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HEADER HYDROLASE 28-OCT-14 4ROT
TITLE CRYSTAL STRUCTURE OF ESTERASE A FROM STREPTOCOCCUS PYOGENES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE A;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1, 3.1.1.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;
SOURCE 3 ORGANISM_TAXID: 1314;
SOURCE 4 GENE: EST A, HMPREF1245_1265;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPROEXHTB SPYTBESTERASE
KEYWDS HYDROLASE ESTERASE ACYLTRANSFERASE, ACYLGLYCERASE, HYDROLYSIS,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.BENNETT,R.HOLLAND,F.COULIBALY,T.S.LOO,G.E.NORRIS,B.F.ANDERSON
REVDAT 1 24-DEC-14 4ROT 0
JRNL AUTH M.D.BENNETT,R.HOLLAND,F.COULIBALY,T.S.LOO,G.E.NORRIS,
JRNL AUTH 2 B.F.ANDERSON
JRNL TITL CRYSTAL STRUCTURE OF ESTERASE A FROM STREPTOCOCCUS PYOGENES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 32310
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1724
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2331
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2173
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 325
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.896
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2281 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2073 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3098 ; 2.107 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4773 ; 1.008 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 279 ; 6.790 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;41.779 ;24.661
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 376 ;14.807 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;15.746 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 311 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2653 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 573 ; 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): 1086 ; 1.727 ; 1.221
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1085 ; 1.726 ; 1.220
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1360 ; 2.625 ; 1.820
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1361 ; 2.624 ; 1.820
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1195 ; 2.455 ; 1.431
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1189 ; 2.460 ; 1.414
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1727 ; 3.809 ; 2.024
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2950 ; 6.317 ;11.331
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2803 ; 5.957 ;10.605
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4ROT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-14.
REMARK 100 THE RCSB ID CODE IS RCSB087610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-05; 24-SEP-05; 24-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y
REMARK 200 RADIATION SOURCE : ESRF; ESRF; ESRF
REMARK 200 BEAMLINE : ID29; ID29; ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93937; 0.93957; 0.89844
REMARK 200 MONOCHROMATOR : HIGH RESOLUTION SI(311) CUT;
REMARK 200 HIGH RESOLUTION SI(311) CUT; HIGH
REMARK 200 RESOLUTION SI(311) CUT
REMARK 200 OPTICS : TOROIDAL MIRROR; TOROIDAL
REMARK 200 MIRROR; TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM
REMARK 200 210; ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37068
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; SINGLE
REMARK 200 WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 20% PEG4000, 10% 2-
REMARK 280 PROPANOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 51.99000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 51.99000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.81550
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 51.99000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 51.99000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 66.81550
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 51.99000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 51.99000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 66.81550
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 51.99000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 51.99000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 66.81550
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 51.99000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 51.99000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 66.81550
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 51.99000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 51.99000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 66.81550
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 51.99000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 51.99000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 66.81550
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 51.99000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 51.99000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 66.81550
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 103.98000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -51.99000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 51.99000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 66.81550
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 51.99000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 51.99000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 66.81550
