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HEADER HYDROLASE 10-JUL-18 6H14
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)PYRIDIN-2-
TITLE 4 YL)UREA
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 6H14 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. 1.86 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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 123607
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 6202
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 46.5081 - 5.7759 0.98 4190 219 0.1932 0.2344
REMARK 3 2 5.7759 - 4.5858 0.99 4060 225 0.1456 0.1625
REMARK 3 3 4.5858 - 4.0065 0.99 4021 212 0.1388 0.1666
REMARK 3 4 4.0065 - 3.6403 1.00 4020 216 0.1516 0.1731
REMARK 3 5 3.6403 - 3.3795 0.99 3957 217 0.1622 0.1835
REMARK 3 6 3.3795 - 3.1803 0.98 3910 212 0.1763 0.1857
REMARK 3 7 3.1803 - 3.0210 0.99 3955 214 0.1810 0.2187
REMARK 3 8 3.0210 - 2.8896 0.99 3931 202 0.1720 0.2273
REMARK 3 9 2.8896 - 2.7783 0.99 3954 211 0.1765 0.2017
REMARK 3 10 2.7783 - 2.6825 0.99 3936 226 0.1761 0.2262
REMARK 3 11 2.6825 - 2.5986 0.99 3980 199 0.1726 0.1888
REMARK 3 12 2.5986 - 2.5243 0.99 3920 211 0.1768 0.2387
REMARK 3 13 2.5243 - 2.4579 0.99 3933 204 0.1762 0.2147
REMARK 3 14 2.4579 - 2.3979 0.99 3953 199 0.1791 0.2517
REMARK 3 15 2.3979 - 2.3434 0.99 3889 231 0.1748 0.2232
REMARK 3 16 2.3434 - 2.2935 0.99 3921 199 0.1758 0.2010
REMARK 3 17 2.2935 - 2.2477 0.96 3799 198 0.1731 0.2277
REMARK 3 18 2.2477 - 2.2052 0.98 3905 198 0.1832 0.2376
REMARK 3 19 2.2052 - 2.1659 0.99 3906 224 0.1927 0.2424
REMARK 3 20 2.1659 - 2.1291 0.99 3883 204 0.1899 0.2403
REMARK 3 21 2.1291 - 2.0948 0.99 3900 218 0.2009 0.2531
REMARK 3 22 2.0948 - 2.0626 0.99 3860 224 0.1988 0.2249
REMARK 3 23 2.0626 - 2.0322 0.99 3863 210 0.2067 0.2578
REMARK 3 24 2.0322 - 2.0036 0.99 3894 196 0.2056 0.2474
REMARK 3 25 2.0036 - 1.9765 0.98 3927 196 0.2213 0.2783
REMARK 3 26 1.9765 - 1.9509 0.98 3816 208 0.2373 0.2789
REMARK 3 27 1.9509 - 1.9265 0.97 3902 177 0.2401 0.2701
REMARK 3 28 1.9265 - 1.9033 0.96 3821 173 0.2543 0.2830
REMARK 3 29 1.9033 - 1.8811 0.95 3722 195 0.2650 0.3167
REMARK 3 30 1.8811 - 1.8600 0.94 3677 184 0.2745 0.3141
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.590
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 : 0.008 9215
REMARK 3 ANGLE : 1.006 12520
REMARK 3 CHIRALITY : 0.054 1294
REMARK 3 PLANARITY : 0.006 1599
REMARK 3 DIHEDRAL : 13.627 5521
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 6H14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1200010883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-15
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123623
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 46.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.96400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2XI4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES PH 6.0, 30% PEG 2000, 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 45.79550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.34900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.96300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.34900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.79550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.96300
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: 5200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 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 GLN A 488
REMARK 465 GLU A 489
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 GLN B 488
REMARK 465 GLU B 489
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 413 CD CE NZ
REMARK 470 LYS A 454 CE NZ
REMARK 470 HIS A 486 ND1 CD2 CE1 NE2
REMARK 470 LYS A 511 CE NZ
REMARK 470 LYS B 413 CD CE NZ
REMARK 470 LYS B 454 CE NZ
REMARK 470 HIS B 486 ND1 CD2 CE1 NE2
