4AO6-pdb | HEADER HYDROLASE 23-MAR-12 4AO6
TITLE NATIVE STRUCTURE OF A NOVEL COLD-ADAPTED ESTERASE FROM AN
TITLE 2 ARCTIC INTERTIDAL METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: A HIS-TAGGED CONSTRUCT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: M15 (PREP4);
SOURCE 8 OTHER_DETAILS: FROM A METAGENOMIC LIBRARY FROM INTERTIDAL ZONE AT
SOURCE 9 SVALBARD ARCHIPELAGO
KEYWDS HYDROLASE, THERMO LABEL
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FU,H.-K.S.LEIROS,D.D.PASCALE,K.A.JOHNSON,H.M.BLENCKE,B.LANDFALD
REVDAT 1 08-AUG-12 4AO6 0
JRNL AUTH J.FU,H.-K.S.LEIROS,D.DE PASCALE,K.A.JOHNSON,H.M.BLENCKE,
JRNL AUTH 2 B.LANDFALD
JRNL TITL FUNCTIONAL AND STRUCTURAL STUDIES OF A NOVEL COLD-ADAPTED
JRNL TITL 2 ESTERASE FROM AN ARCTIC INTERTIDAL METAGENOMIC LIBRARY.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2012
JRNL REFN ESSN 1432-0614
JRNL PMID 22832985
JRNL DOI 10.1007/S00253-012-4276-9
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.48
REMARK 3 NUMBER OF REFLECTIONS : 26718
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) : 0.18877
REMARK 3 R VALUE (WORKING SET) : 0.18715
REMARK 3 FREE R VALUE : 0.21947
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1420
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) : 1.600
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.642
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1869
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.285
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.271
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1743
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.423
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.25
REMARK 3 B22 (A**2) : -0.59
REMARK 3 B33 (A**2) : 0.34
REMARK 3 B12 (A**2) : 0.00
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): 0.094
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.172
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1764 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2396 ; 1.368 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 231 ; 5.178 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 68 ;36.453 ;23.676
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 294 ;12.921 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;10.113 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 263 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1329 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1121 ; 0.803 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1791 ; 1.415 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 643 ; 1.821 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 604 ; 2.872 ; 4.500
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 : 1
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 5 A 247
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5780 16.6247 14.9207
REMARK 3 T TENSOR
REMARK 3 T11: 0.0461 T22: 0.0354
REMARK 3 T33: 0.0513 T12: 0.0002
REMARK 3 T13: 0.0050 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 1.2308 L22: 2.3145
REMARK 3 L33: 0.9728 L12: 0.7021
REMARK 3 L13: 0.3946 L23: 0.2543
REMARK 3 S TENSOR
REMARK 3 S11: -0.0777 S12: -0.0252 S13: 0.1732
REMARK 3 S21: -0.2277 S22: -0.0031 S23: -0.0876
REMARK 3 S31: -0.1664 S32: 0.0281 S33: 0.0808
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4AO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-12.
REMARK 100 THE PDBE ID CODE IS EBI-51838.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS, SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28142
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.2
REMARK 200 R MERGE (I) : 0.02
