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HEADER HYDROLASE 05-OCT-08 3ESD
TITLE CUT-2B; NCN-PT-PINCER-CUTINASE HYBRID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CUTIN HYDROLASE 1;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI F. PISI;
SOURCE 3 ORGANISM_TAXID: 70791;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS PROTEIN-METALLOPINCER COMPLEX, GLYCOPROTEIN, HYDROLASE,
KEYWDS 2 SECRETED, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.RUTTEN,J.P.B.A.MANNIE,M.LUTZ,P.GROS
REVDAT 1 28-JUL-09 3ESD 0
JRNL AUTH L.RUTTEN,B.WIECZOREK,J.P.B.A.MANNIE,C.A.KRUITHOF,
JRNL AUTH 2 H.P.DIJKSTRA,M.R.EGMOND,M.LUTZ,R.J.M.KLEIN GEBBINK,
JRNL AUTH 3 P.GROS,G.VAN KOTEN
JRNL TITL SOLID-STATE STRUCTURAL CHARACTERIZATION OF
JRNL TITL 2 CUTINASE-ECE-PINCER-METAL HYBRIDS
JRNL REF CHEMISTRY V. 15 4270 2009
JRNL REFN ISSN 0947-6539
JRNL PMID 19219875
JRNL DOI 10.1002/CHEM.200801995
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.199
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 61949
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1430
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 ANGLE DISTANCES (A) : 0.040
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 TWINNING WAS OBSERVED IN THE PRESENT CRYSTAL AND REFINED WITH
REMARK 3 SHELXL USING THE TWIN INSTRUCTION,
REMARK 3 RESULTING IN A TWIN FRACTION OF 0.5, OPERATOR H,-H-K,-L.
REMARK 3 THE POINT GROUP 3 OF THE CRYSTAL LATTICE CAN BE OBTAINED VIA
REMARK 3 A COSET DECOMPOSITION OF POINT GROUP 32 OF THE TWIN LATTICE.
REMARK 3 THE TWOFOLD TWIN AXIS CANNOT BE A REAL CRYSTALLOGRAPHIC
REMARK 3 OPERATION
REMARK 3 BECAUSE THIS WOULD RESULT IN ONLY HALF A MOLECULE IN THE
REMARK 3 ASYMMETRIC UNIT.
REMARK 4
REMARK 4 3ESD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-08.
REMARK 100 THE RCSB ID CODE IS RCSB049707.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61949
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.220
REMARK 200 RESOLUTION RANGE LOW (A) : 41.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.200
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: 1CUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6%(W/V) PEG-3350, 30%(V/V)
REMARK 280 GLYCEROL, 0.05M BISTRISP, 0.1M POTASSIUM THIOCYANATE, PH 8.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.18000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.88853
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.92333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 36.18000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 20.88853
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.92333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 36.18000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 20.88853
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.92333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.77707
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 73.84667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 41.77707
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 73.84667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 41.77707
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 73.84667
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 A 284 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 LEU A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 ASN A 5
REMARK 465 PRO A 6
REMARK 465 ALA A 7
REMARK 465 GLN A 8
REMARK 465 GLU A 9
REMARK 465 LEU A 10
REMARK 465 GLU A 11
REMARK 465 ALA A 12
REMARK 465 ARG A 13
REMARK 465 GLN A 14
REMARK 465 LEU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 212
REMARK 465 SER A 213
REMARK 465 ALA A 214
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 ARG A 40 NE ARG A 40 CZ -0.096
REMARK 500 ARG A 40 CZ ARG A 40 NH1 0.111
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 20 NE - CZ - NH1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 22 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 ASP A 22 OD1 - CG - OD2 ANGL. DEV. = -14.3 DEGREES
REMARK 500 ASP A 22 CB - CG - OD1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 22 CB - CG - OD2 ANGL. DEV. = 21.1 DEGREES
REMARK 500 LEU A 23 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 ALA A 32 O - C - N ANGL. DEV. = 18.5 DEGREES
REMARK 500 TYR A 38 CB - CG - CD2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR A 38 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 40 CD - NE - CZ ANGL. DEV. = 19.7 DEGREES
REMARK 500 ARG A 40 NH1 - CZ - NH2 ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG A 40 NE - CZ - NH1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ARG A 40 NE - CZ - NH2 ANGL. DEV. = 24.1 DEGREES
REMARK 500 ARG A 40 O - C - N ANGL. DEV. = 11.0 DEGREES
REMARK 500 GLU A 44 CA - C - N ANGL. DEV. = -15.8 DEGREES
REMARK 500 GLU A 44 O - C - N ANGL. DEV. = 21.3 DEGREES
REMARK 500 ASN A 47 OD1 - CG - ND2 ANGL. DEV. = 19.9 DEGREES
REMARK 500 ASN A 47 CB - CG - ND2 ANGL. DEV. = -16.7 DEGREES
REMARK 500 GLY A 49 CA - C - O ANGL. DEV. = 11.3 DEGREES
REMARK 500 GLY A 49 O - C - N ANGL. DEV. = -13.2 DEGREES
REMARK 500 TYR A 77 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 TYR A 77 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR A 77 CG - CD1 - CE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR A 77 CD1 - CE1 - CZ ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 78 CA - CB - CG ANGL. DEV. = 13.5 DEGREES
REMARK 500 ALA A 79 O - C - N ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ALA A 112 CA - C - O ANGL. DEV. = -13.5 DEGREES
REMARK 500 ALA A 112 CA - C - N ANGL. DEV. = -13.7 DEGREES
REMARK 500 ALA A 112 O - C - N ANGL. DEV. = 27.2 DEGREES
REMARK 500 LEU A 125 CA - C - O ANGL. DEV. = -16.1 DEGREES
REMARK 500 LEU A 125 O - C - N ANGL. DEV. = 17.2 DEGREES
REMARK 500 ARG A 138 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 138 CA - C - O ANGL. DEV. = 12.8 DEGREES
REMARK 500 ASP A 139 CA - C - O ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG A 138 O - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 PHE A 147 CB - CG - CD1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 GLY A 148 CA - C - O ANGL. DEV. = 26.2 DEGREES
REMARK 500 TYR A 149 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 TYR A 149 CG - CD1 - CE1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 TYR A 149 CG - CD2 - CE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 TYR A 149 CZ - CE2 - CD2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLY A 148 O - C - N ANGL. DEV. = -17.0 DEGREES
REMARK 500 GLN A 154 CG - CD - OE1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 GLY A 157 CA - C - O ANGL. DEV. = -16.1 DEGREES
REMARK 500 ARG A 158 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 68 ANGLE DEVIATIONS.
