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HEADER HYDROLASE 09-JUN-08 3DEA
TITLE GLOMERELLA CINGULATA PETFP-CUTINASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 31-224;
COMPND 5 SYNONYM: CUTIN HYDROLASE;
COMPND 6 EC: 3.1.1.74;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLOMERELLA CINGULATA;
SOURCE 3 ORGANISM_COMMON: ANTHRACNOSE FUNGUS;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: ORIGAMI (DE3);
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET32B_CUTA
KEYWDS CATALYTIC TRIAD, HYDROLASE, SECRETED, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.NYON,D.W.RICE,J.M.BERRISFORD,A.M.HOUNSLOW,A.J.G.MOIR,
AUTHOR 2 H.HUANG,S.NATHAN,N.M.MAHADI,A.B.FARAH DIBA,C.J.CRAVEN
REVDAT 1 18-NOV-08 3DEA 0
JRNL AUTH M.P.NYON,D.W.RICE,J.M.BERRISFORD,A.M.HOUNSLOW,
JRNL AUTH 2 A.J.G.MOIR,H.HUANG,S.NATHAN,N.M.MAHADI,F.D.A.BAKAR,
JRNL AUTH 3 C.J.CRAVEN
JRNL TITL CATALYSIS BY GLOMERELLA CINGULATA CUTINASE
JRNL TITL 2 REQUIRES CONFORMATIONAL CYCLING BETWEEN THE ACTIVE
JRNL TITL 3 AND INACTIVE STATES OF ITS CATALYTIC TRIAD
JRNL REF J.MOL.BIOL. 2008
JRNL REFN ASTM JMOBAK UK ESSN 1089-8638
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 20338
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1101
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1426
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2936
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
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): 0.252
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.151
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.221
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2841 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3862 ; 1.521 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 370 ; 5.991 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;41.916 ;24.144
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 428 ;18.697 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;21.243 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 445 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2147 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1344 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1966 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 177 ; 0.173 ; 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): 30 ; 0.300 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.201 ; 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): 1882 ; 1.031 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2948 ; 1.793 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1079 ; 3.065 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 914 ; 4.690 ; 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 : 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: NULL
REMARK 4
REMARK 4 3DEA COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB047930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-2006
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC VARIMAX
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21478
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 37.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
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 3DCN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 70% (V/V) MPD, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 21.66000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.84500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.16000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.84500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.66000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.16000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 ALA A 24
REMARK 465 MET A 25
REMARK 465 ALA A 26
REMARK 465 ILE A 27
REMARK 465 SER A 28
REMARK 465 ASP A 29
REMARK 465 PRO A 30
REMARK 465 GLN A 31
REMARK 465 THR A 197
REMARK 465 LEU A 198
REMARK 465 PHE A 199
REMARK 465 ILE A 200
REMARK 465 LEU A 201
REMARK 465 PRO A 202
REMARK 465 ALA A 203
REMARK 465 HIS A 204
REMARK 465 ALA B 24
REMARK 465 MET B 25
REMARK 465 ALA B 26
REMARK 465 ILE B 27
REMARK 465 SER B 28
REMARK 465 ASP B 29
REMARK 465 PRO B 30
REMARK 465 GLN B 31
REMARK 465 LEU B 201
REMARK 465 PRO B 202
REMARK 465 ALA B 203
REMARK 465 HIS B 204
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
REMARK 500 OG SER A 136 C10 HZH A 401 1.95
REMARK 500 OG SER B 136 C10 HZH B 402 1.98
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 222 NE - CZ - NH2 ANGL. DEV. = -3.2 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 THR A 58 -24.82 87.32
REMARK 500 SER A 66 -106.26 -125.51
REMARK 500 SER A 136 -114.62 60.53
REMARK 500 VAL A 213 -59.14 -121.91
REMARK 500 SER B 66 -111.25 -117.20
REMARK 500 SER B 136 -108.59 59.01
REMARK 500 VAL B 213 -59.23 -133.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HZH A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HZH B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DCN RELATED DB: PDB
REMARK 900 APO CUTINASE
REMARK 900 RELATED ID: 3DD5 RELATED DB: PDB
REMARK 900 E600-CUTINASE COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS BASED ON REFERENCE 2 IN THE DATABASE,
REMARK 999 CUTI_COLGL.
