| content |
HEADER HYDROLASE 10-APR-17 5NO5
TITLE ABYA5 WILDTYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABYA5;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VERRUCOSISPORA;
SOURCE 3 ORGANISM_TAXID: 84593;
SOURCE 4 GENE: ABYA5, VAB18032_16440;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: B834
KEYWDS DEACETYLASE, ELIMINATION, HYDROLASE, SPIROTETRONATE, ACETYL LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.BYRNE,P.R.RACE
REVDAT 1 16-MAY-18 5NO5 0
JRNL AUTH M.J.BYRNE,P.R.RACE
JRNL TITL STRUCTURE OF ABYA5 WILDTYPE AT 2.5 ANGSTROMS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 26076
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1356
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1898
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5301
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.42000
REMARK 3 B22 (A**2) : 3.57000
REMARK 3 B33 (A**2) : -1.14000
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): 0.592
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.306
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.003
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5438 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5067 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7445 ; 1.714 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11607 ; 1.081 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 696 ; 6.224 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 241 ;30.423 ;22.116
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 780 ;15.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;19.304 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 856 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6184 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1192 ; 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): 2790 ; 0.903 ; 1.590
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2789 ; 0.903 ; 1.589
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3484 ; 1.502 ; 2.382
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3485 ; 1.502 ; 2.383
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2648 ; 1.285 ; 1.750
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2646 ; 1.285 ; 1.750
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3961 ; 2.123 ; 2.561
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5927 ; 3.057 ;18.749
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5916 ; 3.049 ;18.756
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 5NO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 65
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97887
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27564
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 41.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.3000
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) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4YWF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WILD TYPE ABYA5 DATA SETS WERE
REMARK 280 COLLECTED FROM CRYSTALS FORMED IN FORMED IN 12.5 % W/V PEG 1000,
REMARK 280 12.5% W/V PEG 3350, 12.5% V/V MPD, 0.02 M SODIUM L-GLUTAMATE,
REMARK 280 0.02 M DL-ALANINE, 0.02 M GLYCINE, 0.02 M DL-LYSINE, HCL, 0.02 M
REMARK 280 DL-SERINE, 0.1 M BICINE/TRIZMA BASE PH 8.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
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 34.61450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.64450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.18000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.64450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.61450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.18000
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: 2320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 GLY A 11
REMARK 465 LEU A 12
REMARK 465 GLU A 13
REMARK 465 VAL A 14
REMARK 465 LEU A 15
REMARK 465 PHE A 16
REMARK 465 GLN A 17
REMARK 465 GLY A 18
REMARK 465 PRO A 19
REMARK 465 MET A 20
REMARK 465 SER A 21
REMARK 465 GLY A 371
REMARK 465 GLY A 372
REMARK 465 ARG A 373
REMARK 465 ALA A 374
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 GLY B 11
REMARK 465 LEU B 12
REMARK 465 GLU B 13
REMARK 465 VAL B 14
REMARK 465 LEU B 15
REMARK 465 PHE B 16
REMARK 465 GLN B 17
REMARK 465 GLY B 18
REMARK 465 PRO B 19
REMARK 465 MET B 20
REMARK 465 SER B 21
REMARK 465 GLY B 371
REMARK 465 GLY B 372
REMARK 465 ARG B 373
REMARK 465 ALA B 374
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 GLN A 38 CG CD OE1 NE2
REMARK 470 ASP A 54 CG OD1 OD2
