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HEADER HYDROLASE 04-JUL-15 5A7G
TITLE COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED
TITLE 2 AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 21-552;
COMPND 5 SYNONYM: ACYL-COENZYME A- CHOLESTEROL ACYLTRANSFERASE, ACAT, BRAIN
COMPND 6 CARBOXYLESTERASE HBR1, CARBOXYLESTERASE 1, CE-1, HCE-1, COCAINE
COMPND 7 CARBOXYLESTERASE, EGASYN, HMSE, METHYLUMBELLIFERYL-ACETATE
COMPND 8 DEACETYLASE 1, MONOCYTE/MACROPHAGE SERINE ESTERASE, RETINYL ESTER
COMPND 9 HYDROLASE, REH, SERINE ESTERASE 1, TRIACYLGLYCEROL HYDROLASE, TGH,
COMPND 10 CARBOXYLESTERASE 1;
COMPND 11 EC: 3.1.1.1, 3.1.1.56;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: HEK 323;
SOURCE 6 ATCC: CRL-1573;
SOURCE 7 ORGAN: LIVER;
SOURCE 8 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: HEK 323;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: POPINTTG
KEYWDS HYDROLASE, ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.ARENA DE SOUZA,D.J.SCOTT,M.CHARLTON,M.A.WALSH,R.J.OWEN
REVDAT 1 13-JAN-16 5A7G 0
JRNL AUTH V.ARENA DE SOUZA,D.J.SCOTT,J.E.NETTLESHIP,N.RAHMAN,
JRNL AUTH 2 M.H.CHARLTON,M.A.WALSH,R.J.OWENS
JRNL TITL COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED
JRNL TITL 2 AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1.
JRNL REF PLOS ONE V. 10 43919 2015
JRNL REFN ISSN 1932-6203
JRNL PMID 26657071
JRNL DOI 10.1371/JOURNAL.PONE.0143919
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.68
REMARK 3 NUMBER OF REFLECTIONS : 93337
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.13137
REMARK 3 R VALUE (WORKING SET) : 0.12916
REMARK 3 FREE R VALUE : 0.17277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 4985
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.480
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.518
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5418
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.234
REMARK 3 BIN FREE R VALUE SET COUNT : 286
REMARK 3 BIN FREE R VALUE : 0.292
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4107
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 695
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.014
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16
REMARK 3 B22 (A**2) : 0.16
REMARK 3 B33 (A**2) : -0.53
REMARK 3 B12 (A**2) : 0.16
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.062
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.316
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.974
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4242 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4083 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5764 ; 1.510 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9430 ; 0.924 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 531 ; 8.568 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;32.301 ;24.740
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 717 ;11.853 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;15.897 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 641 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4749 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 924 ; 0.002 ; 0.020
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2118 ; 3.367 ; 2.669
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2117 ; 3.365 ; 2.667
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2645 ; 4.113 ; 4.023
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2) : 2646 ; 4.113 ; 4.024
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2124 ; 4.298 ; 3.051
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2) : 2124 ; 4.299 ; 3.051
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2) : 3118 ; 4.958 ; 4.414
REMARK 3 LONG RANGE B REFINED ATOMS (A**2) : 5461 ; 6.440 ;24.443
REMARK 3 LONG RANGE B OTHER ATOMS (A**2) : 5058 ; 5.633 ;22.752
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 8325 ; 3.589 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 186 ;65.490 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 8725 ;24.361 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5A7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-AUG-15.
REMARK 100 THE PDBE ID CODE IS EBI-64284.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-13
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.48
REMARK 200 RESOLUTION RANGE LOW (A) : 53.94
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.9
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2
REMARK 200 R MERGE FOR SHELL (I) : 0.69
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.00
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: PDB ENTRY 5A7F
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT 4C IN
REMARK 280 0.1 M BICINE/TRIZMA BASE, PH 8.5, CONTAINING 0.03 M EACH
REMARK 280 OF DIETHYLENE GLYCOL, TRIETHYLENE GLYCOL, TETRAETHYLENE
REMARK 280 GLYCOL, PENTAETHYLENE GLYCOL, 10 % (W/V) PEG 4000, 20 %
REMARK 280 (V/V) GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.69500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.31022
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.71333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 57.69500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 33.31022
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.71333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 57.69500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 33.31022
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.71333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.62045
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 85.42667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 66.62045
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 85.42667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 66.62045
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 85.42667
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 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 A2695 LIES ON A SPECIAL POSITION.
