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HEADER HYDROLASE 12-NOV-17 6EYF
TITLE BUTYRYLCOLINESTERASE EXPRESSED IN CHO CELLS CO-CRYSTALLISED WITH A
TITLE 2 RIVASTIGMINE ANALOGUE
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, ALZHEIMER DISEASE, ORGANOPHOSPHATE,
KEYWDS 2 CARBAMYLATED, RIVASTIGMINE ANALOGUE, RATIONAL DESIGN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,E.DE LA MORA,S.DIGHE,B.ROSS
REVDAT 1 21-NOV-18 6EYF 0
SPRSDE 21-NOV-18 6EYF 6EUL
JRNL AUTH S.DIGHE,E.DE LA MORA,S.CHAN,S.KANTHAM,G.MCCOLL,S.K.VELIYATH,
JRNL AUTH 2 J.A.MILES,Z.Y.NESSAR,R.MCGEARY,I.SILMAN,I.WEIK,M.O.PARAT,
JRNL AUTH 3 X.BRAZZOLOTTO,B.ROSS
JRNL TITL ANALOGUES OF RIVASTIGMINE AND NAP FOR THE CNS DELIVERY OF
JRNL TITL 2 POLYPHENOLS WITH PUTATIVE ALZHEIMER DISEASE-MODIFYING
JRNL TITL 3 PROPERTIES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 23889
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 1158
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 38.5500 - 5.1963 0.99 2971 155 0.1886 0.2229
REMARK 3 2 5.1963 - 4.1260 1.00 2864 155 0.1503 0.1723
REMARK 3 3 4.1260 - 3.6049 1.00 2827 141 0.1559 0.2064
REMARK 3 4 3.6049 - 3.2755 1.00 2843 147 0.1754 0.2261
REMARK 3 5 3.2755 - 3.0408 1.00 2805 147 0.1992 0.2505
REMARK 3 6 3.0408 - 2.8616 1.00 2788 151 0.2125 0.3035
REMARK 3 7 2.8616 - 2.7183 1.00 2806 146 0.2314 0.2869
REMARK 3 8 2.7183 - 2.6000 1.00 2827 116 0.2603 0.4021
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.49
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 : 0.031 4461
REMARK 3 ANGLE : 1.655 6066
REMARK 3 CHIRALITY : 0.093 647
REMARK 3 PLANARITY : 0.014 779
REMARK 3 DIHEDRAL : 19.240 1625
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 6EYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007461.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
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 PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23889
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 38.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.02830
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.28070
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.470
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: 4AQD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.5, 2.15 M AMMONIUM
REMARK 280 SULFATE., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 77.09150
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.09150
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.87600
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.09150
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.09150
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.87600
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.09150
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.09150
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.87600
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.09150
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.09150
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.87600
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.09150
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.09150
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.87600
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.09150
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.09150
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.87600
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.09150
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.09150
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.87600
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.09150
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.09150
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.87600
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: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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 TYR A 237 CG CD1 CD2 CE1 CE2 CZ OH