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 0.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.7
REMARK 200 R MERGE FOR SHELL (I) : 0.49
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30% POLYETHYLENE GLYCOL
REMARK 280 (PEG) 3350, 3% GLYCEROL 0.1 M SODIUM MALONATE PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 27.93000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.93500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.93500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.7 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 -1.000000 0.000000 0.000000 55.86000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 MET A -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 HIS A 3
REMARK 465 GLN A 4
REMARK 465 GLY A 52
REMARK 465 GLY A 53
REMARK 465 THR A 54
REMARK 465 THR A 55
REMARK 465 HIS A 56
REMARK 465 LYS A 57
REMARK 465 LYS A 58
REMARK 465 VAL A 59
REMARK 465 HIS A 84
REMARK 465 GLY A 85
REMARK 465 GLU A 86
REMARK 465 ARG A 87
REMARK 465 ALA A 88
REMARK 465 SER A 89
REMARK 465 VAL A 90
REMARK 465 GLN A 91
REMARK 465 ALA A 92
REMARK 465 GLY A 93
REMARK 465 ARG A 94
REMARK 465 GLU A 95
REMARK 465 PRO A 96
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET A 5 CB CG SD CE
REMARK 480 GLU A 12 CG CD OE1 OE2
REMARK 480 ASP A 27 CG OD1 OD2
REMARK 480 GLU A 40 CB CG CD OE1 OE2
REMARK 480 ASP A 44 OD2
REMARK 480 TYR A 61 CE2
REMARK 480 GLU A 63 OE1
REMARK 480 PRO A 82 O
REMARK 480 GLU A 171 OE2
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 CD GLU A 12 OE2 GLU A 12 2665 1.98
REMARK 500 OE2 GLU A 12 OE2 GLU A 12 2665 1.12
REMARK 500 O HOH A 2077 O HOH A 2077 2655 1.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 5 CA MET A 5 CB 0.153
REMARK 500 GLU A 12 CB GLU A 12 CG 0.204
REMARK 500 ASP A 27 CB ASP A 27 CG -0.238
REMARK 500 TYR A 61 CE2 TYR A 61 CZ 0.147
REMARK 500 GLU A 63 CD A GLU A 63 OE1A -0.087
REMARK 500 GLU A 171 CD GLU A 171 OE2 -0.287
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 MET A 5 N - CA - CB ANGL. DEV. = -19.6 DEGREES
REMARK 500 GLU A 63 CG - CD - OE1 ANGL. DEV. = -12.7 DEGREES
REMARK 500 GLU A 63 OE1 - CD - OE2 ANGL. DEV. = 11.4 DEGREES
REMARK 500 GLU A 171 CG - CD - OE2 ANGL. DEV. = 37.1 DEGREES
REMARK 500 GLU A 171 OE1 - CD - OE2 ANGL. DEV. = -47.5 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 ASN A 8 111.09 72.22
REMARK 500 LYS A 10 128.53 83.24
REMARK 500 LEU A 15 -121.57 61.14
REMARK 500 ASP A 27 43.72 39.22
REMARK 500 GLU A 40 133.52 171.94
REMARK 500 SER A 144 -116.02 64.05
REMARK 500 LYS A 158 0.38 -68.98
REMARK 500 PHE A 235 -84.34 -100.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASP A 44 0.10 SIDE CHAIN
REMARK 500 GLU A 171 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AO7 RELATED DB: PDB
REMARK 900 ZINC BOUND STRUCTURE OF A NOVEL COLD-ADAPTED ESTERASE
REMARK 900 FROM AN ARCTIC INTERTIDAL METAGENOMIC LIBRARY
REMARK 900 RELATED ID: 4AO8 RELATED DB: PDB
REMARK 900 PEG-BOUND COMPLEX OF A NOVEL COLD-ADAPTED ESTERASE
REMARK 900 FROM AN ARCTIC INTERTIDAL METAGENOMIC LIBRARY
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES MRGSHHHHHHGS ARE THE N-TERMINAL HIS TAG
DBREF 4AO6 A 1 247 PDB 4AO6 4AO6 1 247
SEQADV 4AO6 MET A -11 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 ARG A -10 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 GLY A -9 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 SER A -8 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 HIS A -7 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 HIS A -6 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 HIS A -5 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 HIS A -4 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 HIS A -3 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 HIS A -2 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 GLY A -1 PDB 4AO6 EXPRESSION TAG
