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HEADER HYDROLASE 17-FEB-15 4Y9S
TITLE STRUCTURE OF AN H300N MUTANT OF POTATO EPOXIDE HYDROLASE, STEH1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM TUBEROSUM;
SOURCE 3 ORGANISM_COMMON: POTATO;
SOURCE 4 ORGANISM_TAXID: 4113;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGTACSTEH1-5H
KEYWDS MUTATION OF CATALYTIC RESIDUE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NAWORYTA,S.L.MOWBRAY,M.WIDERSTEN
REVDAT 1 16-SEP-15 4Y9S 0
JRNL AUTH B.A.AMREIN,P.BAUER,F.DUARTE,A.J.CARLSSON,A.NAWORYTA,
JRNL AUTH 2 S.L.MOWBRAY,M.WIDERSTEN,S.C.L.KAMERLIN
JRNL TITL EXPANDING THE CATALYTIC TRIAD IN EPOXIDE HYDROLASES AND
JRNL TITL 2 RELATED ENZYMES
JRNL REF ACS CATALYSIS V. 5 5702 2015
JRNL REFN ESSN 2155-5435
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 42817
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2276
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3099
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1770
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5111
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 482
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : 0.78000
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): 0.156
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.353
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5271 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5011 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7171 ; 1.817 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11547 ; 0.912 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 637 ; 6.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;35.881 ;23.917
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 844 ;14.811 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;20.954 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 763 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5917 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1235 ; 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): 2554 ; 1.776 ; 1.732
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2553 ; 1.772 ; 1.731
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3189 ; 2.612 ; 2.587
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3190 ; 2.612 ; 2.587
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2717 ; 2.817 ; 2.038
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2718 ; 2.817 ; 2.039
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3983 ; 4.400 ; 2.916
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6408 ; 6.295 ;15.161
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6243 ; 6.158 ;14.771
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 4Y9S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206944.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93300
REMARK 200 MONOCHROMATOR : DIAMOND (111)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45161
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 51.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC 5.8.0073
REMARK 200 STARTING MODEL: 2CJP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL DROPS OF PROTEIN SOLUTION (7.2
REMARK 280 MG/ML, I.E. 0.2 MM, IN 30 MM TRIS-HCL, PH 7.4, 5 MM VALPROMIDE)