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 O4 PGE B 611 O HOH B 701 2.02
REMARK 500 O HOH B 701 O HOH B 1190 2.09
REMARK 500 OBL FW8 B 609 O HOH B 702 2.09
REMARK 500 OD1 ASN B 65 O HOH B 703 2.11
REMARK 500 NE2 GLN B 74 O HOH B 704 2.12
REMARK 500 O HOH A 702 O HOH A 1060 2.13
REMARK 500 O HOH B 736 O HOH B 956 2.14
REMARK 500 O HOH B 1089 O HOH B 1214 2.14
REMARK 500 O2 GOL A 607 O HOH A 701 2.15
REMARK 500 ND2 ASN A 65 O HOH A 702 2.17
REMARK 500 O HOH B 1257 O HOH B 1265 2.17
REMARK 500 O HOH B 1004 O HOH B 1234 2.18
REMARK 500 O HOH A 1083 O HOH A 1134 2.18
REMARK 500 OE1 GLN A 526 O HOH A 701 2.19
REMARK 500 OG SER B 4 O HOH B 705 2.19
REMARK 500 O HOH B 1033 O HOH B 1144 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 PHE A 45 -5.61 77.05
REMARK 500 ALA A 60 44.01 -106.53
REMARK 500 SER A 108 77.36 -154.27
REMARK 500 SER A 200 -121.79 59.06
REMARK 500 GLU A 299 -72.19 -129.39
REMARK 500 ASP A 380 52.96 -161.52
REMARK 500 VAL A 400 -60.27 -129.09
REMARK 500 HIS A 486 131.57 73.33
REMARK 500 SER B 25 -159.66 -131.81
REMARK 500 PHE B 45 -9.50 81.68
REMARK 500 ALA B 60 44.60 -108.20
REMARK 500 SER B 108 73.68 -155.24
REMARK 500 SER B 200 -122.03 54.45
REMARK 500 GLU B 299 -76.33 -123.58
REMARK 500 ASP B 380 46.33 -158.41
REMARK 500 VAL B 400 -59.24 -129.24
REMARK 500 PRO B 485 82.48 -60.05
REMARK 500 HIS B 486 126.03 155.24
REMARK 500 ASN B 506 -169.57 -165.49
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 A1213 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A1214 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A1215 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1216 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH B1263 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B1264 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B1265 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH B1266 DISTANCE = 9.49 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FW8 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FW8 B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800 to ASN A 457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 601 through NAG B 602 bound to ASN B 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound
REMARK 800 to ASN B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 457
DBREF 6H14 A 1 565 UNP P04058 ACES_TETCF 22 586
DBREF 6H14 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 NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET EDO A 604 4
HET EDO A 605 4
HET PEG A 606 7
HET GOL A 607 6
HET EDO A 608 4
HET EDO A 609 4
HET FW8 A 610 92
HET PGE A 611 10
HET SO4 A 612 5
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET EDO B 605 4
HET GOL B 606 6
HET EDO B 607 4
HET EDO B 608 4
HET FW8 B 609 92
HET CL B 610 1
HET PGE B 611 10
HET MES B 612 12
HET EDO B 613 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETNAM FW8 1-[(10~{B}~{S})-6-OXIDANYLIDENE-2,3,4,10~{B}-
HETNAM 2 FW8 TETRAHYDRO-1~{H}-PYRIDO[2,1-A]ISOINDOL-10-YL]-3-[4-[1-
HETNAM 3 FW8 [2-(1,2,3,4-TETRAHYDROACRIDIN-9-YLAMINO)ETHYL]-1,2,3-
HETNAM 4 FW8 TRIAZOL-4-YL]PYRIDIN-2-YL]UREA
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 6 EDO 8(C2 H6 O2)
FORMUL 8 PEG C4 H10 O3
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 12 FW8 2(C35 H35 N9 O2)
FORMUL 13 PGE 2(C6 H14 O4)
FORMUL 14 SO4 O4 S 2-
FORMUL 23 CL CL 1-
FORMUL 25 MES C6 H13 N O4 S
FORMUL 27 HOH *1082(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 LYS A 269 1 12
HELIX 12 AB3 LYS A 270 VAL A 277 1 8
HELIX 13 AB4 GLU A 278 LEU A 282 5 5
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 SER A 348 VAL A 360 1 13
HELIX 17 AB8 ASN A 364 THR A 376 1 13
HELIX 18 AB9 ASN A 383 VAL A 400 1 18
HELIX 19 AC1 VAL A 400 LYS A 413 1 14
HELIX 20 AC2 PRO A 433 GLY A 437 5 5
HELIX 21 AC3 GLU A 443 PHE A 448 1 6