REMARK 470 ARG A 130 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 258 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 287 CG CD OE1 NE2
REMARK 470 ARG A 293 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 316 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 320 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 38 CG CD OE1 NE2
REMARK 470 GLN B 72 CG CD OE1 NE2
REMARK 470 ARG B 258 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 316 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 320 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 357 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 368 CG CD OE1 NE2
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 OD1 ASN A 84 NH1 ARG A 87 1.98
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 TRP A 158 CB TRP A 158 CG -0.127
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 87 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP A 200 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 280 NE - CZ - NH1 ANGL. DEV. = 3.6 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 VAL A 35 -49.59 -133.23
REMARK 500 SER A 217 -130.42 59.12
REMARK 500 VAL A 243 -70.41 -125.62
REMARK 500 ALA A 244 -61.13 -144.24
REMARK 500 THR A 270 -144.66 -118.83
REMARK 500 SER A 333 55.23 33.64
REMARK 500 VAL B 35 -46.33 -132.42
REMARK 500 SER B 217 -132.61 62.18
REMARK 500 VAL B 243 -69.52 -121.54
REMARK 500 ALA B 244 -58.91 -140.00
REMARK 500 THR B 270 -138.29 -113.88
REMARK 500 SER B 333 60.27 27.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YWF RELATED DB: PDB
REMARK 900 ABYA5_QM
DBREF 5NO5 A 20 374 UNP F4F7F5 F4F7F5_VERMA 1 355
DBREF 5NO5 B 20 374 UNP F4F7F5 F4F7F5_VERMA 1 355
SEQADV 5NO5 MET A 1 UNP F4F7F5 INITIATING METHIONINE
SEQADV 5NO5 ALA A 2 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS A 3 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS A 4 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS A 5 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS A 6 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS A 7 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS A 8 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 SER A 9 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 SER A 10 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLY A 11 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 LEU A 12 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLU A 13 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 VAL A 14 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 LEU A 15 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 PHE A 16 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLN A 17 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLY A 18 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 PRO A 19 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 MET B 1 UNP F4F7F5 INITIATING METHIONINE
SEQADV 5NO5 ALA B 2 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS B 3 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS B 4 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS B 5 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS B 6 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS B 7 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 HIS B 8 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 SER B 9 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 SER B 10 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLY B 11 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 LEU B 12 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLU B 13 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 VAL B 14 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 LEU B 15 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 PHE B 16 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLN B 17 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 GLY B 18 UNP F4F7F5 EXPRESSION TAG
SEQADV 5NO5 PRO B 19 UNP F4F7F5 EXPRESSION TAG
SEQRES 1 A 374 MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU
SEQRES 2 A 374 VAL LEU PHE GLN GLY PRO MET 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 LEU 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 MET 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 LEU 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 LEU 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 LEU 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 MET
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
SEQRES 1 B 374 MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU
SEQRES 2 B 374 VAL LEU PHE GLN GLY PRO MET SER ASN ASP VAL ALA GLU