REMARK 280 WERE MIXED WITH 1 UL DROPS OF RESERVOIR SOLUTION (CONTAINING 90
REMARK 280 MM NA-HEPES, PH 7.5, 25% PEG 10, 000). ONCE CRYSTALS WERE
REMARK 280 OBTAINED THEY WERE SOAKED IN MOTHER LIQUOR AT PH 3.5 PRIOR TO
REMARK 280 FREEZING., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 28.01050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.77550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.01800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.77550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.01050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.01800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 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 THR A -6
REMARK 465 SER A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR B -6
REMARK 465 SER B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LYS B 2
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 OE1 GLU B 224 O HOH B 514 2.03
REMARK 500 O HOH A 560 O HOH A 567 2.09
REMARK 500 O HOH B 509 O HOH B 529 2.10
REMARK 500 O HOH B 564 O HOH B 574 2.12
REMARK 500 NZ LYS B 121 O HOH B 529 2.12
REMARK 500 O HOH B 433 O HOH B 438 2.16
REMARK 500 NH2 ARG A 306 OE2 GLU A 309 2.18
REMARK 500 O HOH A 524 O HOH A 566 2.19
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 409 O HOH B 426 2674 2.15
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 GLU A 151 CD GLU A 151 OE1 0.074
REMARK 500 GLY A 227 CA GLY A 227 C 0.098
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 53 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 53 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 60 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 120 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH2 ANGL. DEV. = -3.3 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 ASP A 105 -122.30 62.77
REMARK 500 SER A 129 -49.97 78.74
REMARK 500 ALA A 299 -119.01 -113.56
REMARK 500 ASP B 105 -125.29 62.52
REMARK 500 SER B 129 -51.19 80.39
REMARK 500 ALA B 299 -125.17 -113.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CXU RELATED DB: PDB
REMARK 900 3CXU IS A Y149F MUTANT
REMARK 900 RELATED ID: 2CJP RELATED DB: PDB
REMARK 900 2CJP IS WILD-TYPE PROTEIN
DBREF 4Y9S A 3 321 UNP Q41415 Q41415_SOLTU 3 321
DBREF 4Y9S B 3 321 UNP Q41415 Q41415_SOLTU 3 321
SEQADV 4Y9S THR A -6 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S SER A -5 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS A -4 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS A -3 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS A -2 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS A -1 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS A 0 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S MET A 1 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S LYS A 2 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S ASN A 300 UNP Q41415 HIS 300 ENGINEERED MUTATION
SEQADV 4Y9S THR B -6 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S SER B -5 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS B -4 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS B -3 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS B -2 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS B -1 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S HIS B 0 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S MET B 1 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S LYS B 2 UNP Q41415 EXPRESSION TAG