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 ND2 ASN A 485 C1 NAG A 604 1.14
REMARK 500 ND2 ASN A 485 O5 NAG A 604 1.52
REMARK 500 ND2 ASN A 485 C2 NAG A 604 1.78
REMARK 500 CG ASN A 485 C1 NAG A 604 1.98
REMARK 500 ND2 ASN A 341 O7 NAG A 603 2.16
REMARK 500 NH2 ARG A 381 OD1 ASN A 384 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PHE A 195 N - CA - C ANGL. DEV. = 26.2 DEGREES
REMARK 500 PHE A 195 N - CA - C ANGL. DEV. = 34.0 DEGREES
REMARK 500 PHE A 195 CA - C - O ANGL. DEV. = -33.9 DEGREES
REMARK 500 PHE A 195 CA - C - O ANGL. DEV. = -38.9 DEGREES
REMARK 500 PHE A 195 CA - C - N ANGL. DEV. = 27.2 DEGREES
REMARK 500 PHE A 195 CA - C - N ANGL. DEV. = 34.7 DEGREES
REMARK 500 GLY A 196 N - CA - C ANGL. DEV. = -15.4 DEGREES
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 -4.26 75.14
REMARK 500 ASP A 54 -167.44 -74.39
REMARK 500 ALA A 58 66.38 -107.68
REMARK 500 PHE A 153 10.86 -143.69
REMARK 500 ALA A 162 76.70 -152.32
REMARK 500 BXT A 198 -121.30 56.97
REMARK 500 GLU A 255 -81.56 -96.20
REMARK 500 ASN A 256 100.35 -46.99
REMARK 500 ASP A 297 -74.98 -124.36
REMARK 500 PHE A 398 -59.81 -138.85
REMARK 500 ARG A 453 7.52 -64.48
REMARK 500 PRO A 480 47.73 -87.98
REMARK 500 GLN A 484 -60.00 -92.10
REMARK 500 ASN A 485 30.30 -68.87
REMARK 500 ASN A 486 71.18 52.02
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 PHE A 195 GLY A 196 -141.86
REMARK 500 PHE A 195 GLY A 196 -146.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PHE A 195 24.88
REMARK 500 PHE A 195 23.69
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 NAG A 603
REMARK 610 NAG A 604
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BY2 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 106
DBREF 6EYF A 3 529 UNP P06276 CHLE_HUMAN 31 557
SEQRES 1 A 527 ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL ARG GLY
SEQRES 2 A 527 MET ASN LEU THR VAL PHE GLY GLY THR VAL THR ALA PHE
SEQRES 3 A 527 LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY ARG LEU
SEQRES 4 A 527 ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP SER ASP
SEQRES 5 A 527 ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS CYS GLN
SEQRES 6 A 527 ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY SER GLU
SEQRES 7 A 527 MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP CYS LEU
SEQRES 8 A 527 TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO LYS ASN
SEQRES 9 A 527 ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE GLN
SEQRES 10 A 527 THR GLY THR SER SER LEU HIS VAL TYR ASP GLY LYS PHE
SEQRES 11 A 527 LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER MET ASN
SEQRES 12 A 527 TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU PRO GLY
SEQRES 13 A 527 ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE ASP GLN
SEQRES 14 A 527 GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE ALA ALA
SEQRES 15 A 527 PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE GLY GLU
SEQRES 16 A 527 BXT ALA GLY ALA ALA SER VAL SER LEU HIS LEU LEU SER
SEQRES 17 A 527 PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE LEU GLN
SEQRES 18 A 527 SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR SER LEU
SEQRES 19 A 527 TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA LYS LEU
SEQRES 20 A 527 THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE ILE LYS
SEQRES 21 A 527 CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU LEU ASN
SEQRES 22 A 527 GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU SER VAL
SEQRES 23 A 527 ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU THR ASP
SEQRES 24 A 527 MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE LYS LYS
SEQRES 25 A 527 THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU GLY THR
SEQRES 26 A 527 ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP
SEQRES 27 A 527 ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN GLU GLY
SEQRES 28 A 527 LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE GLY LYS
SEQRES 29 A 527 GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL ASP ASP
