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HEADER HYDROLASE 28-MAR-19 6R6V
TITLE STRUCTURE OF RECOMBINANT HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH A
TITLE 2 FLUORESCENT COUMARIN-BASED PROBE
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
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, PROTEIN-LIGAND COMPLEX, FLUORESCENT PROBE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,F.NACHON,D.KNEZ,S.GOBEC
REVDAT 1 15-JAN-20 6R6V 0
JRNL AUTH S.PAJK,D.KNEZ,U.KOSAK,M.ZOROVIC,X.BRAZZOLOTTO,N.COQUELLE,
JRNL AUTH 2 F.NACHON,J.P.COLLETIER,M.ZIVIN,J.STOJAN,S.GOBEC
JRNL TITL DEVELOPMENT OF POTENT REVERSIBLE SELECTIVE INHIBITORS OF
JRNL TITL 2 BUTYRYLCHOLINESTERASE AS FLUORESCENT PROBES
JRNL REF J ENZYME INHIB MED CHEM 2020
JRNL REFN ESSN 1475-6374
JRNL DOI 10.1080/14756366.2019.1710502
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 26943
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1078
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 47.9026 - 4.9983 0.98 3370 141 0.1848 0.2422
REMARK 3 2 4.9983 - 3.9679 0.99 3265 136 0.1565 0.2269
REMARK 3 3 3.9679 - 3.4665 0.98 3184 133 0.1871 0.2404
REMARK 3 4 3.4665 - 3.1497 0.99 3215 134 0.2118 0.2734
REMARK 3 5 3.1497 - 2.9239 0.99 3211 133 0.2231 0.3082
REMARK 3 6 2.9239 - 2.7516 1.00 3205 134 0.2309 0.2876
REMARK 3 7 2.7516 - 2.6138 0.99 3203 134 0.2458 0.3536
REMARK 3 8 2.6138 - 2.5000 1.00 3212 133 0.2378 0.3337
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.18
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 6R6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101518.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9724
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27001
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 47.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07755
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.63760
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.550
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 (%): 61.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, 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 77.46500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.46500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 64.01500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.46500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.46500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 64.01500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.46500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.46500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 64.01500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.46500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.46500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 64.01500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.46500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.46500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 64.01500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.46500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.46500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 64.01500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.46500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.46500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 64.01500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.46500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.46500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.01500
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: 3590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 866 LIES ON A SPECIAL POSITION.