SEQADV 4Y9S ASN B 300 UNP Q41415 HIS 300 ENGINEERED MUTATION
SEQRES 1 A 328 THR SER HIS HIS HIS HIS HIS MET LYS LYS ILE GLU HIS
SEQRES 2 A 328 LYS MET VAL ALA VAL ASN GLY LEU ASN MET HIS LEU ALA
SEQRES 3 A 328 GLU LEU GLY GLU GLY PRO THR ILE LEU PHE ILE HIS GLY
SEQRES 4 A 328 PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN MET VAL
SEQRES 5 A 328 TYR LEU ALA GLU ARG GLY TYR ARG ALA VAL ALA PRO ASP
SEQRES 6 A 328 LEU ARG GLY TYR GLY ASP THR THR GLY ALA PRO LEU ASN
SEQRES 7 A 328 ASP PRO SER LYS PHE SER ILE LEU HIS LEU VAL GLY ASP
SEQRES 8 A 328 VAL VAL ALA LEU LEU GLU ALA ILE ALA PRO ASN GLU GLU
SEQRES 9 A 328 LYS VAL PHE VAL VAL ALA HIS ASP TRP GLY ALA LEU ILE
SEQRES 10 A 328 ALA TRP HIS LEU CYS LEU PHE ARG PRO ASP LYS VAL LYS
SEQRES 11 A 328 ALA LEU VAL ASN LEU SER VAL HIS PHE SER LYS ARG ASN
SEQRES 12 A 328 PRO LYS MET ASN VAL VAL GLU GLY LEU LYS ALA ILE TYR
SEQRES 13 A 328 GLY GLU ASP HIS TYR ILE SER ARG PHE GLN VAL PRO GLY
SEQRES 14 A 328 GLU ILE GLU ALA GLU PHE ALA PRO ILE GLY ALA LYS SER
SEQRES 15 A 328 VAL LEU LYS LYS ILE LEU THR TYR ARG ASP PRO ALA PRO
SEQRES 16 A 328 PHE TYR PHE PRO LYS GLY LYS GLY LEU GLU ALA ILE PRO
SEQRES 17 A 328 ASP ALA PRO VAL ALA LEU SER SER TRP LEU SER GLU GLU
SEQRES 18 A 328 GLU LEU ASP TYR TYR ALA ASN LYS PHE GLU GLN THR GLY
SEQRES 19 A 328 PHE THR GLY ALA VAL ASN TYR TYR ARG ALA LEU PRO ILE
SEQRES 20 A 328 ASN TRP GLU LEU THR ALA PRO TRP THR GLY ALA GLN VAL
SEQRES 21 A 328 LYS VAL PRO THR LYS PHE ILE VAL GLY GLU PHE ASP LEU
SEQRES 22 A 328 VAL TYR HIS ILE PRO GLY ALA LYS GLU TYR ILE HIS ASN
SEQRES 23 A 328 GLY GLY PHE LYS LYS ASP VAL PRO LEU LEU GLU GLU VAL
SEQRES 24 A 328 VAL VAL LEU GLU GLY ALA ALA ASN PHE VAL SER GLN GLU
SEQRES 25 A 328 ARG PRO HIS GLU ILE SER LYS HIS ILE TYR ASP PHE ILE
SEQRES 26 A 328 GLN LYS PHE
SEQRES 1 B 328 THR SER HIS HIS HIS HIS HIS MET LYS LYS ILE GLU HIS
SEQRES 2 B 328 LYS MET VAL ALA VAL ASN GLY LEU ASN MET HIS LEU ALA
SEQRES 3 B 328 GLU LEU GLY GLU GLY PRO THR ILE LEU PHE ILE HIS GLY
SEQRES 4 B 328 PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN MET VAL
SEQRES 5 B 328 TYR LEU ALA GLU ARG GLY TYR ARG ALA VAL ALA PRO ASP
SEQRES 6 B 328 LEU ARG GLY TYR GLY ASP THR THR GLY ALA PRO LEU ASN
SEQRES 7 B 328 ASP PRO SER LYS PHE SER ILE LEU HIS LEU VAL GLY ASP
SEQRES 8 B 328 VAL VAL ALA LEU LEU GLU ALA ILE ALA PRO ASN GLU GLU
SEQRES 9 B 328 LYS VAL PHE VAL VAL ALA HIS ASP TRP GLY ALA LEU ILE
SEQRES 10 B 328 ALA TRP HIS LEU CYS LEU PHE ARG PRO ASP LYS VAL LYS
SEQRES 11 B 328 ALA LEU VAL ASN LEU SER VAL HIS PHE SER LYS ARG ASN
SEQRES 12 B 328 PRO LYS MET ASN VAL VAL GLU GLY LEU LYS ALA ILE TYR
SEQRES 13 B 328 GLY GLU ASP HIS TYR ILE SER ARG PHE GLN VAL PRO GLY
SEQRES 14 B 328 GLU ILE GLU ALA GLU PHE ALA PRO ILE GLY ALA LYS SER
SEQRES 15 B 328 VAL LEU LYS LYS ILE LEU THR TYR ARG ASP PRO ALA PRO
SEQRES 16 B 328 PHE TYR PHE PRO LYS GLY LYS GLY LEU GLU ALA ILE PRO
SEQRES 17 B 328 ASP ALA PRO VAL ALA LEU SER SER TRP LEU SER GLU GLU
SEQRES 18 B 328 GLU LEU ASP TYR TYR ALA ASN LYS PHE GLU GLN THR GLY
