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HEADER HYDROLASE 20-MAR-15 4YWF
TITLE ABYA5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABYA5;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VERRUCOSISPORA MARIS;
SOURCE 3 ORGANISM_TAXID: 1003110;
SOURCE 4 GENE: ABYA5, VAB18032_16440;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS DEACETYLASE, ELIMINATION, HYDROLASE, SPIROTETRONATE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.BYRNE,P.R.RACE
REVDAT 1 29-JUN-16 4YWF 0
JRNL AUTH M.J.BYRNE,P.R.RACE
JRNL TITL STRUCTURE OF ABYA5 AT 2.0 ANGSTROMS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 36.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23787
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1275
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) : 1758
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2493
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.44000
REMARK 3 B22 (A**2) : 1.08000
REMARK 3 B33 (A**2) : -3.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.76000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.192
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.158
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.395
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2556 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2381 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3501 ; 1.817 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5433 ; 2.062 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 331 ; 6.355 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;32.266 ;22.075
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 333 ;15.648 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;24.472 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 400 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2933 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 592 ; 0.007 ; 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): 1330 ; 2.419 ; 3.044
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1329 ; 2.412 ; 3.043
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1659 ; 3.253 ; 4.555
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1660 ; 3.255 ; 4.556
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1226 ; 3.086 ; 3.312
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1227 ; 3.084 ; 3.312
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1843 ; 4.267 ; 4.863
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2880 ; 5.913 ;25.427
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2867 ; 5.912 ;25.361
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 4YWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208197.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97957
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25075
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 36.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M MAGNESIUM CHLORIDE, 0.1M HEPES,
REMARK 280 22% W/V POLYACRYLIC ACID 5100 SODIUM SALT, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 46.04000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.59000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.04000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.59000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 MSE A -19
REMARK 465 ALA A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 LEU A -8
REMARK 465 GLU A -7
REMARK 465 VAL A -6
REMARK 465 LEU A -5
REMARK 465 VAL A 12
REMARK 465 LEU A 13
REMARK 465 ALA A 14
REMARK 465 HIS A 15
REMARK 465 VAL A 16
REMARK 465 SER A 17
REMARK 465 ALA A 18
REMARK 465 GLN A 19
REMARK 465 ASN A 20
REMARK 465 ALA A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 ASP A 24
REMARK 465 GLY A 25
REMARK 465 VAL A 26
REMARK 465 LEU A 27
REMARK 465 ALA A 28
REMARK 465 ARG A 29
REMARK 465 ALA A 348
REMARK 465 GLN A 349
REMARK 465 VAL A 350
REMARK 465 GLU A 351
REMARK 465 GLY A 352
REMARK 465 GLY A 353
