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HEADER TRANSFERASE 12-JUN-14 4QLO
TITLE CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE FROM
TITLE 2 STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.1.31;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE 3 ORGANISM_TAXID: 451516;
SOURCE 4 STRAIN: TCH1516;
SOURCE 5 GENE: AZ30_00060, METX, SACOL0012, USA300HOU_0012;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST42
KEYWDS ROSSMANN FOLD, ACETYLTRANSFERASE, ACETYLCO-A BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.THANGAVELU,A.G.PAVLOVSKY,R.E.VIOLA
REVDAT 1 20-AUG-14 4QLO 0
JRNL AUTH B.THANGAVELU,A.G.PAVLOVSKY,R.E.VIOLA
JRNL TITL CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE FROM
JRNL TITL 2 STAPHYLOCOCCUS AUREUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 12155
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) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 635
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) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 561
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 28
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.23000
REMARK 3 B22 (A**2) : 2.23000
REMARK 3 B33 (A**2) : -7.23000
REMARK 3 B12 (A**2) : 1.11000
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): 0.853
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.352
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.295
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.646
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2733 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2529 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3708 ; 1.359 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5790 ; 0.796 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 328 ; 7.500 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;36.573 ;23.425
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 438 ;17.401 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;17.485 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 393 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3147 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 708 ; 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): 1309 ; 2.915 ; 5.605
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1308 ; 2.914 ; 5.602
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1635 ; 4.483 ; 8.399
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1636 ; 4.425 ; 8.736
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1424 ; 3.061 ; 6.061
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1425 ; 3.042 ; 6.243
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2073 ; 4.821 ; 9.244
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3122 ; 6.882 ;47.943
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3122 ; 6.878 ;47.954
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 4QLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-14.
REMARK 100 THE RCSB ID CODE IS RCSB086211.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI 111
REMARK 200 OPTICS : HORIZONTALLY AND VERTICALLY
REMARK 200 FOCUSING BIMORPH MIRRORS IN
REMARK 200 KIRKPATRICK-BAEZ CONFIGURATION
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12887
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.15300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 M AMMONIUM FORMATE, 100 MM
REMARK 280 IMIDAZOLE HYDROCHLORIDE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 160.47233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 320.94467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 240.70850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 401.18083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.23617
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 160.47233
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 320.94467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 401.18083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 240.70850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 80.23617
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 80.23617
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 THR A 2
REMARK 465 VAL A 330
REMARK 465 VAL A 331
REMARK 465 ILE A 332
REMARK 465 ASN A 333
REMARK 465 SER A 334
REMARK 465 LYS A 335
REMARK 465 LEU A 336
REMARK 465 GLU A 337
REMARK 465 GLY A 338
REMARK 465 LYS A 339
REMARK 465 PRO A 340
REMARK 465 ILE A 341
REMARK 465 PRO A 342
REMARK 465 ASN A 343
REMARK 465 PRO A 344
REMARK 465 LEU A 345
REMARK 465 LEU A 346
REMARK 465 GLY A 347
REMARK 465 LEU A 348
REMARK 465 ASP A 349
REMARK 465 SER A 350
REMARK 465 THR A 351
REMARK 465 ARG A 352
REMARK 465 THR A 353
REMARK 465 GLY A 354
REMARK 465 HIS A 355
REMARK 465 HIS A 356
REMARK 465 HIS A 357
REMARK 465 HIS A 358
REMARK 465 HIS A 359
REMARK 465 HIS A 360
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 LYS A 198 CG CD CE NZ
REMARK 470 LYS A 283 CG CD CE NZ
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 CG2 THR A 205 OE1 GLU A 208 1.71
REMARK 500 O PHE A 326 O LYS A 329 1.78
REMARK 500 O ILE A 116 O LEU A 119 2.13
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 TYR A 58 72.39 -119.32
REMARK 500 ASP A 122 -50.48 -136.71
REMARK 500 SER A 197 -128.87 -89.20
REMARK 500 LYS A 198 4.07 -55.42
REMARK 500 PHE A 204 -104.50 -53.29
REMARK 500 ASP A 207 -32.50 94.17
REMARK 500 ASN A 240 111.06 -170.61
REMARK 500 ASN A 293 106.98 -163.22
REMARK 500 LYS A 317 36.27 -171.37
REMARK 500 ASP A 323 -38.97 106.14
REMARK 500 LEU A 327 69.21 -68.48
REMARK 500 TYR A 328 48.13 178.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4QLO A 1 322 UNP A8YYT5 A8YYT5_STAAT 1 322
