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HEADER HYDROLASE 19-DEC-18 6QAE
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH (S)-N2-BUTYL-N1-(2-
TITLE 2 CYCLOHEPTYLETHYL)-3-(1H-INDOL-3-YL)-N1,N2-DIMETHYLPROPANE-1,2-DIAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: NAG AND FUC ARE GLYCOSYLATION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS BUTYRYLCHOLINESTERASE, INHIBITOR, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,F.NACHON,M.HARST,D.KNEZ,S.GOBEC
REVDAT 1 27-MAR-19 6QAE 0
JRNL AUTH A.MEDEN,D.KNEZ,M.JUKIC,X.BRAZZOLOTTO,M.GRSIC,A.PISLAR,
JRNL AUTH 2 A.ZAHIROVIC,J.KOS,F.NACHON,J.SVETE,S.GOBEC,U.GROSELJ
JRNL TITL TRYPTOPHAN-DERIVED BUTYRYLCHOLINESTERASE INHIBITORS AS
JRNL TITL 2 PROMISING LEADS AGAINST ALZHEIMER'S DISEASE.
JRNL REF CHEM.COMMUN.(CAMB.) 2019
JRNL REFN ESSN 1364-548X
JRNL PMID 30864579
JRNL DOI 10.1039/C9CC01330J
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 26944
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1300
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 54.8255 - 5.1711 0.99 3014 147 0.1943 0.2303
REMARK 3 2 5.1711 - 4.1048 1.00 2872 164 0.1603 0.2105
REMARK 3 3 4.1048 - 3.5861 1.00 2831 156 0.1739 0.2205
REMARK 3 4 3.5861 - 3.2582 1.00 2862 137 0.2038 0.2523
REMARK 3 5 3.2582 - 3.0247 1.00 2796 161 0.2271 0.2852
REMARK 3 6 3.0247 - 2.8464 1.00 2833 135 0.2388 0.2659
REMARK 3 7 2.8464 - 2.7039 1.00 2834 120 0.2416 0.3028
REMARK 3 8 2.7039 - 2.5862 1.00 2823 131 0.2525 0.3403
REMARK 3 9 2.5862 - 2.4866 1.00 2807 149 0.2611 0.3204
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.93
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 : 0.004 4554
REMARK 3 ANGLE : 0.710 6212
REMARK 3 CHIRALITY : 0.053 684
REMARK 3 PLANARITY : 0.004 781
REMARK 3 DIHEDRAL : 10.904 3609
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 6QAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1200013536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : 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) : 1.0720
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26948
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.487
REMARK 200 RESOLUTION RANGE LOW (A) : 54.812
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.300
REMARK 200 R MERGE (I) : 0.07352
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.84330
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE MES PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 76.87200
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.47000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 76.87200
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.47000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 76.87200
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.47000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 76.87200
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.47000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 76.87200
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.47000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 76.87200
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.47000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 76.87200
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.47000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 76.87200
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 76.87200
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.47000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 -27
REMARK 465 ASP A -26
REMARK 465 SER A -25
REMARK 465 LYS A -24
REMARK 465 VAL A -23
REMARK 465 THR A -22
REMARK 465 ILE A -21
REMARK 465 ILE A -20
REMARK 465 CYS A -19
REMARK 465 ILE A -18
REMARK 465 ARG A -17
REMARK 465 PHE A -16
REMARK 465 LEU A -15
REMARK 465 PHE A -14
REMARK 465 TRP A -13
REMARK 465 PHE A -12
REMARK 465 LEU A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 CYS A -8
REMARK 465 MET A -7
REMARK 465 LEU A -6
REMARK 465 ILE A -5
REMARK 465 GLY A -4
REMARK 465 LYS A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 THR A 0
