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HEADER HYDROLASE 03-JUL-15 5A7F
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 21-553;
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, 3.1.1.1, 3.1.1.56;
COMPND 12 ENGINEERED: 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 5A7F 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. 1.86 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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.94
REMARK 3 NUMBER OF REFLECTIONS : 44506
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) : 0.15979
REMARK 3 R VALUE (WORKING SET) : 0.15832
REMARK 3 FREE R VALUE : 0.18762
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2367
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) : 1.863
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.911
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2584
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.257
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.288
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4135
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.377
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12
REMARK 3 B22 (A**2) : -0.12
REMARK 3 B33 (A**2) : 0.39
REMARK 3 B12 (A**2) : -0.12
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): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.486
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4267 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4092 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5801 ; 1.630 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9453 ; 0.814 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 533 ; 5.797 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;33.464 ;24.740
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 717 ;13.297 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;20.170 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 644 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4771 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 926 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2129 ; 1.227 ; 1.634
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2128 ; 1.226 ; 1.633
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2660 ; 1.984 ; 2.444
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2138 ; 1.988 ; 1.894
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3140 ; 2.953 ; 2.735
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 21 A 302
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3340 -14.6230 32.3310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1431 T22: 0.1583
REMARK 3 T33: 0.0084 T12: 0.0306
REMARK 3 T13: 0.0133 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.7951 L22: 0.7387
REMARK 3 L33: 0.2672 L12: -0.3937
REMARK 3 L13: -0.0907 L23: 0.1362
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: -0.0474 S13: 0.0410
REMARK 3 S21: -0.0112 S22: 0.0155 S23: -0.0536
REMARK 3 S31: -0.0091 S32: -0.0276 S33: -0.0367
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 303 A 552
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3800 -12.4690 28.4360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1482 T22: 0.1764
REMARK 3 T33: 0.0180 T12: 0.0250
REMARK 3 T13: 0.0223 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 1.4352 L22: 1.0009
REMARK 3 L33: 0.4545 L12: 0.1620
REMARK 3 L13: 0.0048 L23: -0.0381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0586 S12: 0.0822 S13: -0.0468
REMARK 3 S21: -0.1223 S22: 0.0547 S23: 0.0874
REMARK 3 S31: 0.0211 S32: -0.1182 S33: 0.0039
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 5A7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUL-15.
REMARK 100 THE PDBE ID CODE IS EBI-64251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-11
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 : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46879
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.86
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 2.8
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.3
REMARK 200 R MERGE FOR SHELL (I) : 0.43
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.80
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 2H7C
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 20C IN
REMARK 280 0.1 M MES/IMIDAZOLE, PH 6.5 CONTAINING 0.03 M EACH OF
REMARK 280 DIETHYLENE GLYCOL, TRIETHYLENE GLYCOL, TETRAETHYLENE
REMARK 280 GLYCOL, PENTAETHYLENE GLYCOL, 10 % (W/V) POLYETHYLENE
REMARK 280 GLYCOL 4000, 20% (W/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 57.35750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.11537
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.26000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 57.35750
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 33.11537
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 39.26000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 57.35750
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 33.11537
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.26000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.23074
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 78.52000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 66.23074
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 78.52000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 66.23074
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 78.52000
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: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.5 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 57.35750
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -99.34610
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 114.71500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 ARG A 64 NE - CZ - NH2 ANGL. DEV. = -3.8 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 76 -153.16 62.60
REMARK 500 ALA A 80 62.79 -101.09
REMARK 500 SER A 185 82.72 -159.49
REMARK 500 SER A 221 -119.81 59.36
REMARK 500 MET A 326 -62.10 -120.51
REMARK 500 THR A 343 45.26 -90.51
REMARK 500 TRP A 357 -53.49 -154.35
REMARK 500 PHE A 425 -54.31 -123.61
REMARK 500 ASN A 520 -156.13 -108.49
REMARK 500 ALA A 551 40.56 -78.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): GLYCOSYLATION SITE N79
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
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: 5A7G 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
DBREF 5A7F A 21 552 UNP P23141-3 EST1_HUMAN 21 552
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 SER 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 5A7F ASN A 79 ASN GLYCOSYLATION SITE
HET NAG A1553 14
HET PO4 A1554 5
HET PO4 A1555 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PO4 PHOSPHATE ION
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *270(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 GLY A 154 ASN A 162 1 9
HELIX 4 4 LEU A 172 PHE A 178 1 7
HELIX 5 5 ASN A 188 ILE A 205 1 18
HELIX 6 6 ALA A 206 PHE A 208 5 3
HELIX 7 7 SER A 221 LEU A 232 1 12
HELIX 8 8 SER A 233 LYS A 237 5 5
HELIX 9 9 THR A 252 VAL A 254 5 3
HELIX 10 10 VAL A 261 GLY A 273 1 13
HELIX 11 11 THR A 278 LYS A 289 1 12
HELIX 12 12 THR A 290 LYS A 302 1 13
HELIX 13 13 ASP A 311 SER A 315 5 5
HELIX 14 14 THR A 331 GLU A 338 1 8
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 LYS A 481 1 6
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 1.95
SSBOND 2 CYS A 274 CYS A 285 1555 1555 2.11
LINK ND2 ASN A 79 C1 NAG A1553 1555 1555 1.45
SITE 1 AC1 7 ALA A 236 LYS A 237 ASN A 238 LEU A 239
SITE 2 AC1 7 PHE A 240 HIS A 342 VAL A 344
SITE 1 AC2 5 ARG A 64 HIS A 284 GLN A 288 LYS A 289
SITE 2 AC2 5 HOH A2037
SITE 1 AC3 3 ASN A 79 THR A 81 SER A 82
CRYST1 114.715 114.715 117.780 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 0.008717 0.005033 0.000000 0.00000
SCALE2 0.000000 0.010066 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008490 0.00000
TER 4136 LYS A 552
MASTER 369 0 3 25 18 0 5 6 4429 1 29 41
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