SEQADV 4AO6 SER A 0 PDB 4AO6 EXPRESSION TAG
SEQRES 1 A 259 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 A 259 ARG HIS GLN MET SER TRP ASN GLY LYS ASP GLU ARG LYS
SEQRES 3 A 259 LEU SER VAL GLN GLU ARG GLY PHE SER LEU GLU VAL ASP
SEQRES 4 A 259 GLY ARG THR VAL PRO GLY VAL TYR TRP SER PRO ALA GLU
SEQRES 5 A 259 GLY SER SER ASP ARG LEU VAL LEU LEU GLY HIS GLY GLY
SEQRES 6 A 259 THR THR HIS LYS LYS VAL GLU TYR ILE GLU GLN VAL ALA
SEQRES 7 A 259 LYS LEU LEU VAL GLY ARG GLY ILE SER ALA MET ALA ILE
SEQRES 8 A 259 ASP GLY PRO GLY HIS GLY GLU ARG ALA SER VAL GLN ALA
SEQRES 9 A 259 GLY ARG GLU PRO THR ASP VAL VAL GLY LEU ASP ALA PHE
SEQRES 10 A 259 PRO ARG MET TRP HIS GLU GLY GLY GLY THR ALA ALA VAL
SEQRES 11 A 259 ILE ALA ASP TRP ALA ALA ALA LEU ASP PHE ILE GLU ALA
SEQRES 12 A 259 GLU GLU GLY PRO ARG PRO THR GLY TRP TRP GLY LEU SER
SEQRES 13 A 259 MET GLY THR MET MET GLY LEU PRO VAL THR ALA SER ASP
SEQRES 14 A 259 LYS ARG ILE LYS VAL ALA LEU LEU GLY LEU MET GLY VAL
SEQRES 15 A 259 GLU GLY VAL ASN GLY GLU ASP LEU VAL ARG LEU ALA PRO
SEQRES 16 A 259 GLN VAL THR CYS PRO VAL ARG TYR LEU LEU GLN TRP ASP
SEQRES 17 A 259 ASP GLU LEU VAL SER LEU GLN SER GLY LEU GLU LEU PHE
SEQRES 18 A 259 GLY LYS LEU GLY THR LYS GLN LYS THR LEU HIS VAL ASN
SEQRES 19 A 259 PRO GLY LYS HIS SER ALA VAL PRO THR TRP GLU MET PHE
SEQRES 20 A 259 ALA GLY THR VAL ASP TYR LEU ASP GLN ARG LEU LYS
FORMUL 2 HOH *110(H2 O)
HELIX 1 1 GLU A 60 ARG A 72 1 13
HELIX 2 2 ASP A 98 LEU A 102 5 5
HELIX 3 3 ALA A 104 GLY A 112 1 9
HELIX 4 4 GLY A 113 GLY A 134 1 22
HELIX 5 5 SER A 144 ASP A 157 1 14
HELIX 6 6 ASN A 174 ALA A 182 1 9
HELIX 7 7 PRO A 183 VAL A 185 5 3
HELIX 8 8 SER A 201 LEU A 212 1 12
HELIX 9 9 PRO A 230 PHE A 235 1 6
HELIX 10 10 PHE A 235 LEU A 246 1 12
SHEET 1 AA 2 SER A 6 TRP A 7 0
SHEET 2 AA 2 VAL A 17 VAL A 26 -1 O SER A 23 N SER A 6
SHEET 1 AB 2 GLU A 12 LYS A 14 0
SHEET 2 AB 2 VAL A 17 VAL A 26 -1 O VAL A 17 N LYS A 14
SHEET 1 AC 9 LYS A 217 ASN A 222 0
SHEET 2 AC 9 VAL A 189 GLN A 194 1 O VAL A 189 N THR A 218
SHEET 3 AC 9 ILE A 160 GLY A 166 1 O ALA A 163 N ARG A 190
SHEET 4 AC 9 THR A 138 GLY A 142 1 O THR A 138 N LYS A 161
SHEET 5 AC 9 ARG A 45 GLY A 50 1 O LEU A 46 N GLY A 139
SHEET 6 AC 9 ILE A 74 ILE A 79 1 O SER A 75 N VAL A 47
SHEET 7 AC 9 ARG A 29 PRO A 38 -1 O VAL A 34 N ALA A 78
SHEET 8 AC 9 VAL A 17 VAL A 26 -1 O GLN A 18 N SER A 37
SHEET 9 AC 9 GLU A 12 LYS A 14 -1 O GLU A 12 N GLU A 19
SHEET 1 AD 9 LYS A 217 ASN A 222 0
SHEET 2 AD 9 VAL A 189 GLN A 194 1 O VAL A 189 N THR A 218
SHEET 3 AD 9 ILE A 160 GLY A 166 1 O ALA A 163 N ARG A 190
SHEET 4 AD 9 THR A 138 GLY A 142 1 O THR A 138 N LYS A 161
SHEET 5 AD 9 ARG A 45 GLY A 50 1 O LEU A 46 N GLY A 139
SHEET 6 AD 9 ILE A 74 ILE A 79 1 O SER A 75 N VAL A 47
SHEET 7 AD 9 ARG A 29 PRO A 38 -1 O VAL A 34 N ALA A 78
SHEET 8 AD 9 VAL A 17 VAL A 26 -1 O GLN A 18 N SER A 37
SHEET 9 AD 9 SER A 6 TRP A 7 -1 O SER A 6 N SER A 23
CISPEP 1 ASN A 8 GLY A 9 0 -5.68
CISPEP 2 GLU A 40 GLY A 41 0 -1.05
CRYST1 55.860 69.870 54.060 90.00 90.00 90.00 P 21 21 2 4
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 0.017902 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014312 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018498 0.00000
TER 1744 LYS A 247
MASTER 435 0 0 10 22 0 0 6 1853 1 0 20
END
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