HEADER HYDROLASE 02-APR-07 2UY5
TITLE SCCTS1_KINETIN CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOCHITINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 22-315;
COMPND 5 SYNONYM: SOLUBLE CELL WALL PROTEIN 2, SCCTS1;
COMPND 6 EC: 3.2.1.14;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: X-33
KEYWDS CARBOHYDRATE METABOLISM, POLYSACCHARIDE DEGRADATION, CHITINASE,
KEYWDS 2 GLYCOSIDE HYDROLASE FAMILY 18, CHITIN-BINDING, CHITIN DEGRADATION,
KEYWDS 3 CAZY, HYDROLASE, GLYCOSIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.HURTADO-GUERRERO,D.M.F.VAN AALTEN
REVDAT 4 13-DEC-23 2UY5 1 REMARK
REVDAT 3 13-JUL-11 2UY5 1 VERSN
REVDAT 2 24-FEB-09 2UY5 1 VERSN
REVDAT 1 24-APR-07 2UY5 0
JRNL AUTH R.HURTADO-GUERRERO,D.M.F.VAN AALTEN
JRNL TITL STRUCTURE OF SACCHAROMYCES CEREVISIAE CHITINASE 1 AND
JRNL TITL 2 SCREENING-BASED DISCOVERY OF POTENT INHIBITORS.
JRNL REF CHEM.BIOL. V. 14 589 2007
JRNL REFN ISSN 1074-5521
JRNL PMID 17524989
JRNL DOI 10.1016/J.CHEMBIOL.2007.03.015
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 39014
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 825
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2180
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 40
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2159
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.89000
REMARK 3 B22 (A**2) : 0.75000
REMARK 3 B33 (A**2) : 0.13000
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): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.522
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2254 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3081 ; 1.542 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 295 ; 8.092 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;41.495 ;26.095
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 325 ;12.325 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;12.259 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 340 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1763 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1087 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1549 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 160 ; 0.129 ; 0.200
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): 39 ; 0.182 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.173 ; 0.200
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): 1452 ; 0.815 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2276 ; 1.204 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 928 ; 1.923 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 799 ; 2.883 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 26 A 310
REMARK 3 ORIGIN FOR THE GROUP (A): 42.7099 21.6962 32.6508
REMARK 3 T TENSOR
REMARK 3 T11: -0.0869 T22: -0.1316
REMARK 3 T33: -0.1475 T12: -0.0086
REMARK 3 T13: -0.0145 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 5.1970 L22: 1.1986
REMARK 3 L33: 0.4783 L12: -1.0443
REMARK 3 L13: -0.0951 L23: 0.0462
REMARK 3 S TENSOR
REMARK 3 S11: -0.1002 S12: 0.0138 S13: 0.4866
REMARK 3 S21: -0.0234 S22: 0.0760 S23: -0.0580
REMARK 3 S31: -0.0397 S32: 0.0015 S33: 0.0242
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1313 A 1313
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2133 23.6290 25.4075
REMARK 3 T TENSOR
REMARK 3 T11: -0.0148 T22: 0.0513
REMARK 3 T33: -0.0584 T12: 0.0471
REMARK 3 T13: -0.0494 T23: 0.0930
REMARK 3 L TENSOR
REMARK 3 L11: 29.0006 L22: 22.5888
REMARK 3 L33: 44.0231 L12: 22.0719
REMARK 3 L13: 6.1343 L23: 20.3973
REMARK 3 S TENSOR
REMARK 3 S11: -0.3236 S12: 2.0796 S13: 1.6312
REMARK 3 S21: 0.4324 S22: 0.3640 S23: -0.0305
REMARK 3 S31: -0.1634 S32: 0.5166 S33: -0.0403
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2UY5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1290032093.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 77.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39904
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2HVM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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 -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 36.67300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.81000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.67300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.81000
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 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 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 HOH A2040 LIES ON A SPECIAL POSITION.
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 ASP A 22