SEQRES 30 A 527 GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY ASP VAL
SEQRES 31 A 527 VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU GLU PHE
SEQRES 32 A 527 THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA PHE PHE
SEQRES 33 A 527 TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO TRP PRO
SEQRES 34 A 527 GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE GLU PHE
SEQRES 35 A 527 VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN TYR THR
SEQRES 36 A 527 LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL LYS ARG
SEQRES 37 A 527 TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN GLU THR
SEQRES 38 A 527 GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS SER THR
SEQRES 39 A 527 GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER THR ARG
SEQRES 40 A 527 ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG PHE TRP
SEQRES 41 A 527 THR SER PHE PHE PRO LYS VAL
MODRES 6EYF BXT A 198 SER MODIFIED RESIDUE
HET BXT A 198 12
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET BY2 A 605 19
HET GOL A 606 6
HET GOL A 607 6
HET GOL A 608 6
HET GOL A 609 6
HET SO4 A 610 5
HETNAM BXT (2~{S})-2-AZANYL-3-[ETHYL(METHYL)CARBAMOYL]OXY-
HETNAM 2 BXT PROPANOIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BY2 [3-[(1~{R})-1-(DIMETHYLAMINO)ETHYL]-4-OXIDANYL-PHENYL]
HETNAM 2 BY2 ~{N}-ETHYL-~{N}-METHYL-CARBAMATE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 BXT C7 H14 N2 O4
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 6 BY2 C14 H22 N2 O3
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 11 SO4 O4 S 2-
FORMUL 12 HOH *80(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 BXT A 198 SER A 210 1 13
HELIX 8 AA8 PRO A 211 PHE A 217 5 7
HELIX 9 AA9 SER A 235 THR A 250 1 16
HELIX 10 AB1 ASN A 256 ARG A 265 1 10
HELIX 11 AB2 ASP A 268 ALA A 277 1 10
HELIX 12 AB3 MET A 302 LEU A 309 1 8
HELIX 13 AB4 GLY A 326 VAL A 331 1 6
HELIX 14 AB5 THR A 346 PHE A 358 1 13
HELIX 15 AB6 SER A 362 THR A 374 1 13
HELIX 16 AB7 GLU A 383 PHE A 398 1 16
HELIX 17 AB8 PHE A 398 GLU A 411 1 14
HELIX 18 AB9 PRO A 431 GLY A 435 5 5
HELIX 19 AC1 GLU A 441 PHE A 446 1 6
HELIX 20 AC2 GLY A 447 ASN A 455 5 9
HELIX 21 AC3 THR A 457 GLY A 478 1 22
HELIX 22 AC4 ARG A 515 SER A 524 1 10
HELIX 23 AC5 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 LYS A 12
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 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 TRP A 112 O VAL A 142
SHEET 6 AA211 GLY A 187 GLY A 196 1 O THR A 193 N VAL A 109
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 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
SHEET 1 AA3 2 SER A 64 CYS A 65 0
SHEET 2 AA3 2 LEU A 88 SER A 89 1 O SER A 89 N SER A 64
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.05
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
LINK ND2 ASN A 57 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 602 1555 1555 1.45
LINK C GLU A 197 N BXT A 198 1555 1555 1.33
LINK C BXT A 198 N ALA A 199 1555 1555 1.34
CISPEP 1 ALA A 101 PRO A 102 0 6.95
SITE 1 AC1 2 ASN A 341 HOH A 717
SITE 1 AC2 3 ARG A 465 GLU A 482 ASN A 485
SITE 1 AC3 11 ASN A 68 ILE A 69 ASP A 70 TRP A 82
SITE 2 AC3 11 GLN A 119 THR A 120 PHE A 329 TYR A 332
SITE 3 AC3 11 GOL A 606 HOH A 750 HOH A 752
SITE 1 AC4 8 TRP A 82 GLU A 197 BXT A 198 GLY A 439
SITE 2 AC4 8 BY2 A 605 HOH A 720 HOH A 732 HOH A 750
SITE 1 AC5 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC5 5 LYS A 131
SITE 1 AC6 2 ASP A 340 PRO A 429
SITE 1 AC7 4 LYS A 323 TYR A 420 ARG A 509 ARG A 515
SITE 1 AC8 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC9 1 ASN A 57
SITE 1 AD1 2 ASN A 106 LYS A 190
CRYST1 154.183 154.183 127.752 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 0.006486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006486 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007828 0.00000
TER 4230 VAL A 529
MASTER 405 0 11 23 16 0 14 6 4381 1 126 41
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