REMARK 465 ARG A 354
REMARK 465 ALA A 355
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 VAL A 4 CG1 CG2
REMARK 470 GLN A 9 CG CD OE1 NE2
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 46 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 49 CG CD OE1 OE2
REMARK 470 GLN A 53 CG CD OE1 NE2
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 93 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 104 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 170 CG CD1 CD2
REMARK 470 GLU A 232 CG CD OE1 OE2
REMARK 470 ARG A 239 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 268 CG CD OE1 NE2
REMARK 470 GLU A 286 CG CD OE1 OE2
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 322 CG CD NE CZ NH1 NH2
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 NH2 ARG A 304 OE1 GLU A 331 2.19
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 185 CD GLU A 185 OE1 0.070
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 68 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 68 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 89 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 213 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 213 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 215 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 297 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 297 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 304 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 304 NE - CZ - NH2 ANGL. DEV. = -5.0 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 ASP A 33 41.70 -109.69
REMARK 500 SER A 118 131.95 -170.14
REMARK 500 THR A 156 -156.78 -133.95
REMARK 500 SER A 198 -136.60 52.66
REMARK 500 VAL A 224 -64.16 -133.07
REMARK 500 ALA A 225 -60.09 -138.58
REMARK 500 THR A 251 -157.47 -129.33
REMARK 500 SER A 314 62.72 37.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 151 ALA A 152 149.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4YWF A 0 355 UNP F4F7F5 F4F7F5_VERMA 1 355
SEQADV 4YWF MSE A -19 UNP F4F7F5 INITIATING METHIONINE
SEQADV 4YWF ALA A -18 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF HIS A -17 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF HIS A -16 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF HIS A -15 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF HIS A -14 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF HIS A -13 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF HIS A -12 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF SER A -11 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF SER A -10 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF GLY A -9 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF LEU A -8 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF GLU A -7 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF VAL A -6 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF LEU A -5 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF PHE A -4 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF GLN A -3 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF GLY A -2 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF PRO A -1 UNP F4F7F5 EXPRESSION TAG
SEQADV 4YWF MSE A 66 UNP F4F7F5 LEU 66 ENGINEERED MUTATION
SEQADV 4YWF MSE A 158 UNP F4F7F5 LEU 158 ENGINEERED MUTATION
SEQADV 4YWF MSE A 195 UNP F4F7F5 LEU 195 ENGINEERED MUTATION
SEQADV 4YWF MSE A 295 UNP F4F7F5 LEU 295 ENGINEERED MUTATION
SEQRES 1 A 374 MSE ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU
SEQRES 2 A 374 VAL LEU PHE GLN GLY PRO MSE SER ASN ASP VAL ALA GLU
SEQRES 3 A 374 LEU LYS GLN TYR VAL LEU ALA HIS VAL SER ALA GLN ASN
SEQRES 4 A 374 ALA SER ALA ASP GLY VAL LEU ALA ARG ILE ASP ASP ASP
SEQRES 5 A 374 GLY ASP GLY PRO ARG SER TRP THR THR GLN TRP ILE ARG
SEQRES 6 A 374 ALA GLY GLU GLU ARG GLU GLN ALA GLY ASP LEU LEU ALA
SEQRES 7 A 374 ALA THR THR PHE TYR ASN MSE ALA ARG PHE PRO PHE VAL