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 SER A 120 -117.12 56.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 251 DISTANCE = 5.79 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 SXC A 215
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SXC A 215
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEE REFERENCE 2 IN UNIPROT DATABASE P00590
DBREF 3ESD A 1 214 UNP P00590 CUTI1_FUSSO 17 230
SEQADV 3ESD ALA A 32 UNP P00590 ARG 48 SEE REMARK 999
SEQADV 3ESD LYS A 172 UNP P00590 ASN 188 ENGINEERED
SEQRES 1 A 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 A 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 A 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 A 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 A 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 A 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 A 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER
SEQRES 8 A 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 A 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 A 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 A 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 A 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 A 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 A 214 PHE CYS LYS THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 A 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA
SEQRES 16 A 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 A 214 ALA VAL ARG GLY SER ALA
HET SXC A 215 22
HETNAM SXC BROMO(4-{3-[(R)-ETHOXY(4-NITROPHENOXY)
HETNAM 2 SXC PHOSPHORYL]PROPYL}-2,6-BIS[(METHYLSULFANYL-KAPPAS)
HETNAM 3 SXC METHYL]PHENYL-KAPPAC~1~)PALLADIUM(2+)
HETSYN SXC ETHYL 4-NITROPHENYL P-[3-(4-(BROMOPALLADO)-1,3-
HETSYN 2 SXC BIS[(METHYLTHIO)METHYL]-PHENYL)PROPYL]PHOSPHONATE
FORMUL 2 SXC C21 H27 BR N O5 P PD S2 2+
FORMUL 3 HOH *73(H2 O)
HELIX 1 1 ASN A 27 CYS A 31 5 5
HELIX 2 2 LEU A 51 GLY A 64 1 14
HELIX 3 3 LEU A 81 LEU A 86 5 6
HELIX 4 4 SER A 91 CYS A 109 1 19
HELIX 5 5 SER A 120 LEU A 133 1 14
HELIX 6 6 ASP A 134 LYS A 140 1 7
HELIX 7 7 PRO A 163 ASP A 165 5 3
HELIX 8 8 ASP A 175 GLY A 180 5 6
HELIX 9 9 ALA A 185 ALA A 190 5 6
HELIX 10 10 TYR A 191 GLY A 197 1 7
HELIX 11 11 GLY A 197 ARG A 211 1 15
SHEET 1 A 5 VAL A 68 GLY A 72 0
SHEET 2 A 5 VAL A 34 ALA A 39 1 N PHE A 36 O TRP A 69
SHEET 3 A 5 THR A 113 TYR A 119 1 O ILE A 115 N ILE A 35
SHEET 4 A 5 ILE A 141 PHE A 147 1 O VAL A 145 N ALA A 116
SHEET 5 A 5 THR A 167 PHE A 170 1 O PHE A 170 N LEU A 146
SSBOND 1 CYS A 31 CYS A 109 1555 1555 2.05
SSBOND 2 CYS A 171 CYS A 178 1555 1555 2.08
LINK OG SER A 120 P1 SXC A 215 1555 1555 1.57
SITE 1 AC1 10 SER A 42 LEU A 81 GLY A 82 ASN A 84
SITE 2 AC1 10 TYR A 119 SER A 120 GLN A 121 LEU A 182
SITE 3 AC1 10 ILE A 183 HIS A 188
CRYST1 72.360 72.360 110.770 90.00 90.00 120.00 H 3 9
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 0.013820 0.007979 0.000000 0.00000
SCALE2 0.000000 0.015958 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009028 0.00000
TER 1431 ARG A 211
MASTER 378 0 1 11 5 0 3 6 1525 1 27 17
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