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 ZN ZN A 301 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 679 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 408 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 520 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 719 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 540 LIES ON A SPECIAL POSITION.
REMARK 375 C2 OXL A 302 LIES ON A SPECIAL POSITION.
REMARK 375 C1 OXL A 302 LIES ON A SPECIAL POSITION.
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 LEU A -5 CG CD1 CD2
REMARK 470 GLU A 158 CG CD OE1 OE2
REMARK 470 ASN A 160 CG OD1 ND2
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 516 O HOH A 720 1.36
REMARK 500 O HOH A 523 O HOH A 703 1.99
REMARK 500 O HOH A 561 O HOH A 701 1.99
REMARK 500 O HOH A 618 O HOH A 705 2.02
REMARK 500 O HOH A 721 O HOH A 722 2.06
REMARK 500 CA GLY A 159 O HOH A 634 2.11
REMARK 500 O HOH A 667 O HOH A 704 2.14
REMARK 500 O HOH A 461 O HOH A 652 2.15
REMARK 500 O HOH A 506 O HOH A 681 2.16
REMARK 500 O LEU A 157 O HOH A 645 2.18
REMARK 500 O HOH A 561 O HOH A 696 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 ARG A 58 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 LEU A 157 CA - CB - CG ANGL. DEV. = 19.8 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 LEU A -5 -34.74 83.19
REMARK 500 ASP A 38 49.87 -143.92
REMARK 500 ASN A 51 -169.20 -161.18
REMARK 500 ASP A 78 -138.18 54.44
REMARK 500 SER A 123 -124.04 54.35
REMARK 500 LEU A 157 94.46 -172.21
REMARK 500 GLU A 158 118.84 -6.92
REMARK 500 LYS A 233 -169.34 -127.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 163 24.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 692 DISTANCE = 5.35 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 228 NE2
REMARK 620 2 ASP A 226 OD2 103.6
REMARK 620 3 ASP A 226 OD1 85.2 54.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL A 302
DBREF 4ROT A 1 261 UNP V6W522 V6W522_STRPY 1 261
SEQADV 4ROT ASN A -6 UNP V6W522 EXPRESSION TAG
SEQADV 4ROT LEU A -5 UNP V6W522 EXPRESSION TAG
SEQADV 4ROT TYR A -4 UNP V6W522 EXPRESSION TAG
SEQADV 4ROT PHE A -3 UNP V6W522 EXPRESSION TAG
SEQADV 4ROT GLN A -2 UNP V6W522 EXPRESSION TAG
SEQADV 4ROT GLY A -1 UNP V6W522 EXPRESSION TAG
SEQADV 4ROT ALA A 0 UNP V6W522 EXPRESSION TAG
SEQADV 4ROT ASN A 156 UNP V6W522 LEU 156 ENGINEERED MUTATION
SEQRES 1 A 268 ASN LEU TYR PHE GLN GLY ALA MET ALA SER ILE ALA ILE
SEQRES 2 A 268 GLU TYR HIS SER VAL VAL LEU GLY MET GLU ARG LYS VAL
SEQRES 3 A 268 ASN VAL ILE TYR PRO ASP GLN SER GLU ILE PRO LYS LYS
SEQRES 4 A 268 ASP GLN GLY ASP LYS ASP ILE PRO VAL LEU TYR LEU LEU
SEQRES 5 A 268 HIS GLY MET GLY GLY ASN GLU ASN SER TRP GLN LYS ARG
SEQRES 6 A 268 THR ALA ILE GLU ARG LEU LEU ARG HIS THR ASN LEU ILE
SEQRES 7 A 268 VAL VAL MET PRO SER THR ASP LEU GLY TRP TYR THR ASP
SEQRES 8 A 268 THR ALA TYR GLY LEU ASN TYR TYR ARG ALA LEU SER GLN
SEQRES 9 A 268 GLU LEU PRO GLN VAL LEU ALA ALA PHE PHE PRO ASN MET
SEQRES 10 A 268 THR GLN LYS ARG GLU LYS THR PHE VAL ALA GLY LEU SER
SEQRES 11 A 268 MET GLY GLY TYR GLY ALA PHE LYS TRP ALA LEU LYS SER
SEQRES 12 A 268 ASN ARG PHE SER TYR ALA ALA SER PHE SER GLY ALA LEU
SEQRES 13 A 268 ASP PHE SER PRO GLU THR ASN LEU GLU GLY ASN LEU GLY
SEQRES 14 A 268 GLU LEU ALA TYR TRP GLN GLY VAL PHE GLY GLN PHE GLU
SEQRES 15 A 268 ASP PRO ASP LEU ASP LYS HIS TYR LEU LYS ASN MET VAL
SEQRES 16 A 268 ALA GLU SER ASP GLY LYS THR LYS PHE TYR ALA TRP CYS
SEQRES 17 A 268 GLY TYR GLU ASP PHE LEU PHE ALA THR ASN GLU LYS ALA
SEQRES 18 A 268 ILE ALA ASP PHE GLN ALA GLN GLY LEU ASP ILE ASP TYR
SEQRES 19 A 268 HIS LYS GLY HIS GLY LYS HIS GLU TRP TYR TYR TRP ASN
SEQRES 20 A 268 GLN GLN LEU GLU VAL LEU LEU GLU TRP LEU PRO ILE ASN
SEQRES 21 A 268 TYR GLN LYS GLU GLU ARG LEU SER
HET ZN A 301 1
HET OXL A 302 6
HETNAM ZN ZINC ION
HETNAM OXL OXALATE ION
FORMUL 2 ZN ZN 2+
FORMUL 3 OXL C2 O4 2-
FORMUL 4 HOH *325(H2 O)
HELIX 1 1 PRO A 30 GLN A 34 5 5
HELIX 2 2 ASN A 53 THR A 59 1 7
HELIX 3 3 ALA A 60 LEU A 65 1 6
HELIX 4 4 ASN A 90 GLN A 97 1 8
HELIX 5 5 GLN A 97 PHE A 107 1 11
HELIX 6 6 LYS A 113 GLU A 115 5 3
HELIX 7 7 SER A 123 ASN A 137 1 15
HELIX 8 8 SER A 152 LEU A 157 1 6
HELIX 9 9 GLU A 163 GLY A 172 1 10
HELIX 10 10 ASP A 178 VAL A 188 5 11
HELIX 11 11 LEU A 207 GLN A 221 1 15
HELIX 12 12 GLU A 235 LEU A 250 1 16
SHEET 1 A 8 ALA A 2 SER A 10 0
SHEET 2 A 8 MET A 15 TYR A 23 -1 O VAL A 21 N ILE A 4
SHEET 3 A 8 ILE A 71 MET A 74 -1 O MET A 74 N ASN A 20
SHEET 4 A 8 VAL A 41 LEU A 45 1 N LEU A 44 O VAL A 73
SHEET 5 A 8 THR A 117 LEU A 122 1 O PHE A 118 N TYR A 43
SHEET 6 A 8 TYR A 141 PHE A 145 1 O PHE A 145 N GLY A 121
SHEET 7 A 8 LYS A 196 GLY A 202 1 O TRP A 200 N SER A 144
SHEET 8 A 8 ILE A 225 GLY A 230 1 O HIS A 228 N ALA A 199
LINK NE2 HIS A 228 ZN ZN A 301 1555 1555 1.96
LINK OD2 ASP A 226 ZN ZN A 301 1555 1555 2.12
LINK OD1 ASP A 226 ZN ZN A 301 1555 1555 2.45
CISPEP 1 LEU A 157 GLU A 158 0 21.84
SITE 1 AC1 2 ASP A 226 HIS A 228
SITE 1 AC2 4 ARG A 259 SER A 261 HOH A 497 HOH A 643
CRYST1 103.980 103.980 133.631 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 0.009617 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007483 0.00000
TER 2208 SER A 261
MASTER 442 0 2 12 8 0 2 6 2505 1 10 21
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