SEQRES 8 A 374 ASP SER PRO GLY ARG ALA GLU ALA LEU ARG ARG CYS VAL
SEQRES 9 A 374 ALA VAL PHE ASP ARG TRP ARG ARG THR VAL PRO GLY ILE
SEQRES 10 A 374 GLU ARG LEU GLU LEU ARG LEU PRO GLY GLY VAL VAL ARG
SEQRES 11 A 374 ALA TRP ALA ALA GLY LEU SER THR THR GLU ARG ARG PRO
SEQRES 12 A 374 VAL LEU LEU MSE THR GLY GLY ILE VAL SER ILE LYS GLU
SEQRES 13 A 374 GLN TRP ALA PRO ILE LEU PRO GLU LEU ALA ARG TYR GLY
SEQRES 14 A 374 PHE ALA ALA VAL VAL THR GLU MSE PRO GLY VAL GLY GLU
SEQRES 15 A 374 ASN GLU LEU ARG TYR ASP LEU ASP SER ALA ALA LEU PHE
SEQRES 16 A 374 GLY VAL LEU LEU ASP ALA VAL ALA GLU ARG ALA ASP THR
SEQRES 17 A 374 SER ARG ALA TYR ALA MSE ALA LEU SER PHE SER GLY HIS
SEQRES 18 A 374 LEU ALA LEU ARG ALA ALA PRO SER GLU PRO ARG LEU ARG
SEQRES 19 A 374 GLY ILE VAL THR ALA GLY ALA PRO VAL ALA ALA PHE PHE
SEQRES 20 A 374 THR ASP LYS GLU TRP GLN ALA ALA VAL PRO ARG VAL THR
SEQRES 21 A 374 VAL ASP THR LEU ALA ARG LEU THR GLN THR THR PRO ALA
SEQRES 22 A 374 THR VAL PHE ASP HIS VAL ARG ASN TRP ALA LEU THR PRO
SEQRES 23 A 374 GLN ASP LEU ALA GLY VAL ARG ILE PRO VAL ALA TYR VAL
SEQRES 24 A 374 ALA SER GLY ARG ASP GLU ILE ILE PRO PRO ALA ASP PRO
SEQRES 25 A 374 ALA MSE LEU ARG THR HIS VAL ARG ASP PHE ARG THR ILE
SEQRES 26 A 374 THR HIS ASP ASP VAL HIS GLY SER PRO ALA HIS PHE PRO
SEQRES 27 A 374 HIS THR ARG LEU TRP THR LEU ALA GLN VAL LEU GLU MSE
SEQRES 28 A 374 SER GLY ALA ASP PRO ARG HIS ARG ALA ALA VAL ASP GLY
SEQRES 29 A 374 ALA LEU ALA GLN VAL GLU GLY GLY ARG ALA
MODRES 4YWF MSE A 0 MET MODIFIED RESIDUE
MODRES 4YWF MSE A 128 MET MODIFIED RESIDUE
MODRES 4YWF MSE A 332 MET MODIFIED RESIDUE
HET MSE A 0 8
HET MSE A 66 8
HET MSE A 128 8
HET MSE A 158 8
HET MSE A 195 8
HET MSE A 295 8
HET MSE A 332 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 HOH *50(H2 O)
HELIX 1 AA1 ASP A 3 TYR A 10 1 8
HELIX 2 AA2 SER A 39 ALA A 54 1 16
HELIX 3 AA3 ASP A 56 PHE A 69 1 14
HELIX 4 AA4 SER A 74 ARG A 93 1 20
HELIX 5 AA5 ILE A 135 PRO A 141 5 7
HELIX 6 AA6 ILE A 142 TYR A 149 1 8
HELIX 7 AA7 ASP A 171 ALA A 173 5 3
HELIX 8 AA8 ALA A 174 VAL A 183 1 10
HELIX 9 AA9 SER A 198 ALA A 208 1 11
HELIX 10 AB1 PRO A 209 GLU A 211 5 3
HELIX 11 AB2 ALA A 225 ASP A 230 1 6
HELIX 12 AB3 ASP A 230 VAL A 237 1 8
HELIX 13 AB4 PRO A 238 GLN A 250 1 13
HELIX 14 AB5 THR A 255 VAL A 260 1 6
HELIX 15 AB6 ARG A 261 ALA A 264 5 4
HELIX 16 AB7 THR A 266 GLY A 272 1 7
HELIX 17 AB8 PRO A 290 VAL A 300 1 11
HELIX 18 AB9 SER A 314 ALA A 316 5 3
HELIX 19 AC1 HIS A 317 SER A 333 1 17
HELIX 20 AC2 ASP A 336 LEU A 347 1 12
SHEET 1 AA1 8 GLU A 99 LEU A 105 0
SHEET 2 AA1 8 GLY A 108 ALA A 115 -1 O ALA A 114 N GLU A 99
SHEET 3 AA1 8 ALA A 152 VAL A 155 -1 O VAL A 155 N TRP A 113
SHEET 4 AA1 8 PRO A 124 THR A 129 1 N MSE A 128 O VAL A 154
SHEET 5 AA1 8 ASP A 188 ALA A 196 1 O MSE A 195 N LEU A 127
SHEET 6 AA1 8 LEU A 214 ALA A 220 1 O ARG A 215 N ALA A 192
SHEET 7 AA1 8 VAL A 277 ARG A 284 1 O ALA A 278 N THR A 219
SHEET 8 AA1 8 PHE A 303 VAL A 311 1 O HIS A 308 N GLY A 283
LINK C PRO A -1 N MSE A 0 1555 1555 1.33
LINK C MSE A 0 N SER A 1 1555 1555 1.34
LINK C ASN A 65 N MSE A 66 1555 1555 1.34
LINK C MSE A 66 N ALA A 67 1555 1555 1.32
LINK C LEU A 127 N MSE A 128 1555 1555 1.33
LINK C MSE A 128 N THR A 129 1555 1555 1.33
LINK C GLU A 157 N MSE A 158 1555 1555 1.33
LINK C MSE A 158 N PRO A 159 1555 1555 1.37
LINK C ALA A 194 N MSE A 195 1555 1555 1.34
LINK C MSE A 195 N ALA A 196 1555 1555 1.33
LINK C ALA A 294 N MSE A 295 1555 1555 1.33
LINK C MSE A 295 N LEU A 296 1555 1555 1.32
LINK C GLU A 331 N MSE A 332 1555 1555 1.35
LINK C MSE A 332 N SER A 333 1555 1555 1.31
CISPEP 1 PHE A 69 PRO A 70 0 4.75
CRYST1 92.080 87.180 47.910 90.00 101.63 90.00 C 1 2 1 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 0.010860 0.000000 0.002235 0.00000
SCALE2 0.000000 0.011470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021310 0.00000
TER 2494 LEU A 347
MASTER 405 0 7 20 8 0 0 6 2543 1 70 29
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