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HEADER HYDROLASE 08-SEP-08 3EF3
TITLE CUT-1A; 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. SP. 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 3EF3 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. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0008
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 39725
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2109
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2897
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1482
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 322
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.02000
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): 0.058
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.913
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1545 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2119 ; 1.454 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 216 ; 4.672 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 63 ;34.493 ;23.016
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 241 ;12.042 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;13.157 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 237 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1190 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 709 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1067 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 245 ; 0.137 ; 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): 34 ; 0.197 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.184 ; 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): 1016 ; 0.602 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1596 ; 0.988 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 611 ; 1.715 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 510 ; 2.826 ; 4.500
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 20 A 200
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0872 15.6246 28.1998
REMARK 3 T TENSOR
REMARK 3 T11: -0.0166 T22: -0.0150
REMARK 3 T33: -0.0127 T12: -0.0011
REMARK 3 T13: -0.0042 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.3780 L22: 0.3705
REMARK 3 L33: 0.5496 L12: 0.0932
REMARK 3 L13: -0.0204 L23: -0.0492
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: 0.0302 S13: 0.0251
REMARK 3 S21: 0.0118 S22: 0.0037 S23: -0.0216
REMARK 3 S31: 0.0185 S32: -0.0149 S33: -0.0108
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 215 A 215
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7008 21.0803 44.1350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0016 T22: -0.0535
REMARK 3 T33: -0.0030 T12: 0.0247
REMARK 3 T13: 0.0221 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 8.2491 L22: 23.6561
REMARK 3 L33: 38.7429 L12: 10.9816
REMARK 3 L13: -11.1580 L23: -0.2348
REMARK 3 S TENSOR
REMARK 3 S11: 1.8293 S12: 0.7384 S13: -0.7178
REMARK 3 S21: -0.5023 S22: -1.0450 S23: 1.8901
REMARK 3 S31: -1.7277 S32: 0.1534 S33: -0.7842
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3EF3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-08.
REMARK 100 THE RCSB ID CODE IS RCSB049243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41835
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.63000
REMARK 200 FOR SHELL : 2.500
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: PDB ENTRY 1CUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG-6000, 0.1M SODIUM
REMARK 280 ACETATE, 0.2M SODIUM CHLORIDE, PH 4.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.63750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.89700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.76300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.63750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.89700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.76300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.63750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.89700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.76300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.63750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.89700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.76300
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 239 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 389 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 SER A 213
REMARK 465 ALA A 214
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 THR A 43 -3.29 69.63
REMARK 500 SER A 120 -120.09 60.31
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 526 DISTANCE = 6.59 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 NXC 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 NXC A 215
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEE REFERENCE 2 IN UNIPROT DATABASE P00590
DBREF 3EF3 A 1 214 UNP P00590 CUTI1_FUSSO 17 230
SEQADV 3EF3 ALA A 32 UNP P00590 ARG 48 SEE REMARK 999
SEQADV 3EF3 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 NXC A 215 24
HETNAM NXC (2,6-BIS[(DIMETHYLAMINO-KAPPAN)METHYL]-4-{3-[(S)-
HETNAM 2 NXC ETHOXY(4-NITROPHENOXY)PHOSPHORYL]PROPYL}PHENYL-
HETNAM 3 NXC KAPPAC~1~)(CHLORO)PLATINUM(2+)
HETSYN NXC ETHYL 4-NITROPHENYL P-[3-(4-(CHLOROPLATINO)-1,3-BIS >
HETSYN 2 NXC [(DIMETHYLAMINO)METHYL]-PHENYL)PROPYL]PHOSPHONATE
FORMUL 2 NXC C23 H33 CL N3 O5 P PT 2+
FORMUL 3 HOH *322(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 THR A 80 LEU A 86 5 7
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 ASP A 139 1 6
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 GLY A 212 1 16
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 THR A 113 N ILE A 35
SHEET 4 A 5 ILE A 141 PHE A 147 1 O PHE A 147 N GLY A 118
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 2.04
SSBOND 2 CYS A 171 CYS A 178 1555 1555 2.06
LINK OG SER A 120 P NXC A 215 1555 1555 1.56
SITE 1 AC1 9 GLY A 41 SER A 42 ASN A 84 SER A 120
SITE 2 AC1 9 GLN A 121 LEU A 182 VAL A 184 HIS A 188
SITE 3 AC1 9 LEU A 189
CRYST1 59.275 89.794 97.526 90.00 90.00 90.00 I 2 2 2 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 0.016871 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011137 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010254 0.00000
TER 1483 GLY A 212
MASTER 365 0 1 11 5 0 3 6 1828 1 29 17
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