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 395 NH2 ARG A 515 1.63
REMARK 500 OD1 ASP A 454 O HOH A 701 2.08
REMARK 500 OG1 THR A 508 O HOH A 702 2.14
REMARK 500 NE2 GLN A 517 O HOH A 703 2.16
REMARK 500 N GLY A 117 O HOH A 704 2.17
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 -3.15 70.41
REMARK 500 ALA A 58 70.37 -102.97
REMARK 500 GLN A 67 144.34 -171.73
REMARK 500 LYS A 103 125.97 -31.50
REMARK 500 ASN A 106 54.89 -156.71
REMARK 500 ALA A 162 70.57 -153.34
REMARK 500 SER A 198 -122.97 64.69
REMARK 500 TYR A 237 -70.88 -56.97
REMARK 500 ASN A 256 102.31 -58.72
REMARK 500 ASP A 297 -79.45 -133.95
REMARK 500 PHE A 398 -57.09 -135.68
REMARK 500 LYS A 458 -56.09 -28.16
REMARK 500 GLU A 506 -70.08 -63.16
REMARK 500
REMARK 500 REMARK: NULL
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 JU5 A 612
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JU5 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 Poly-Saccharide residues NAG A
REMARK 800 601 through FUC A 602 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
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: AC8
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: AC9
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: AD1
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: AD2
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 6R6V A 4 529 UNP P06276 CHLE_HUMAN 32 557
SEQADV 6R6V GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 6R6V GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 6R6V GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 6R6V GLN A 486 UNP P06276 ASN 514 ENGINEERED MUTATION
SEQRES 1 A 526 ILE ILE ILE ALA THR LYS ASN GLY LYS VAL ARG GLY MET
SEQRES 2 A 526 GLN LEU THR VAL PHE GLY GLY THR VAL THR ALA PHE LEU
SEQRES 3 A 526 GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY ARG LEU ARG
SEQRES 4 A 526 PHE LYS LYS PRO GLN SER LEU THR LYS TRP SER ASP ILE
SEQRES 5 A 526 TRP ASN ALA THR LYS TYR ALA ASN SER CYS CYS GLN ASN
SEQRES 6 A 526 ILE ASP GLN SER PHE PRO GLY PHE HIS GLY SER GLU MET
SEQRES 7 A 526 TRP ASN PRO ASN THR ASP LEU SER GLU ASP CYS LEU TYR
SEQRES 8 A 526 LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO LYS ASN ALA
SEQRES 9 A 526 THR VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE GLN THR
SEQRES 10 A 526 GLY THR SER SER LEU HIS VAL TYR ASP GLY LYS PHE LEU
SEQRES 11 A 526 ALA ARG VAL GLU ARG VAL ILE VAL VAL SER MET ASN TYR
SEQRES 12 A 526 ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU PRO GLY ASN
SEQRES 13 A 526 PRO GLU ALA PRO GLY ASN MET GLY LEU PHE ASP GLN GLN
SEQRES 14 A 526 LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE ALA ALA PHE
SEQRES 15 A 526 GLY GLY ASN PRO LYS SER VAL THR LEU PHE GLY GLU SER
SEQRES 16 A 526 ALA GLY ALA ALA SER VAL SER LEU HIS LEU LEU SER PRO
SEQRES 17 A 526 GLY SER HIS SER LEU PHE THR ARG ALA ILE LEU GLN SER
SEQRES 18 A 526 GLY SER PHE ASN ALA PRO TRP ALA VAL THR SER LEU TYR
SEQRES 19 A 526 GLU ALA ARG ASN ARG THR LEU ASN LEU ALA LYS LEU THR
SEQRES 20 A 526 GLY CYS SER ARG GLU ASN GLU THR GLU ILE ILE LYS CYS
SEQRES 21 A 526 LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU LEU ASN GLU
SEQRES 22 A 526 ALA PHE VAL VAL PRO TYR GLY THR PRO LEU SER VAL ASN
SEQRES 23 A 526 PHE GLY PRO THR VAL ASP GLY ASP PHE LEU THR ASP MET
SEQRES 24 A 526 PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE LYS LYS THR
SEQRES 25 A 526 GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU GLY THR ALA
SEQRES 26 A 526 PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN
SEQRES 27 A 526 ASN SER ILE ILE THR ARG LYS GLU PHE GLN GLU GLY LEU
SEQRES 28 A 526 LYS ILE PHE PHE PRO GLY VAL SER GLU PHE GLY LYS GLU
