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HEADER HYDROLASE 04-JUL-15 5A7H
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 SYNONYM: ACYL-COENZYME A, CHOLESTEROL ACYLTRANSFERASE, ACAT, BRAIN
COMPND 5 CARBOXYLESTERASE HBR1, CARBOXYLESTERASE 1, CE-1, HCE-1, COCAINE
COMPND 6 CARBOXYLESTERASE, EGASYN, HMSE, METHYLUMBELLIFERYL-ACETATE
COMPND 7 DEACETYLASE 1, MONOCYTE/MACROPHAGE SERINE ESTERASE, RETINYL ESTER
COMPND 8 HYDROLASE, REH, SERINE ESTERASE 1, TRIACYLGLYCEROL HYDROLASE, TGH,
COMPND 9 CARBOXYLESTERASE 1;
COMPND 10 EC: 3.1.1.1, 3.1.1.56;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES [N79Q]
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: VECTOR;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: POPINTTG
KEYWDS HYDROLASE, ESTERASE, AGLYCOSYLATED
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 5A7H 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. 2.01 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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.73
REMARK 3 NUMBER OF REFLECTIONS : 38317
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) : 0.18123
REMARK 3 R VALUE (WORKING SET) : 0.17897
REMARK 3 FREE R VALUE : 0.22163
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2034
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) : 2.010
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.062
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2536
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.205
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.249
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4130
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 221
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.370
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03
REMARK 3 B22 (A**2) : 0.03
REMARK 3 B33 (A**2) : -0.09
REMARK 3 B12 (A**2) : 0.03
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): 0.170
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.467
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4239 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4078 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5760 ; 1.469 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9425 ; 0.784 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 5.914 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;34.668 ;24.740
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 718 ;14.513 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.138 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 638 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4756 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 925 ; 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): 2125 ; 2.720 ; 4.175
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2124 ; 2.719 ; 4.173
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2655 ; 3.865 ; 6.254
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2114 ; 2.912 ; 4.407
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3140 ; 5.477 ; 6.488
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 : 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 3
REMARK 3 OTHER DETAILS: N79Q SITE MUTATION AGLYCOSYLATED. THE
REMARK 3 STEREOCHEMISTRY OF SER22 IS NOT WELL DEFINED DUE TO ILL-DEFINED
REMARK 3 ELECTRON DENSITY AT THE PROTEIN N-TERMINUS
REMARK 4
REMARK 4 5A7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-15.
REMARK 100 THE PDBE ID CODE IS EBI-64280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : PIXEL (PILATUS 6M-F)
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 : 41414
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.01
REMARK 200 RESOLUTION RANGE LOW (A) : 78.63
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3
REMARK 200 R MERGE FOR SHELL (I) : 0.61
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.30
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 BIS-TRIS PROPANE, PH 7.5, CONTAINING 20 % (W/V)
REMARK 280 POLYETHYLENE GLYCOL 3350, 0.2 M NAI
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 57.73500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.33332
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.42667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 57.73500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 33.33332
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.42667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 57.73500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 33.33332
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.42667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.66664
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 84.85333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 66.66664
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 84.85333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 66.66664
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 84.85333
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 A2221 LIES ON A SPECIAL POSITION.