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 SER A 315
REMARK 465 GLN A 316
REMARK 465 PRO A 317
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 SG CYS A 389 O HOH A 2519 2.09
REMARK 500 O HOH A 2003 O HOH A 2017 2.06
REMARK 500 O HOH A 2114 O HOH A 2115 2.10
REMARK 500 O HOH A 2126 O HOH A 2128 2.00
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 76 -148.13 64.41
REMARK 500 ALA A 80 60.56 -115.26
REMARK 500 SER A 185 82.45 -157.50
REMARK 500 ALA A 221 -118.26 64.81
REMARK 500 THR A 252 90.66 -69.65
REMARK 500 TRP A 357 -59.60 -153.26
REMARK 500 PHE A 425 -59.25 -122.91
REMARK 500 ASN A 520 -153.62 -109.36
REMARK 500 LYS A 539 26.74 49.92
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 ARG A 339 ASN A 340 137.62
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 MONO-SACCHARIDE
REMARK 800 NAG A1553 BOUND TO ASN A 79
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A7F RELATED DB: PDB
REMARK 900 COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED
REMARK 900 AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1
REMARK 900 RELATED ID: 5A7H RELATED DB: PDB
REMARK 900 COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED
REMARK 900 AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SITE MUTATION S221A DISORDERED RESIDUES 315-317
DBREF 5A7G A 21 552 UNP P23141 EST1_HUMAN 21 553
SEQADV 5A7G ALA A 221 UNP P23141 SER 221 ENGINEERED MUTATION
SEQRES 1 A 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 A 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 A 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 A 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 A 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 A 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 A 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 A 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 A 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 A 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 A 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 A 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 A 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 A 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 A 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 A 532 THR ILE PHE GLY GLU ALA ALA GLY GLY GLU SER VAL SER
SEQRES 17 A 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 A 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 A 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 A 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 A 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 A 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 A 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 A 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 A 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 A 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 A 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 A 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 A 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 A 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 A 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 A 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 A 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 A 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 A 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 A 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 A 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 A 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 A 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 A 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 A 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
MODRES 5A7G ASN A 79 ASN GLYCOSYLATION SITE
HET NAG A1553 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 HOH *695(H2 O)
HELIX 1 1 LEU A 60 ARG A 64 5 5
HELIX 2 2 ASP A 90 THR A 102 1 13
HELIX 3 3 ALA A 148 TYR A 152 5 5
HELIX 4 4 GLY A 154 ASN A 162 1 9
HELIX 5 5 LEU A 172 PHE A 178 1 7
HELIX 6 6 ASN A 188 ILE A 205 1 18
HELIX 7 7 ALA A 206 PHE A 208 5 3
HELIX 8 8 ALA A 221 LEU A 232 1 12
HELIX 9 9 SER A 233 LYS A 237 5 5
HELIX 10 10 THR A 252 VAL A 254 5 3
HELIX 11 11 VAL A 261 GLY A 273 1 13
HELIX 12 12 THR A 278 LYS A 289 1 12
HELIX 13 13 THR A 290 LYS A 302 1 13
HELIX 14 14 THR A 331 ARG A 339 1 9
HELIX 15 15 TRP A 357 MET A 363 1 7
HELIX 16 16 ASP A 373 SER A 384 1 12
HELIX 17 17 SER A 384 CYS A 389 1 6
HELIX 18 18 ALA A 391 GLU A 393 5 3
HELIX 19 19 LEU A 394 GLY A 404 1 11
HELIX 20 20 ASP A 408 PHE A 425 1 18
HELIX 21 21 PHE A 425 ALA A 439 1 15
HELIX 22 22 GLU A 470 PHE A 475 1 6
HELIX 23 23 GLY A 476 LEU A 480 5 5
HELIX 24 24 SER A 485 GLY A 506 1 22
HELIX 25 25 LYS A 539 ALA A 551 1 13
SHEET 1 AA 3 VAL A 25 THR A 28 0
SHEET 2 AA 3 GLY A 31 LEU A 34 -1 O GLY A 31 N THR A 28
SHEET 3 AA 3 VAL A 77 ASN A 79 1 O LYS A 78 N LEU A 34
SHEET 1 AB11 LYS A 36 VAL A 38 0
SHEET 2 AB11 VAL A 47 PRO A 54 -1 O VAL A 47 N VAL A 38
SHEET 3 AB11 TYR A 118 THR A 123 -1 O LEU A 119 N ILE A 53
SHEET 4 AB11 VAL A 164 ILE A 168 -1 O VAL A 165 N TYR A 122
SHEET 5 AB11 LEU A 133 ILE A 139 1 O PRO A 134 N VAL A 164
SHEET 6 AB11 GLY A 210 GLU A 220 1 N ASN A 211 O LEU A 133
SHEET 7 AB11 ARG A 242 GLU A 246 1 O ARG A 242 N ILE A 217
SHEET 8 AB11 TYR A 346 ASN A 351 1 O MET A 347 N SER A 245
SHEET 9 AB11 THR A 443 GLN A 449 1 O TYR A 444 N VAL A 348
SHEET 10 AB11 GLY A 524 GLY A 529 1 O LEU A 526 N GLU A 447
SHEET 11 AB11 GLN A 533 GLN A 536 -1 O GLN A 533 N GLN A 527
SHEET 1 AC 2 MET A 86 CYS A 87 0
SHEET 2 AC 2 LEU A 112 SER A 113 1 N SER A 113 O MET A 86
SHEET 1 AD 2 VAL A 256 LYS A 257 0
SHEET 2 AD 2 THR A 321 VAL A 322 1 O THR A 321 N LYS A 257
SSBOND 1 CYS A 87 CYS A 116 1555 1555 2.02
SSBOND 2 CYS A 274 CYS A 285 1555 1555 2.07
LINK ND2 ASN A 79 C1 NAG A1553 1555 1555 1.46
SITE 1 AC1 3 ASN A 79 THR A 81 HOH A2694
CRYST1 115.390 115.390 128.140 90.00 90.00 120.00 H 3 9
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 0.008666 0.005003 0.000000 0.00000
SCALE2 0.000000 0.010007 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007804 0.00000
TER 4120 LYS A 552
MASTER 331 0 1 25 18 0 1 6 4828 1 19 41
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