SEQADV 4QLO ASP A 323 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO PRO A 324 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO ALA A 325 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO PHE A 326 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LEU A 327 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO TYR A 328 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LYS A 329 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO VAL A 330 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO VAL A 331 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO ILE A 332 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO ASN A 333 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO SER A 334 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LYS A 335 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LEU A 336 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO GLU A 337 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO GLY A 338 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LYS A 339 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO PRO A 340 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO ILE A 341 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO PRO A 342 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO ASN A 343 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO PRO A 344 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LEU A 345 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LEU A 346 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO GLY A 347 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO LEU A 348 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO ASP A 349 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO SER A 350 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO THR A 351 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO ARG A 352 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO THR A 353 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO GLY A 354 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO HIS A 355 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO HIS A 356 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO HIS A 357 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO HIS A 358 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO HIS A 359 UNP A8YYT5 EXPRESSION TAG
SEQADV 4QLO HIS A 360 UNP A8YYT5 EXPRESSION TAG
SEQRES 1 A 360 MET THR ASN TYR THR VAL ASP THR LEU ASN LEU GLY GLU
SEQRES 2 A 360 PHE ILE THR GLU SER GLY GLU VAL ILE ASP ASN LEU ARG
SEQRES 3 A 360 LEU ARG TYR GLU HIS VAL GLY TYR HIS GLY GLN PRO LEU
SEQRES 4 A 360 VAL VAL VAL CYS HIS ALA LEU THR GLY ASN HIS LEU THR
SEQRES 5 A 360 TYR GLY THR ASP ASP TYR PRO GLY TRP TRP ARG GLU ILE
SEQRES 6 A 360 ILE ASP GLY GLY TYR ILE PRO ILE HIS ASP TYR GLN PHE
SEQRES 7 A 360 LEU THR PHE ASP VAL ILE GLY SER PRO PHE GLY SER SER
SEQRES 8 A 360 SER PRO LEU ASN ASP PRO HIS PHE PRO LYS LYS LEU THR
SEQRES 9 A 360 LEU ARG ASP ILE VAL ARG ALA ASN GLU ARG GLY ILE GLN
SEQRES 10 A 360 ALA LEU GLY TYR ASP LYS ILE ASN ILE LEU ILE GLY GLY
SEQRES 11 A 360 SER LEU GLY GLY MET GLN ALA MET GLU LEU LEU TYR ASN
SEQRES 12 A 360 GLN GLN PHE GLU VAL ASP LYS ALA ILE ILE LEU ALA ALA
SEQRES 13 A 360 THR SER ARG THR SER SER TYR SER ARG ALA PHE ASN GLU
SEQRES 14 A 360 ILE ALA ARG GLN ALA ILE HIS LEU GLY GLY LYS GLU GLY
SEQRES 15 A 360 LEU SER ILE ALA ARG GLN LEU GLY PHE LEU THR TYR ARG
SEQRES 16 A 360 SER SER LYS SER TYR ASP GLU ARG PHE THR PRO ASP GLU
SEQRES 17 A 360 VAL VAL ALA TYR GLN GLN HIS GLN GLY ASN LYS PHE LYS
SEQRES 18 A 360 GLU HIS PHE ASP LEU ASN CYS TYR LEU THR LEU LEU ASP
SEQRES 19 A 360 VAL LEU ASP SER HIS ASN ILE ASP ARG GLY ARG THR ASP
SEQRES 20 A 360 VAL THR HIS VAL PHE LYS ASN LEU GLU THR LYS VAL LEU
SEQRES 21 A 360 THR MET GLY PHE ILE ASP ASP LEU LEU TYR PRO ASP ASP
SEQRES 22 A 360 GLN VAL ARG ALA LEU GLY GLU ARG PHE LYS TYR HIS ARG
SEQRES 23 A 360 HIS PHE PHE VAL PRO ASP ASN VAL GLY HIS ASP GLY PHE
SEQRES 24 A 360 LEU LEU ASN PHE SER THR TRP ALA PRO ASN LEU TYR HIS
SEQRES 25 A 360 PHE LEU ASN LEU LYS HIS PHE LYS ARG LYS ASP PRO ALA
SEQRES 26 A 360 PHE LEU TYR LYS VAL VAL ILE ASN SER LYS LEU GLU GLY
SEQRES 27 A 360 LYS PRO ILE PRO ASN PRO LEU LEU GLY LEU ASP SER THR
SEQRES 28 A 360 ARG THR GLY HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *28(H2 O)
HELIX 1 1 TRP A 62 GLY A 68 1 7
HELIX 2 2 THR A 104 LEU A 119 1 16
HELIX 3 3 SER A 131 GLN A 144 1 14
HELIX 4 4 SER A 161 GLY A 179 1 19
HELIX 5 5 GLY A 179 LEU A 189 1 11
HELIX 6 6 GLY A 190 TYR A 194 5 5
HELIX 7 7 LYS A 198 ARG A 203 1 6
HELIX 8 8 VAL A 209 PHE A 224 1 16
HELIX 9 9 ASP A 225 SER A 238 1 14
HELIX 10 10 ASP A 247 ASN A 254 1 8
HELIX 11 11 PRO A 271 GLU A 280 1 10
HELIX 12 12 GLY A 295 PHE A 299 5 5
HELIX 13 13 ASN A 302 THR A 305 5 4
HELIX 14 14 TRP A 306 ASN A 315 1 10
HELIX 15 15 ASP A 323 LEU A 327 5 5
SHEET 1 A 8 TYR A 4 ASN A 10 0
SHEET 2 A 8 ARG A 26 VAL A 32 -1 O HIS A 31 N THR A 5
SHEET 3 A 8 GLN A 77 PHE A 81 -1 O PHE A 78 N VAL A 32
SHEET 4 A 8 LEU A 39 CYS A 43 1 N VAL A 40 O GLN A 77
SHEET 5 A 8 LYS A 123 GLY A 130 1 O ILE A 128 N CYS A 43
SHEET 6 A 8 GLU A 147 LEU A 154 1 O LYS A 150 N ASN A 125
SHEET 7 A 8 LYS A 258 PHE A 264 1 O LEU A 260 N ALA A 151
SHEET 8 A 8 TYR A 284 VAL A 290 1 O ARG A 286 N THR A 261
SHEET 1 B 2 PHE A 14 ILE A 15 0
SHEET 2 B 2 VAL A 21 ILE A 22 -1 O ILE A 22 N PHE A 14
CISPEP 1 GLY A 130 SER A 131 0 -1.72
CISPEP 2 TYR A 328 LYS A 329 0 -6.50
CRYST1 49.155 49.155 481.417 90.00 90.00 120.00 P 61 2 2 12
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 0.020344 0.011746 0.000000 0.00000
SCALE2 0.000000 0.023491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002077 0.00000
TER 2661 LYS A 329
MASTER 371 0 0 15 10 0 0 6 2680 1 0 28
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