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
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 GLN A 486 CG CD OE1 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 OD1 ASP A 378 O HOH A 701 1.88
REMARK 500 O ASP A 378 NH2 ARG A 381 2.00
REMARK 500 O TRP A 52 O HOH A 702 2.03
REMARK 500 O1 SO4 A 614 O HOH A 703 2.18
REMARK 500 O HOH A 704 O HOH A 799 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 43 -6.65 78.62
REMARK 500 ALA A 58 62.35 -101.17
REMARK 500 ASN A 106 51.07 -152.18
REMARK 500 PHE A 153 11.63 -140.39
REMARK 500 ALA A 162 71.55 -155.64
REMARK 500 SER A 198 -121.17 59.55
REMARK 500 ASN A 256 99.72 -63.07
REMARK 500 ASP A 297 -72.35 -119.37
REMARK 500 VAL A 377 -12.87 -49.15
REMARK 500 ASP A 378 128.15 178.12
REMARK 500 PHE A 398 -57.55 -139.12
REMARK 500 PRO A 449 -8.99 -59.90
REMARK 500 GLU A 506 -72.89 -85.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HUK A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 601 through FUC A 602 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800 to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 607 through FUC A 609 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 610 bound
REMARK 800 to ASN A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 604 through FUC A 606 bound to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 611 bound
REMARK 800 to ASN A 485
DBREF 6QAE A -27 529 UNP P06276 CHLE_HUMAN 1 557
SEQADV 6QAE ASP A -26 UNP P06276 HIS 2 CONFLICT
SEQADV 6QAE GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 6QAE GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 6QAE GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 6QAE GLN A 486 UNP P06276 ASN 514 ENGINEERED MUTATION
SEQRES 1 A 557 MET ASP SER LYS VAL THR ILE ILE CYS ILE ARG PHE LEU
SEQRES 2 A 557 PHE TRP PHE LEU LEU LEU CYS MET LEU ILE GLY LYS SER
SEQRES 3 A 557 HIS THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY
SEQRES 4 A 557 LYS VAL ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR
SEQRES 5 A 557 VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 6 A 557 LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR
SEQRES 7 A 557 LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN
SEQRES 8 A 557 SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE
SEQRES 9 A 557 HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER
SEQRES 10 A 557 GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO
SEQRES 11 A 557 LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY
SEQRES 12 A 557 GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR
SEQRES 13 A 557 ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL
SEQRES 14 A 557 VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU
SEQRES 15 A 557 ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY
SEQRES 16 A 557 LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS
SEQRES 17 A 557 ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR
SEQRES 18 A 557 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU
SEQRES 19 A 557 HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG
SEQRES 20 A 557 ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA
SEQRES 21 A 557 VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN
SEQRES 22 A 557 LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR
SEQRES 23 A 557 GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU
SEQRES 24 A 557 ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR
SEQRES 25 A 557 PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP
SEQRES 26 A 557 PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY
SEQRES 27 A 557 GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS
SEQRES 28 A 557 ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY
SEQRES 29 A 557 PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU
SEQRES 30 A 557 PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER
SEQRES 31 A 557 GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP
SEQRES 32 A 557 TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA
SEQRES 33 A 557 LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO
