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HEADER HYDROLASE 25-OCT-18 6I0B
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE S ENANTIOMER OF A
TITLE 2 CHLOROTACRINE-TRYPTOPHAN MULTI-TARGET INHIBITOR.
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,BUTYRYLCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: (NAG) ARE N-ACETYLGLUCOSAMINE(FUC) ARE FUCOSE
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, HYDROLASE, MULTI-TARGET INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,F.NACHON
REVDAT 1 27-MAR-19 6I0B 0
JRNL AUTH K.CHALUPOVA,J.KORABECNY,M.BARTOLINI,B.MONTI,D.LAMBA,
JRNL AUTH 2 R.CALIANDRO,A.PESARESI,X.BRAZZOLOTTO,A.J.GASTELLIER,
JRNL AUTH 3 F.NACHON,J.PEJCHAL,M.JAROSOVA,V.HEPNAROVA,D.JUN,M.HRABINOVA,
JRNL AUTH 4 R.DOLEZAL,J.ZDAROVA KARASOVA,M.MZIK,Z.KRISTOFIKOVA,J.MISIK,
JRNL AUTH 5 L.MUCKOVA,P.JOST,O.SOUKUP,M.BENKOVA,V.SETNICKA,L.HABARTOVA,
JRNL AUTH 6 M.CHVOJKOVA,L.KLETECKOVA,K.VALES,E.MEZEIOVA,E.ULIASSI,
JRNL AUTH 7 M.VALIS,E.NEPOVIMOVA,M.L.BOLOGNESI,K.KUCA
JRNL TITL NOVEL TACRINE-TRYPTOPHAN HYBRIDS: MULTI-TARGET DIRECTED
JRNL TITL 2 LIGANDS AS POTENTIAL TREATMENT FOR ALZHEIMER'S DISEASE.
JRNL REF EUR.J.MED.CHEM. V. 168 491 2019
JRNL REFN ISSN 0223-5234
JRNL PMID 30851693
JRNL DOI 10.1016/J.EJMECH.2019.02.021
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31033
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
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 : 1583
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 55.2356 - 5.3002 0.99 2816 175 0.1845 0.2403
REMARK 3 2 5.3002 - 4.2074 1.00 2708 153 0.1556 0.2008
REMARK 3 3 4.2074 - 3.6757 1.00 2712 129 0.1643 0.1922
REMARK 3 4 3.6757 - 3.3397 1.00 2657 152 0.1891 0.2400
REMARK 3 5 3.3397 - 3.1003 1.00 2695 135 0.2053 0.2556
REMARK 3 6 3.1003 - 2.9175 1.00 2649 145 0.2081 0.2768
REMARK 3 7 2.9175 - 2.7714 1.00 2625 157 0.2142 0.2970
REMARK 3 8 2.7714 - 2.6508 1.00 2638 147 0.2249 0.3107
REMARK 3 9 2.6508 - 2.5487 1.00 2656 133 0.2356 0.3040
REMARK 3 10 2.5487 - 2.4608 1.00 2657 134 0.2519 0.3542
REMARK 3 11 2.4608 - 2.3838 1.00 2637 123 0.2769 0.3762
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.88
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 : 0.010 4587
REMARK 3 ANGLE : 1.048 6253
REMARK 3 CHIRALITY : 0.056 681
REMARK 3 PLANARITY : 0.006 783
REMARK 3 DIHEDRAL : 12.054 3633
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 6I0B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-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) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31033
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.384
REMARK 200 RESOLUTION RANGE LOW (A) : 55.221
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.07364
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.0200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.78800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.560
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: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.5 AMMONIUM SULPHATE, 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 77.17550
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.17550
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 64.01950
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.17550
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.17550
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 64.01950
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.17550
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.17550
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 64.01950
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.17550
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.17550
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 64.01950
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.17550
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.17550
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 64.01950
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.17550
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.17550
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 64.01950
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.17550
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.17550
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 64.01950
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.17550
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.17550
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.01950
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: 4540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 OH TYR A 420 O2S MES A 612 2.04
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 -5.53 80.48
REMARK 500 ASP A 54 -156.74 -74.93
REMARK 500 ASP A 87 132.59 -39.06
REMARK 500 LYS A 103 126.93 -33.73