HELIX 22 AC4 GLY A 449 ASN A 457 5 9
HELIX 23 AC5 THR A 459 GLY A 480 1 22
HELIX 24 AC6 ARG A 517 GLN A 526 1 10
HELIX 25 AC7 GLN A 526 THR A 535 1 10
HELIX 26 AC8 VAL B 40 ARG B 44 5 5
HELIX 27 AC9 PHE B 78 MET B 83 1 6
HELIX 28 AD1 LEU B 127 ASN B 131 5 5
HELIX 29 AD2 GLY B 132 GLU B 140 1 9
HELIX 30 AD3 VAL B 150 LEU B 156 1 7
HELIX 31 AD4 ASN B 167 ILE B 184 1 18
HELIX 32 AD5 GLN B 185 PHE B 187 5 3
HELIX 33 AD6 SER B 200 SER B 212 1 13
HELIX 34 AD7 SER B 212 ASP B 217 1 6
HELIX 35 AD8 VAL B 238 LEU B 252 1 15
HELIX 36 AD9 SER B 258 GLU B 268 1 11
HELIX 37 AE1 LYS B 270 GLU B 278 1 9
HELIX 38 AE2 TRP B 279 LEU B 282 5 4
HELIX 39 AE3 SER B 304 GLY B 312 1 9
HELIX 40 AE4 GLY B 328 ALA B 336 1 9
HELIX 41 AE5 SER B 348 VAL B 360 1 13
HELIX 42 AE6 ASN B 364 THR B 376 1 13
HELIX 43 AE7 ASN B 383 VAL B 400 1 18
HELIX 44 AE8 VAL B 400 LYS B 413 1 14
HELIX 45 AE9 PRO B 433 GLY B 437 5 5
HELIX 46 AF1 GLU B 443 PHE B 448 1 6
HELIX 47 AF2 GLY B 449 ASN B 457 5 9
HELIX 48 AF3 THR B 459 GLY B 480 1 22
HELIX 49 AF4 ARG B 517 GLN B 526 1 10
HELIX 50 AF5 GLN B 526 ASN B 533 1 8
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
SHEET 1 AA6 2 VAL B 236 SER B 237 0
SHEET 2 AA6 2 VAL B 295 ILE B 296 1 O ILE B 296 N VAL B 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.05
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.05
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 2.03
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.04
LINK ND2 ASN A 59 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 602 1555 1555 1.52
LINK ND2 ASN A 457 C1 NAG A 603 1555 1555 1.48
LINK ND2 ASN B 59 C1 NAG B 601 1555 1555 1.41
LINK ND2 ASN B 416 C1 NAG B 603 1555 1555 1.48
LINK ND2 ASN B 457 C1 NAG B 604 1555 1555 1.49
LINK O4 NAG B 601 C1 NAG B 602 1555 1555 1.42
CISPEP 1 SER A 103 PRO A 104 0 4.37
CISPEP 2 SER B 103 PRO B 104 0 2.04
SITE 1 AC1 2 GLN A 500 VAL A 518
SITE 1 AC2 3 THR A 376 HOH A1058 GLN B 519
SITE 1 AC3 4 VAL A 238 ILE A 296 HOH A 762 HOH A 932
SITE 1 AC4 8 MET A 405 HIS A 406 ASN A 409 CYS A 521
SITE 2 AC4 8 ASN A 525 GLN A 526 HOH A 701 HOH A 726
SITE 1 AC5 3 GLY A 41 ASN A 42 ARG A 267
SITE 1 AC6 2 SER A 55 VAL A 57
SITE 1 AC7 15 TRP A 84 TYR A 121 GLU A 199 TRP A 279
SITE 2 AC7 15 LEU A 282 SER A 286 PHE A 288 PHE A 290
SITE 3 AC7 15 PHE A 330 PHE A 331 TYR A 334 TRP A 432
SITE 4 AC7 15 HIS A 440 HOH A 786 HOH A1057
SITE 1 AC8 3 SER A 79 MET A 83 HOH A 745
SITE 1 AC9 8 LYS A 325 ASP A 326 ARG A 388 ASP A 389
SITE 2 AC9 8 TRP A 435 GLY A 437 HOH A 780 HOH A 924
SITE 1 AD1 3 ASN A 42 THR B 459 THR B 507
SITE 1 AD2 7 MET B 405 HIS B 406 ASN B 409 CYS B 521
SITE 2 AD2 7 ASN B 525 HOH B 711 HOH B 724
SITE 1 AD3 3 TRP B 58 ASN B 59 EDO B 608
SITE 1 AD4 3 SER B 55 VAL B 57 EDO B 607
SITE 1 AD5 16 TRP B 84 TYR B 121 GLU B 199 TRP B 279
SITE 2 AD5 16 LEU B 282 SER B 286 PHE B 288 PHE B 330
SITE 3 AD5 16 PHE B 331 TYR B 334 TRP B 432 HIS B 440
SITE 4 AD5 16 HOH B 702 HOH B 727 HOH B 843 HOH B1087
SITE 1 AD6 1 TRP B 435
SITE 1 AD7 5 MET B 83 ASN B 429 HOH B 701 HOH B 707
SITE 2 AD7 5 HOH B 762
SITE 1 AD8 5 ASN B 481 ASN B 483 LYS B 491 HOH B 732
SITE 2 AD8 5 HOH B 743
SITE 1 AD9 5 THR B 412 THR B 496 THR B 497 HOH B 952
SITE 2 AD9 5 HOH B1162
SITE 1 AE1 2 ASN A 59 SER A 61
SITE 1 AE2 5 ASN A 416 HOH A 729 HOH A 735 HOH A 812
SITE 2 AE2 5 HOH A 955
SITE 1 AE3 2 ASN A 457 HOH A 704
SITE 1 AE4 4 ASN B 59 SER B 61 HOH B 717 HOH B 769
SITE 1 AE5 3 ASN B 416 HOH B 740 HOH B1081
SITE 1 AE6 2 GLU B 455 ASN B 457
CRYST1 91.591 107.926 150.698 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 0.010918 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009266 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006636 0.00000
TER 4289 THR A 535
TER 8556 THR B 535
MASTER 495 0 25 50 32 0 37 6 9793 2 388 88
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