SEQRES 3 B 374 LEU LYS GLN TYR VAL LEU ALA HIS VAL SER ALA GLN ASN
SEQRES 4 B 374 ALA SER ALA ASP GLY VAL LEU ALA ARG ILE ASP ASP ASP
SEQRES 5 B 374 GLY ASP GLY PRO ARG SER TRP THR THR GLN TRP ILE ARG
SEQRES 6 B 374 ALA GLY GLU GLU ARG GLU GLN ALA GLY ASP LEU LEU ALA
SEQRES 7 B 374 ALA THR THR PHE TYR ASN LEU ALA ARG PHE PRO PHE VAL
SEQRES 8 B 374 ASP SER PRO GLY ARG ALA GLU ALA LEU ARG ARG CYS VAL
SEQRES 9 B 374 ALA VAL PHE ASP ARG TRP ARG ARG THR VAL PRO GLY ILE
SEQRES 10 B 374 GLU ARG LEU GLU LEU ARG LEU PRO GLY GLY VAL VAL ARG
SEQRES 11 B 374 ALA TRP ALA ALA GLY LEU SER THR THR GLU ARG ARG PRO
SEQRES 12 B 374 VAL LEU LEU MET THR GLY GLY ILE VAL SER ILE LYS GLU
SEQRES 13 B 374 GLN TRP ALA PRO ILE LEU PRO GLU LEU ALA ARG TYR GLY
SEQRES 14 B 374 PHE ALA ALA VAL VAL THR GLU LEU PRO GLY VAL GLY GLU
SEQRES 15 B 374 ASN GLU LEU ARG TYR ASP LEU ASP SER ALA ALA LEU PHE
SEQRES 16 B 374 GLY VAL LEU LEU ASP ALA VAL ALA GLU ARG ALA ASP THR
SEQRES 17 B 374 SER ARG ALA TYR ALA LEU ALA LEU SER PHE SER GLY HIS
SEQRES 18 B 374 LEU ALA LEU ARG ALA ALA PRO SER GLU PRO ARG LEU ARG
SEQRES 19 B 374 GLY ILE VAL THR ALA GLY ALA PRO VAL ALA ALA PHE PHE
SEQRES 20 B 374 THR ASP LYS GLU TRP GLN ALA ALA VAL PRO ARG VAL THR
SEQRES 21 B 374 VAL ASP THR LEU ALA ARG LEU THR GLN THR THR PRO ALA
SEQRES 22 B 374 THR VAL PHE ASP HIS VAL ARG ASN TRP ALA LEU THR PRO
SEQRES 23 B 374 GLN ASP LEU ALA GLY VAL ARG ILE PRO VAL ALA TYR VAL
SEQRES 24 B 374 ALA SER GLY ARG ASP GLU ILE ILE PRO PRO ALA ASP PRO
SEQRES 25 B 374 ALA LEU LEU ARG THR HIS VAL ARG ASP PHE ARG THR ILE
SEQRES 26 B 374 THR HIS ASP ASP VAL HIS GLY SER PRO ALA HIS PHE PRO
SEQRES 27 B 374 HIS THR ARG LEU TRP THR LEU ALA GLN VAL LEU GLU MET
SEQRES 28 B 374 SER GLY ALA ASP PRO ARG HIS ARG ALA ALA VAL ASP GLY
SEQRES 29 B 374 ALA LEU ALA GLN VAL GLU GLY GLY ARG ALA
FORMUL 3 HOH *98(H2 O)
HELIX 1 AA1 ASP A 23 VAL A 35 1 13
HELIX 2 AA2 ALA A 40 ALA A 47 1 8
HELIX 3 AA3 SER A 58 GLY A 74 1 17
HELIX 4 AA4 ASP A 75 PHE A 88 1 14
HELIX 5 AA5 SER A 93 THR A 113 1 21
HELIX 6 AA6 ILE A 154 PRO A 160 5 7
HELIX 7 AA7 ILE A 161 TYR A 168 1 8
HELIX 8 AA8 ASP A 188 ALA A 192 5 5
HELIX 9 AA9 ALA A 193 VAL A 202 1 10
HELIX 10 AB1 SER A 217 ALA A 227 1 11
HELIX 11 AB2 PRO A 228 GLU A 230 5 3
HELIX 12 AB3 ALA A 244 ASP A 249 1 6
HELIX 13 AB4 ASP A 249 VAL A 256 1 8
HELIX 14 AB5 PRO A 257 GLN A 269 1 13
HELIX 15 AB6 THR A 274 VAL A 279 1 6
HELIX 16 AB7 ARG A 280 ALA A 283 5 4
HELIX 17 AB8 THR A 285 GLY A 291 1 7
HELIX 18 AB9 PRO A 309 VAL A 319 1 11
HELIX 19 AC1 SER A 333 ALA A 335 5 3
HELIX 20 AC2 HIS A 336 GLY A 353 1 18
HELIX 21 AC3 ASP A 355 GLU A 370 1 16
HELIX 22 AC4 ASP B 23 VAL B 35 1 13
HELIX 23 AC5 ALA B 40 ALA B 47 1 8
HELIX 24 AC6 SER B 58 ALA B 73 1 16
HELIX 25 AC7 ASP B 75 PHE B 88 1 14
HELIX 26 AC8 SER B 93 THR B 113 1 21
HELIX 27 AC9 ILE B 154 PRO B 160 5 7
HELIX 28 AD1 ILE B 161 TYR B 168 1 8
HELIX 29 AD2 ASP B 188 ALA B 192 5 5
HELIX 30 AD3 ALA B 193 VAL B 202 1 10
HELIX 31 AD4 SER B 217 ALA B 227 1 11
HELIX 32 AD5 PRO B 228 GLU B 230 5 3
HELIX 33 AD6 ALA B 244 ASP B 249 1 6
HELIX 34 AD7 ASP B 249 VAL B 256 1 8
HELIX 35 AD8 PRO B 257 GLN B 269 1 13
HELIX 36 AD9 THR B 274 VAL B 279 1 6
HELIX 37 AE1 ARG B 280 ALA B 283 5 4
HELIX 38 AE2 THR B 285 GLY B 291 1 7
HELIX 39 AE3 PRO B 309 VAL B 319 1 11
HELIX 40 AE4 SER B 333 ALA B 335 5 3
HELIX 41 AE5 HIS B 336 SER B 352 1 17
HELIX 42 AE6 ASP B 355 GLU B 370 1 16
SHEET 1 AA1 8 GLU A 118 LEU A 124 0
SHEET 2 AA1 8 GLY A 127 ALA A 134 -1 O VAL A 129 N LEU A 122
SHEET 3 AA1 8 ALA A 171 THR A 175 -1 O VAL A 174 N TRP A 132
SHEET 4 AA1 8 PRO A 143 THR A 148 1 N LEU A 145 O VAL A 173
SHEET 5 AA1 8 ASP A 207 ALA A 215 1 O LEU A 214 N LEU A 146
SHEET 6 AA1 8 LEU A 233 ALA A 239 1 O ARG A 234 N ALA A 211
SHEET 7 AA1 8 VAL A 296 SER A 301 1 O ALA A 297 N ILE A 236
SHEET 8 AA1 8 PHE A 322 HIS A 327 1 O ILE A 325 N ALA A 300
SHEET 1 AA2 8 GLU B 118 LEU B 124 0
SHEET 2 AA2 8 GLY B 127 ALA B 134 -1 O ALA B 133 N GLU B 118
SHEET 3 AA2 8 ALA B 171 THR B 175 -1 O VAL B 174 N TRP B 132
SHEET 4 AA2 8 PRO B 143 THR B 148 1 N PRO B 143 O ALA B 171
SHEET 5 AA2 8 ASP B 207 ALA B 215 1 O LEU B 214 N LEU B 146
SHEET 6 AA2 8 LEU B 233 ALA B 239 1 O ARG B 234 N ALA B 211
SHEET 7 AA2 8 VAL B 296 SER B 301 1 O ALA B 297 N ILE B 236
SHEET 8 AA2 8 PHE B 322 HIS B 327 1 O ILE B 325 N ALA B 300
CISPEP 1 PHE A 88 PRO A 89 0 7.11
CISPEP 2 PHE B 88 PRO B 89 0 7.74
CRYST1 69.229 88.360 131.289 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 0.014445 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007617 0.00000
TER 2649 GLU A 370
TER 5303 GLU B 370
MASTER 406 0 0 42 16 0 0 6 5399 2 0 58
END |