REMARK 465 ARG A 23
REMARK 465 SER A 24
REMARK 465 ALA A 25
REMARK 465 ASN A 296
REMARK 465 GLN A 313
REMARK 465 THR A 314
REMARK 465 ALA A 315
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 295 C O
REMARK 470 GLY A 297 N CA
REMARK 470 SER A 312 CB OG
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 ALA A 72 -128.77 43.78
REMARK 500 LEU A 115 139.91 179.97
REMARK 500 ALA A 139 25.11 -76.40
REMARK 500 ASP A 145 -124.53 49.32
REMARK 500 ASP A 155 61.79 -108.06
REMARK 500 SER A 219 166.10 -47.86
REMARK 500 SER A 251 -172.73 -170.18
REMARK 500 ALA A 252 -70.43 -68.28
REMARK 500 SER A 253 -65.50 74.58
REMARK 500 SER A 264 -131.03 54.87
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 SER A 251 ALA A 252 -148.74
REMARK 500 ALA A 252 SER A 253 61.02
REMARK 500 THR A 263 SER A 264 86.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE A 260 -12.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H35 A1313
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2UY2 RELATED DB: PDB
REMARK 900 SCCTS1_APO CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 2UY3 RELATED DB: PDB
REMARK 900 SCCTS1_8-CHLOROTHEOPHYLLINE CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 2UY4 RELATED DB: PDB
REMARK 900 SCCTS1_ACETAZOLAMIDE CRYSTAL STRUCTURE
DBREF 2UY5 A 22 315 UNP P29029 CHIT_YEAST 22 315
SEQRES 1 A 294 ASP ARG SER ALA ASN THR ASN ILE ALA VAL TYR TRP GLY
SEQRES 2 A 294 GLN ASN SER ALA GLY THR GLN GLU SER LEU ALA THR TYR
SEQRES 3 A 294 CYS GLU SER SER ASP ALA ASP ILE PHE LEU LEU SER PHE
SEQRES 4 A 294 LEU ASN GLN PHE PRO THR LEU GLY LEU ASN PHE ALA ASN
SEQRES 5 A 294 ALA CYS SER ASP THR PHE SER ASP GLY LEU LEU HIS CYS
SEQRES 6 A 294 THR GLN ILE ALA GLU ASP ILE GLU THR CYS GLN SER LEU
SEQRES 7 A 294 GLY LYS LYS VAL LEU LEU SER LEU GLY GLY ALA SER GLY
SEQRES 8 A 294 SER TYR LEU PHE SER ASP ASP SER GLN ALA GLU THR PHE
SEQRES 9 A 294 ALA GLN THR LEU TRP ASP THR PHE GLY GLU GLY THR GLY
SEQRES 10 A 294 ALA SER GLU ARG PRO PHE ASP SER ALA VAL VAL ASP GLY
SEQRES 11 A 294 PHE ASP PHE ASP ILE GLU ASN ASN ASN GLU VAL GLY TYR
SEQRES 12 A 294 SER ALA LEU ALA THR LYS LEU ARG THR LEU PHE ALA GLU
SEQRES 13 A 294 GLY THR LYS GLN TYR TYR LEU SER ALA ALA PRO GLN CYS
SEQRES 14 A 294 PRO TYR PRO ASP ALA SER VAL GLY ASP LEU LEU GLU ASN
SEQRES 15 A 294 ALA ASP ILE ASP PHE ALA PHE ILE GLN PHE TYR ASN ASN
SEQRES 16 A 294 TYR CYS SER VAL SER GLY GLN PHE ASN TRP ASP THR TRP
SEQRES 17 A 294 LEU THR TYR ALA GLN THR VAL SER PRO ASN LYS ASN ILE
SEQRES 18 A 294 LYS LEU PHE LEU GLY LEU PRO GLY SER ALA SER ALA ALA
SEQRES 19 A 294 GLY SER GLY TYR ILE SER ASP THR SER LEU LEU GLU SER
SEQRES 20 A 294 THR ILE ALA ASP ILE ALA SER SER SER SER PHE GLY GLY
SEQRES 21 A 294 ILE ALA LEU TRP ASP ALA SER GLN ALA PHE SER ASN GLU
SEQRES 22 A 294 LEU ASN GLY GLU PRO TYR VAL GLU ILE LEU LYS ASN LEU
SEQRES 23 A 294 LEU THR SER ALA SER GLN THR ALA
HET H35 A1313 16
HETNAM H35 N-(FURAN-2-YLMETHYL)-7H-PURIN-6-AMINE
FORMUL 2 H35 C10 H9 N5 O
FORMUL 3 HOH *192(H2 O)
HELIX 1 1 SER A 43 GLU A 49 1 7
HELIX 2 2 PHE A 71 CYS A 75 5 5
HELIX 3 3 CYS A 86 LEU A 99 1 14
HELIX 4 4 ASP A 118 GLY A 134 1 17
HELIX 5 5 GLY A 163 ALA A 176 1 14
HELIX 6 6 VAL A 197 ALA A 204 1 8
HELIX 7 7 ASN A 225 VAL A 236 1 12
HELIX 8 8 ASP A 262 ALA A 274 1 13
HELIX 9 9 ASP A 286 ASN A 293 1 8
HELIX 10 10 PRO A 299 SER A 312 1 14
SHEET 1 AA11 ASN A 28 TRP A 33 0
SHEET 2 AA11 PHE A 279 TRP A 285 1 O GLY A 280 N ASN A 28
SHEET 3 AA11 LYS A 243 PRO A 249 1 O LEU A 244 N GLY A 280
SHEET 4 AA11 PHE A 208 GLN A 212 1 O ALA A 209 N PHE A 245
SHEET 5 AA11 TYR A 183 ALA A 186 1 O ALA A 186 N PHE A 210
SHEET 6 AA11 GLY A 151 ASP A 155 1 O PHE A 152 N SER A 185
SHEET 7 AA11 LYS A 102 GLY A 108 1 O LEU A 105 N ASP A 153
SHEET 8 AA11 ILE A 55 GLN A 63 1 O PHE A 56 N LEU A 104
SHEET 9 AA11 ASN A 28 TRP A 33 1 O VAL A 31 N LEU A 57
SHEET 10 AA11 PHE A 279 TRP A 285 1 O GLY A 280 N ASN A 28
SHEET 11 AA11 ASN A 28 TRP A 33 1 O ASN A 28 N ILE A 282
SSBOND 1 CYS A 48 CYS A 96 1555 1555 2.01
SSBOND 2 CYS A 75 CYS A 86 1555 1555 2.06
SSBOND 3 CYS A 190 CYS A 218 1555 1555 2.06
CISPEP 1 SER A 59 PHE A 60 0 6.91
CISPEP 2 PHE A 64 PRO A 65 0 2.74
CISPEP 3 TYR A 192 PRO A 193 0 -1.25
CISPEP 4 TRP A 285 ASP A 286 0 -7.01
SITE 1 AC1 8 TYR A 32 PHE A 60 ASP A 155 GLU A 157
SITE 2 AC1 8 PHE A 210 GLN A 212 TYR A 214 TRP A 285
CRYST1 73.346 111.620 37.268 90.00 90.00 90.00 P 21 21 2 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 0.013634 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026833 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