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 O HOH A 2099 O HOH A 2195 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2127 O HOH A 2127 2765 1.97
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 ARG A 434 NE - CZ - NH2 ANGL. DEV. = -3.0 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 -162.99 70.35
REMARK 500 ALA A 80 63.97 -114.98
REMARK 500 ARG A 132 59.53 -151.45
REMARK 500 SER A 185 84.44 -152.10
REMARK 500 SER A 221 -126.39 66.28
REMARK 500 ASN A 238 15.99 57.52
REMARK 500 THR A 343 46.95 -85.74
REMARK 500 TRP A 357 -60.19 -153.81
REMARK 500 SER A 368 -59.02 -152.22
REMARK 500 PHE A 425 -52.93 -128.07
REMARK 500 ASN A 507 115.16 -163.08
REMARK 500 ASN A 520 -160.02 -109.66
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 IOD A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1557
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1560
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: 5A7G 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 N79Q
DBREF 5A7H A 22 552 UNP P23141 EST1_HUMAN 22 552
SEQADV 5A7H GLN A 79 UNP P23141 ASN 79 ENGINEERED MUTATION
SEQRES 1 A 531 SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL LEU
SEQRES 2 A 531 GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO VAL
SEQRES 3 A 531 ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO LEU
SEQRES 4 A 531 GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU PRO
SEQRES 5 A 531 TRP SER PHE VAL LYS GLN ALA THR SER TYR PRO PRO MET
SEQRES 6 A 531 CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER GLU
SEQRES 7 A 531 LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS LEU
SEQRES 8 A 531 SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO ALA
SEQRES 9 A 531 ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL TRP
SEQRES 10 A 531 ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER THR
SEQRES 11 A 531 TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL VAL
SEQRES 12 A 531 VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY PHE
SEQRES 13 A 531 PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP GLY
SEQRES 14 A 531 HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN ASP
SEQRES 15 A 531 ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL THR
SEQRES 16 A 531 ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER VAL
SEQRES 17 A 531 LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS ARG
SEQRES 18 A 531 ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL LEU
SEQRES 19 A 531 VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN ILE
SEQRES 20 A 531 ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA VAL
SEQRES 21 A 531 MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU LEU
SEQRES 22 A 531 LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU ASP
SEQRES 23 A 531 LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU GLY
SEQRES 24 A 531 THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO GLU
SEQRES 25 A 531 GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO TYR
SEQRES 26 A 531 MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU ILE
SEQRES 27 A 531 PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN LEU
SEQRES 28 A 531 ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER TYR
SEQRES 29 A 531 PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU ALA
SEQRES 30 A 531 THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL LYS
SEQRES 31 A 531 LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL MET
SEQRES 32 A 531 PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS ARG
SEQRES 33 A 531 ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN TYR
SEQRES 34 A 531 ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR VAL
SEQRES 35 A 531 ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE GLY
SEQRES 36 A 531 ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU ILE
SEQRES 37 A 531 ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN PHE
SEQRES 38 A 531 ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO HIS
SEQRES 39 A 531 TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN ILE
SEQRES 40 A 531 GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP LYS
SEQRES 41 A 531 GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
HET IOD A1553 1
HET IOD A1554 1
HET IOD A1555 1
HET IOD A1556 1
HET IOD A1557 1
HET IOD A1558 1
HET IOD A1559 1
HET IOD A1560 1
HETNAM IOD IODIDE ION
FORMUL 2 IOD 8(I 1-)
FORMUL 10 HOH *221(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 ARG A 287 1 10
HELIX 12 12 THR A 290 LYS A 302 1 13
HELIX 13 13 THR A 331 ARG A 339 1 9
HELIX 14 14 TRP A 357 MET A 363 1 7
HELIX 15 15 ASP A 373 SER A 384 1 12
HELIX 16 16 SER A 384 CYS A 389 1 6
HELIX 17 17 ALA A 391 GLU A 393 5 3
HELIX 18 18 LEU A 394 GLY A 404 1 11
HELIX 19 19 ASP A 408 PHE A 425 1 18
HELIX 20 20 PHE A 425 ALA A 439 1 15
HELIX 21 21 GLU A 470 PHE A 475 1 6
HELIX 22 22 GLY A 476 LYS A 481 1 6
HELIX 23 23 SER A 485 GLY A 506 1 22
HELIX 24 24 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 GLN 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 2.00
SSBOND 2 CYS A 274 CYS A 285 1555 1555 2.12
CISPEP 1 SER A 22 PRO A 23 0 17.56
SITE 1 AC1 6 SER A 98 ILE A 108 LEU A 110 SER A 150
SITE 2 AC1 6 THR A 151 HOH A2047
SITE 1 AC2 2 GLN A 95 LEU A 110
SITE 1 AC3 5 GLN A 45 PRO A 46 ALA A 48 ALA A 125
SITE 2 AC3 5 HOH A2061
SITE 1 AC4 2 SER A 75 IOD A1559
SITE 1 AC5 4 SER A 75 ASP A 182 GLU A 183 IOD A1558
SITE 1 AC6 1 MET A 326
CRYST1 115.470 115.470 127.280 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 0.008660 0.005000 0.000000 0.00000
SCALE2 0.000000 0.010000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007857 0.00000
TER 4131 LYS A 552
MASTER 377 0 8 24 18 0 8 6 4359 1 4 41
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