SEQRES 29 A 526 SER ILE LEU PHE HIS TYR THR ASP TRP VAL ASP ASP GLN
SEQRES 30 A 526 ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY ASP VAL VAL
SEQRES 31 A 526 GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU GLU PHE THR
SEQRES 32 A 526 LYS LYS PHE SER GLU TRP GLY ASN ASN ALA PHE PHE TYR
SEQRES 33 A 526 TYR PHE GLU HIS ARG SER SER LYS LEU PRO TRP PRO GLU
SEQRES 34 A 526 TRP MET GLY VAL MET HIS GLY TYR GLU ILE GLU PHE VAL
SEQRES 35 A 526 PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN TYR THR LYS
SEQRES 36 A 526 ALA GLU GLU ILE LEU SER ARG SER ILE VAL LYS ARG TRP
SEQRES 37 A 526 ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN GLU THR GLN
SEQRES 38 A 526 ASN GLN SER THR SER TRP PRO VAL PHE LYS SER THR GLU
SEQRES 39 A 526 GLN LYS TYR LEU THR LEU ASN THR GLU SER THR ARG ILE
SEQRES 40 A 526 MET THR LYS LEU ARG ALA GLN GLN CYS ARG PHE TRP THR
SEQRES 41 A 526 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 JU5 A 612 32
HET SO4 A 613 5
HET SO4 A 614 5
HET SO4 A 615 5
HET SO4 A 616 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM JU5 ~{N}-[[(3~{S})-1-[[2-[7-(DIETHYLAMINO)-2-OXIDANYLIDENE-
HETNAM 2 JU5 CHROMEN-3-YL]-1,3-THIAZOL-4-YL]METHYL]PIPERIDIN-3-
HETNAM 3 JU5 YL]METHYL]-~{N}-[2-(DIMETHYLAMINO)ETHYL]NAPHTHALENE-2-
HETNAM 4 JU5 CARBOXAMIDE
HETNAM SO4 SULFATE ION
FORMUL 2 NAG 8(C8 H15 N O6)
FORMUL 2 FUC 3(C6 H12 O5)
FORMUL 8 JU5 C38 H45 N5 O3 S
FORMUL 9 SO4 4(O4 S 2-)
FORMUL 13 HOH *172(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 LYS A 267 1 12
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 GLY A 333 5 8
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 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 VAL A 25 N LEU A 18
SHEET 3 AA211 TYR A 94 PRO A 100 -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 TRP A 112 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 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 421 N VAL A 321
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 2.06
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.03
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.01
LINK ND2 ASN A 57 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 106 C1 NAG A 603 1555 1555 1.46
LINK ND2 ASN A 241 C1 NAG A 607 1555 1555 1.49
LINK ND2 ASN A 256 C1 NAG A 610 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG A 605 1555 1555 1.43
LINK ND2 ASN A 485 C1 NAG A 611 1555 1555 1.44
LINK O6 NAG A 601 C1 FUC A 602 1555 1555 1.45
LINK C1 NAG A 604 O4 NAG A 605 1555 1555 1.44
LINK O6 NAG A 605 C1 FUC A 606 1555 1555 1.46
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.46
LINK O6 NAG A 607 C1 FUC A 609 1555 1555 1.44
CISPEP 1 ALA A 101 PRO A 102 0 0.88
SITE 1 AC1 13 TRP A 82 GLY A 116 GLY A 117 THR A 120
SITE 2 AC1 13 GLU A 197 SER A 198 TRP A 231 LEU A 286
SITE 3 AC1 13 PHE A 329 TYR A 332 PHE A 398 HIS A 438
SITE 4 AC1 13 HOH A 816
SITE 1 AC2 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC3 6 TRP A 231 ARG A 242 SER A 287 VAL A 288
SITE 2 AC3 6 HOH A 708 HOH A 712
SITE 1 AC4 4 SER A 487 THR A 488 THR A 508 HOH A 717
SITE 1 AC5 3 ARG A 347 LYS A 348 GLN A 351
SITE 1 AC6 2 ARG A 14 ASN A 57
SITE 1 AC7 2 ASN A 106 ASN A 188
SITE 1 AC8 6 ASN A 241 ASN A 245 LEU A 249 PHE A 278
SITE 2 AC8 6 PRO A 281 HOH A 722
SITE 1 AC9 1 ASN A 256
SITE 1 AD1 5 GLY A 336 SER A 338 ASN A 341 ASN A 342
SITE 2 AD1 5 HOH A 724
SITE 1 AD2 3 ARG A 465 LYS A 469 ASN A 485
CRYST1 154.930 154.930 128.030 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 0.006455 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007811 0.00000
TER 4223 VAL A 529
MASTER 364 0 16 24 14 0 17 6 4557 1 206 41
END |