511 TYR B 96 VAL B 101 -1 O ILE B 99 N PHE B 30
SHEET 4 AA511 VAL B 142 SER B 145 -1 O LEU B 143 N TRP B 100
SHEET 5 AA511 THR B 109 ILE B 115 1 N TRP B 114 O VAL B 144
SHEET 6 AA511 GLY B 189 GLU B 199 1 O ASP B 190 N THR B 109
SHEET 7 AA511 ARG B 221 GLN B 225 1 O GLN B 225 N GLY B 198
SHEET 8 AA511 ILE B 319 ASN B 324 1 O LEU B 320 N LEU B 224
SHEET 9 AA511 THR B 418 PHE B 423 1 O PHE B 423 N VAL B 323
SHEET 10 AA511 LYS B 501 LEU B 505 1 O LEU B 505 N PHE B 422
SHEET 11 AA511 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.07
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.03
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.05
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.07
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.04
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.03
LINK ND2 ASN A 59 C1 NAG A 619 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 620 1555 1555 1.51
LINK ND2 ASN B 59 C1 NAG B 615 1555 1555 1.45
LINK ND2 ASN B 416 C1 NAG B 616 1555 1555 1.48
CISPEP 1 SER A 103 PRO A 104 0 5.39
CISPEP 2 SER B 103 PRO B 104 0 6.97
SITE 1 AC1 5 GLY A 41 ASN A 42 HIS A 264 ARG A 267
SITE 2 AC1 5 HOH A 966
SITE 1 AC2 6 HIS A 425 ASN A 506 THR A 507 GLU A 508
SITE 2 AC2 6 HOH A 837 HOH B 817
SITE 1 AC3 1 GLN A 500
SITE 1 AC4 5 HIS A 425 THR A 459 GLU A 461 THR A 507
SITE 2 AC4 5 ASN B 42
SITE 1 AC5 1 LYS A 107
SITE 1 AC6 1 PHE A 78
SITE 1 AC7 4 LEU A 430 VAL A 431 TRP A 432 HOH A 861
SITE 1 AC8 4 HIS A 398 PRO A 403 TRP A 524 HOH A 717
SITE 1 AC9 8 SER A 108 THR A 109 THR A 110 GLU A 139
SITE 2 AC9 8 GLU A 140 ASP A 190 THR A 193 LYS A 478
SITE 1 AD1 4 ASN A 481 ASN A 483 PRO A 485 LYS A 491
SITE 1 AD2 5 PRO A 21 VAL A 22 LEU A 23 LYS A 133
SITE 2 AD2 5 TYR A 134
SITE 1 AD3 5 ARG A 242 ARG A 243 VAL A 246 LEU A 256
SITE 2 AD3 5 ASP A 259
SITE 1 AD4 5 LYS A 325 ASP A 326 ASP A 389 ASP A 393
SITE 2 AD4 5 ARG A 517
SITE 1 AD5 2 ASN A 230 SER A 235
SITE 1 AD6 5 ARG A 220 ARG A 221 GLN A 318 THR A 479
SITE 2 AD6 5 HOH A 705
SITE 1 AD7 2 ARG A 216 ASP A 217
SITE 1 AD8 1 TRP B 435
SITE 1 AD9 2 LYS A 454 GLU A 463
SITE 1 AE1 15 TYR A 70 GLN A 74 TRP A 84 TYR A 121
SITE 2 AE1 15 GLU A 199 TRP A 279 PHE A 330 PHE A 331
SITE 3 AE1 15 TRP A 432 HIS A 440 TYR A 442 HOH A 757
SITE 4 AE1 15 HOH A 805 HOH A 806 HOH A 945
SITE 1 AE2 7 HOH A 736 HOH A 962 HOH A 973 THR B 412
SITE 2 AE2 7 THR B 496 THR B 497 HOH B 740
SITE 1 AE3 3 ASN B 230 SER B 235 HOH B 709
SITE 1 AE4 1 GLN B 500
SITE 1 AE5 6 THR B 109 GLU B 139 GLU B 140 LYS B 478
SITE 2 AE5 6 HOH B 748 HOH B 894
SITE 1 AE6 4 SER B 108 ASP B 190 THR B 193 HOH B 894
SITE 1 AE7 5 ARG B 216 ASP B 217 LYS B 315 HOH B 720
SITE 2 AE7 5 HOH B 815
SITE 1 AE8 2 PHE B 75 PEG B 614
SITE 1 AE9 3 ASP B 369 LEU B 373 TRP B 378
SITE 1 AF1 6 PRO B 21 VAL B 22 LEU B 23 LYS B 133
SITE 2 AF1 6 TYR B 134 HOH B 768
SITE 1 AF2 2 TRP B 58 ASN B 59
SITE 1 AF3 2 GLY B 41 GLU B 268
SITE 1 AF4 5 ARG B 242 VAL B 246 LEU B 256 SER B 258
SITE 2 AF4 5 ASP B 259
SITE 1 AF5 1 ILE B 296
SITE 1 AF6 5 GLU B 306 SER B 307 ASN B 310 HOH B 821
SITE 2 AF6 5 HOH B 898
SITE 1 AF7 4 LEU B 333 PHE B 339 EDO B 606 HOH B 735
SITE 1 AF8 3 GLU B 455 ASN B 457 HOH B 718
SITE 1 AF9 1 LYS B 269
SITE 1 AG1 13 TRP B 84 TYR B 121 TRP B 279 PHE B 284
SITE 2 AG1 13 ASP B 285 SER B 286 PHE B 330 GLY B 335
SITE 3 AG1 13 TRP B 432 HIS B 440 HOH B 791 HOH B 794
SITE 4 AG1 13 HOH B 797
SITE 1 AG2 6 ASN A 59 SER A 61 HOH A 712 HOH A 747
SITE 2 AG2 6 HOH A 866 HOH A 913
SITE 1 AG3 4 ASN A 416 HOH A 713 HOH A 798 HOH A 871
SITE 1 AG4 7 ASN B 59 SER B 61 THR B 62 HOH B 711
SITE 2 AG4 7 HOH B 823 HOH B 886 HOH B 908
SITE 1 AG5 6 ASN B 416 HOH B 712 HOH B 733 HOH B 814
SITE 2 AG5 6 HOH B 825 HOH B 907
SITE 1 AG6 6 GLU A 240 PRO A 283 PHE A 284 ARG A 289
SITE 2 AG6 6 HOH A 707 HOH A 964
CRYST1 91.270 105.090 149.690 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010957 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009516 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006680 0.00000
TER 4312 THR A 535
TER 8608 THR B 535
MASTER 547 0 46 52 30 0 66 6 9611 2 393 88
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