SEQRES 19 B 328 PHE THR GLY ALA VAL ASN TYR TYR ARG ALA LEU PRO ILE
SEQRES 20 B 328 ASN TRP GLU LEU THR ALA PRO TRP THR GLY ALA GLN VAL
SEQRES 21 B 328 LYS VAL PRO THR LYS PHE ILE VAL GLY GLU PHE ASP LEU
SEQRES 22 B 328 VAL TYR HIS ILE PRO GLY ALA LYS GLU TYR ILE HIS ASN
SEQRES 23 B 328 GLY GLY PHE LYS LYS ASP VAL PRO LEU LEU GLU GLU VAL
SEQRES 24 B 328 VAL VAL LEU GLU GLY ALA ALA ASN PHE VAL SER GLN GLU
SEQRES 25 B 328 ARG PRO HIS GLU ILE SER LYS HIS ILE TYR ASP PHE ILE
SEQRES 26 B 328 GLN LYS PHE
FORMUL 3 HOH *482(H2 O)
HELIX 1 AA1 LEU A 36 SER A 39 5 4
HELIX 2 AA2 TRP A 40 GLU A 49 1 10
HELIX 3 AA3 ASP A 72 PHE A 76 5 5
HELIX 4 AA4 SER A 77 ALA A 93 1 17
HELIX 5 AA5 ASP A 105 ARG A 118 1 14
HELIX 6 AA6 ASN A 140 GLY A 150 1 11
HELIX 7 AA7 HIS A 153 PHE A 158 1 6
HELIX 8 AA8 GLY A 162 ALA A 169 1 8
HELIX 9 AA9 GLY A 172 THR A 182 1 11
HELIX 10 AB1 PRO A 204 SER A 209 5 6
HELIX 11 AB2 SER A 212 GLY A 227 1 16
HELIX 12 AB3 PHE A 228 ALA A 237 1 10
HELIX 13 AB4 ALA A 237 THR A 245 1 9
HELIX 14 AB5 ALA A 246 THR A 249 5 4
HELIX 15 AB6 LEU A 266 ILE A 270 5 5
HELIX 16 AB7 GLY A 272 ASN A 279 1 8
HELIX 17 AB8 GLY A 280 VAL A 286 1 7
HELIX 18 AB9 PHE A 301 ARG A 306 1 6
HELIX 19 AC1 ARG A 306 LYS A 320 1 15
HELIX 20 AC2 LEU B 36 SER B 39 5 4
HELIX 21 AC3 TRP B 40 GLU B 49 1 10
HELIX 22 AC4 ASP B 72 PHE B 76 5 5
HELIX 23 AC5 SER B 77 ALA B 93 1 17
HELIX 24 AC6 ASP B 105 ARG B 118 1 14
HELIX 25 AC7 ASN B 140 GLY B 150 1 11
HELIX 26 AC8 HIS B 153 PHE B 158 1 6
HELIX 27 AC9 GLY B 162 ALA B 169 1 8
HELIX 28 AD1 GLY B 172 THR B 182 1 11
HELIX 29 AD2 PRO B 204 SER B 209 5 6
HELIX 30 AD3 SER B 212 GLY B 227 1 16
HELIX 31 AD4 PHE B 228 ALA B 237 1 10
HELIX 32 AD5 ALA B 237 THR B 245 1 9
HELIX 33 AD6 ALA B 246 THR B 249 5 4
HELIX 34 AD7 ASP B 265 ILE B 270 5 6
HELIX 35 AD8 GLY B 272 ASN B 279 1 8
HELIX 36 AD9 GLY B 280 VAL B 286 1 7
HELIX 37 AE1 PHE B 301 ARG B 306 1 6
HELIX 38 AE2 ARG B 306 LYS B 320 1 15
SHEET 1 AA1 8 GLU A 5 VAL A 11 0
SHEET 2 AA1 8 LEU A 14 LEU A 21 -1 O LEU A 18 N LYS A 7
SHEET 3 AA1 8 ARG A 53 PRO A 57 -1 O ALA A 54 N LEU A 21
SHEET 4 AA1 8 THR A 26 ILE A 30 1 N PHE A 29 O VAL A 55
SHEET 5 AA1 8 VAL A 99 HIS A 104 1 O VAL A 102 N ILE A 30
SHEET 6 AA1 8 VAL A 122 LEU A 128 1 O VAL A 126 N VAL A 101
SHEET 7 AA1 8 THR A 257 GLY A 262 1 O LYS A 258 N ASN A 127
SHEET 8 AA1 8 VAL A 293 LEU A 295 1 O LEU A 295 N VAL A 261
SHEET 1 AA2 8 GLU B 5 VAL B 11 0
SHEET 2 AA2 8 LEU B 14 LEU B 21 -1 O MET B 16 N VAL B 9
SHEET 3 AA2 8 ARG B 53 PRO B 57 -1 O ALA B 54 N LEU B 21
SHEET 4 AA2 8 THR B 26 ILE B 30 1 N ILE B 27 O VAL B 55
SHEET 5 AA2 8 VAL B 99 HIS B 104 1 O VAL B 102 N LEU B 28
SHEET 6 AA2 8 VAL B 122 LEU B 128 1 O VAL B 126 N VAL B 101
SHEET 7 AA2 8 THR B 257 GLY B 262 1 O LYS B 258 N LEU B 125
SHEET 8 AA2 8 VAL B 293 LEU B 295 1 O LEU B 295 N VAL B 261
CISPEP 1 PHE A 33 PRO A 34 0 -14.49
CISPEP 2 PHE B 33 PRO B 34 0 -11.79
CRYST1 56.021 96.036 121.551 90.00 90.00 90.00 P 21 21 21 8
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 0.017851 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010413 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008227 0.00000
TER 2561 PHE A 321
TER 5113 PHE B 321
MASTER 380 0 0 38 16 0 0 6 5593 2 0 52
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