SEQRES 34 A 557 ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN
SEQRES 35 A 557 ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS
SEQRES 36 A 557 LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR
SEQRES 37 A 557 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG
SEQRES 38 A 557 ASP GLN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER
SEQRES 39 A 557 ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN
SEQRES 40 A 557 PRO GLN GLU THR GLN ASN GLN SER THR SER TRP PRO VAL
SEQRES 41 A 557 PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR
SEQRES 42 A 557 GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN
SEQRES 43 A 557 CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL
HET NAG A 601 14
HET FUC A 602 10
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET FUC A 606 10
HET NAG A 607 14
HET NAG A 608 14
HET FUC A 609 10
HET NAG A 610 14
HET NAG A 611 14
HET HUK A 612 29
HET SO4 A 613 5
HET SO4 A 614 5
HET SO4 A 615 5
HET SO4 A 616 5
HET SO4 A 617 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM HUK BUTYL-[(2~{S})-1-[2-CYCLOHEPTYLETHYL(METHYL)AZANIUMYL]-
HETNAM 2 HUK 3-(1~{H}-INDOL-3-YL)PROPAN-2-YL]-METHYL-AZANIUM
HETNAM SO4 SULFATE ION
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 FUC 3(C6 H12 O5)
FORMUL 8 HUK C26 H45 N3 2+
FORMUL 9 SO4 5(O4 S 2-)
FORMUL 14 HOH *110(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 SER A 198 SER A 210 1 13
HELIX 9 AA9 PRO A 211 PHE A 217 5 7
HELIX 10 AB1 SER A 235 THR A 250 1 16
HELIX 11 AB2 ASN A 256 ARG A 265 1 10
HELIX 12 AB3 ASP A 268 GLU A 276 1 9
HELIX 13 AB4 ALA A 277 VAL A 280 5 4
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 VAL A 331 1 6
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 THR A 374 1 13
HELIX 18 AB9 GLU A 383 PHE A 398 1 16
HELIX 19 AC1 PHE A 398 GLU A 411 1 14
HELIX 20 AC2 PRO A 431 GLY A 435 5 5
HELIX 21 AC3 GLU A 441 PHE A 446 1 6
HELIX 22 AC4 GLY A 447 GLU A 451 5 5
HELIX 23 AC5 THR A 457 GLY A 478 1 22
HELIX 24 AC6 ARG A 515 SER A 524 1 10
HELIX 25 AC7 PHE A 525 VAL A 529 5 5
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA211 MET A 16 VAL A 20 0
SHEET 2 AA211 GLY A 23 PRO A 32 -1 O ALA A 27 N MET A 16
SHEET 3 AA211 TYR A 94 ALA A 101 -1 O LEU A 95 N ILE A 31
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N LEU A 110 O ILE A 140
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O GLN A 223 N GLY A 196
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 501 N PHE A 418
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.03
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.00
LINK ND2 ASN A 57 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 607 1555 1555 1.45
LINK ND2 ASN A 256 C1 NAG A 610 1555 1555 1.46
LINK ND2 ASN A 341 C1 NAG A 605 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A 611 1555 1555 1.44
LINK O6 NAG A 601 C1 FUC A 602 1555 1555 1.44
LINK C1 NAG A 604 O4 NAG A 605 1555 1555 1.45
LINK O6 NAG A 605 C1 FUC A 606 1555 1555 1.46
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.45
LINK O6 NAG A 607 C1 FUC A 609 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 -0.54
SITE 1 AC1 12 ASN A 68 ILE A 69 TRP A 82 GLY A 117
SITE 2 AC1 12 THR A 120 SER A 198 PRO A 285 LEU A 286
SITE 3 AC1 12 SER A 287 VAL A 288 TYR A 332 HIS A 438
SITE 1 AC2 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC3 4 LEU A 286 VAL A 288 HOH A 703 HOH A 754
SITE 1 AC4 3 SER A 487 THR A 488 THR A 508
SITE 1 AC5 2 ARG A 347 GLN A 351
SITE 1 AC6 4 LYS A 323 TYR A 420 ARG A 509 ARG A 515
SITE 1 AC7 2 ARG A 14 ASN A 57
SITE 1 AC8 2 ASN A 106 ASN A 188
SITE 1 AC9 4 ASN A 241 ASN A 245 LEU A 249 PHE A 278
SITE 1 AD1 1 ASN A 256
SITE 1 AD2 3 GLY A 336 ASN A 341 HOH A 712
SITE 1 AD3 3 ARG A 465 GLU A 482 ASN A 485
CRYST1 153.744 153.744 126.940 90.00 90.00 90.00 I 4 2 2 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 0.006504 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007878 0.00000
TER 4223 VAL A 529
MASTER 392 0 17 25 14 0 14 6 4497 1 208 43
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