REMARK 500 ASN A 106 55.68 -149.09
REMARK 500 PHE A 153 11.86 -143.47
REMARK 500 ALA A 162 67.03 -157.57
REMARK 500 SER A 198 -124.21 59.48
REMARK 500 ARG A 254 -166.83 -127.04
REMARK 500 ASP A 297 -75.74 -129.97
REMARK 500 PHE A 398 -57.29 -138.07
REMARK 500 ARG A 453 27.30 -15.97
REMARK 500 GLN A 455 -3.77 -59.90
REMARK 500 GLU A 506 -85.20 -80.73
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 GLU A 255 ASN A 256 149.46
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 MES A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9A5 A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 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 residue SO4 A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 621
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 800 601 through FUC A 602 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
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: AD4
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: AD5
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: AD6
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: AD7
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 6I0B A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 6I0B GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 6I0B GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 6I0B GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 6I0B GLN A 486 UNP P06276 ASN 514 ENGINEERED MUTATION
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN
SEQRES 38 A 529 GLU THR GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 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 MES A 612 12
HET 9A5 A 613 37
HET GOL A 614 6
HET GOL A 615 6
HET GOL A 616 6
HET SO4 A 617 5
HET SO4 A 618 5
HET SO4 A 619 5
HET SO4 A 620 5
HET CL A 621 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM 9A5 (2~{S})-2-AZANYL-~{N}-[6-[(6-CHLORANYL-1,2,3,4-
HETNAM 2 9A5 TETRAHYDROACRIDIN-9-YL)AMINO]HEXYL]-3-(1~{H}-INDOL-3-
HETNAM 3 9A5 YL)PROPANAMIDE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 FUC 3(C6 H12 O5)
FORMUL 8 MES C6 H13 N O4 S
FORMUL 9 9A5 C30 H36 CL N5 O
FORMUL 10 GOL 3(C3 H8 O3)
FORMUL 13 SO4 4(O4 S 2-)
FORMUL 17 CL CL 1-
FORMUL 18 HOH *114(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 VAL A 148 LEU A 154 1 7
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 ASN A 266 1 11
HELIX 12 AB3 ASP A 268 ALA A 277 1 10
HELIX 13 AB4 MET A 302 LEU A 309 1 8
HELIX 14 AB5 GLY A 326 VAL A 331 1 6
HELIX 15 AB6 THR A 346 PHE A 358 1 13
HELIX 16 AB7 SER A 362 THR A 374 1 13
HELIX 17 AB8 GLU A 383 PHE A 398 1 16
HELIX 18 AB9 PHE A 398 GLU A 411 1 14
HELIX 19 AC1 PRO A 431 GLY A 435 5 5
HELIX 20 AC2 GLU A 441 GLY A 447 1 7
HELIX 21 AC3 LEU A 448 GLU A 451 5 4
HELIX 22 AC4 THR A 457 GLY A 478 1 22
HELIX 23 AC5 ARG A 515 SER A 524 1 10
HELIX 24 AC6 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 VAL A 13 N ILE A 6
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 VAL A 142
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 ARG A 219 N LEU A 194
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 503 N TYR A 420
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 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.07
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.04
LINK ND2 ASN A 57 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 603 1555 1555 1.46
LINK ND2 ASN A 241 C1 NAG A 607 1555 1555 1.45
LINK ND2 ASN A 256 C1 NAG A 610 1555 1555 1.45
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 1.43
LINK O6 NAG A 605 C1 FUC A 606 1555 1555 1.47
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.45
LINK O6 NAG A 607 C1 FUC A 609 1555 1555 1.47
CISPEP 1 ALA A 101 PRO A 102 0 -2.20
SITE 1 AC1 5 LYS A 323 TYR A 420 ARG A 509 ARG A 515
SITE 2 AC1 5 GLN A 518
SITE 1 AC2 16 TRP A 82 GLY A 116 GLY A 117 THR A 120
SITE 2 AC2 16 GLU A 197 PRO A 285 SER A 287 ASN A 289
SITE 3 AC2 16 ALA A 328 PHE A 329 TYR A 332 TRP A 430
SITE 4 AC2 16 MET A 437 HIS A 438 TYR A 440 HOH A 709
SITE 1 AC3 6 MET A 16 LEU A 18 TYR A 61 TRP A 98
SITE 2 AC3 6 ASP A 129 LYS A 131
SITE 1 AC4 4 GLU A 137 ARG A 138 THR A 300 LYS A 476
SITE 1 AC5 3 TRP A 376 ASP A 379 TYR A 385
SITE 1 AC6 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC7 2 ARG A 242 VAL A 288
SITE 1 AC8 3 SER A 487 THR A 488 THR A 508
SITE 1 AC9 3 ARG A 347 LYS A 348 GLN A 351
SITE 1 AD1 2 HOH A 784 HOH A 809
SITE 1 AD2 2 ARG A 14 ASN A 57
SITE 1 AD3 3 ASN A 106 ASN A 188 HOH A 795
SITE 1 AD4 3 ASN A 241 ASN A 245 PHE A 278
SITE 1 AD5 1 ASN A 256
SITE 1 AD6 4 GLY A 336 SER A 338 ASN A 341 ASN A 342
SITE 1 AD7 2 ARG A 465 ASN A 485
CRYST1 154.351 154.351 128.039 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 0.006479 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007810 0.00000
TER 4223 VAL A 529
MASTER 391 0 21 24 14 0 21 6 4535 1 241 41
END |