DBREF 3DEA A 31 224 UNP P11373 CUTI_COLGL 31 224
DBREF 3DEA B 31 224 UNP P11373 CUTI_COLGL 31 224
SEQADV 3DEA ALA A 24 UNP P11373 EXPRESSION TAG
SEQADV 3DEA MET A 25 UNP P11373 EXPRESSION TAG
SEQADV 3DEA ALA A 26 UNP P11373 EXPRESSION TAG
SEQADV 3DEA ILE A 27 UNP P11373 EXPRESSION TAG
SEQADV 3DEA SER A 28 UNP P11373 EXPRESSION TAG
SEQADV 3DEA ASP A 29 UNP P11373 EXPRESSION TAG
SEQADV 3DEA PRO A 30 UNP P11373 EXPRESSION TAG
SEQADV 3DEA ALA B 24 UNP P11373 EXPRESSION TAG
SEQADV 3DEA MET B 25 UNP P11373 EXPRESSION TAG
SEQADV 3DEA ALA B 26 UNP P11373 EXPRESSION TAG
SEQADV 3DEA ILE B 27 UNP P11373 EXPRESSION TAG
SEQADV 3DEA SER B 28 UNP P11373 EXPRESSION TAG
SEQADV 3DEA ASP B 29 UNP P11373 EXPRESSION TAG
SEQADV 3DEA PRO B 30 UNP P11373 EXPRESSION TAG
SEQRES 1 A 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 A 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 A 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 A 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 A 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 A 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 A 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 A 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 A 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 A 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 A 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 A 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 A 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 A 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 A 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 A 201 LEU GLN ALA ARG ILE GLY
SEQRES 1 B 201 ALA MET ALA ILE SER ASP PRO GLN SER SER THR ARG ASN
SEQRES 2 B 201 GLU LEU GLU THR GLY SER SER SER ALA CYS PRO LYS VAL
SEQRES 3 B 201 ILE TYR ILE PHE ALA ARG ALA SER THR GLU PRO GLY ASN
SEQRES 4 B 201 MET GLY ILE SER ALA GLY PRO ILE VAL ALA ASP ALA LEU
SEQRES 5 B 201 GLU ARG ILE TYR GLY ALA ASN ASP VAL TRP VAL GLN GLY
SEQRES 6 B 201 VAL GLY GLY PRO TYR LEU ALA ASP LEU ALA SER ASN PHE
SEQRES 7 B 201 LEU PRO ASP GLY THR SER SER ALA ALA ILE ASN GLU ALA
SEQRES 8 B 201 ARG ARG LEU PHE THR LEU ALA ASN THR LYS CYS PRO ASN
SEQRES 9 B 201 ALA ALA ILE VAL SER GLY GLY TYR SER GLN GLY THR ALA
SEQRES 10 B 201 VAL MET ALA GLY SER ILE SER GLY LEU SER THR THR ILE
SEQRES 11 B 201 LYS ASN GLN ILE LYS GLY VAL VAL LEU PHE GLY TYR THR
SEQRES 12 B 201 LYS ASN LEU GLN ASN LEU GLY ARG ILE PRO ASN PHE GLU
SEQRES 13 B 201 THR SER LYS THR GLU VAL TYR CYS ASP ILE ALA ASP ALA
SEQRES 14 B 201 VAL CYS TYR GLY THR LEU PHE ILE LEU PRO ALA HIS PHE
SEQRES 15 B 201 LEU TYR GLN THR ASP ALA ALA VAL ALA ALA PRO ARG PHE
SEQRES 16 B 201 LEU GLN ALA ARG ILE GLY
HET HZH A 401 16
HET HZH B 402 16
HETNAM HZH 1,1,1-TRIFLUORO-3-[(2-PHENYLETHYL)SULFANYL]PROPAN-2-
HETNAM 2 HZH ONE
HETSYN HZH 3-PHENETHYLTHIO-1,1,1-TRIFLUOROPROPAN-2-ONE, PETFP
FORMUL 3 HZH 2(C11 H11 F3 O S)
FORMUL 5 HOH *146(H2 O)
HELIX 1 1 ASN A 36 GLY A 41 1 6
HELIX 2 2 SER A 66 GLY A 80 1 15
HELIX 3 3 ASP A 96 LEU A 102 5 7
HELIX 4 4 SER A 107 CYS A 125 1 19
HELIX 5 5 SER A 136 GLY A 148 1 13
HELIX 6 6 SER A 150 GLN A 156 1 7
HELIX 7 7 GLU A 179 SER A 181 5 3
HELIX 8 8 ASP A 191 GLY A 196 5 6
HELIX 9 9 TYR A 207 VAL A 213 1 7
HELIX 10 10 VAL A 213 GLY A 224 1 12
HELIX 11 11 ASN B 36 GLY B 41 1 6
HELIX 12 12 SER B 42 CYS B 46 5 5
HELIX 13 13 SER B 66 GLY B 80 1 15
HELIX 14 14 ASP B 96 LEU B 102 5 7
HELIX 15 15 SER B 107 CYS B 125 1 19
HELIX 16 16 SER B 136 GLY B 148 1 13
HELIX 17 17 SER B 150 GLN B 156 1 7
HELIX 18 18 GLU B 179 SER B 181 5 3
HELIX 19 19 ASP B 191 GLY B 196 5 6
HELIX 20 20 TYR B 207 VAL B 213 1 7
HELIX 21 21 VAL B 213 GLY B 224 1 12
SHEET 1 A 5 VAL A 84 GLY A 88 0
SHEET 2 A 5 VAL A 49 ALA A 54 1 N TYR A 51 O TRP A 85
SHEET 3 A 5 ALA A 129 TYR A 135 1 O VAL A 131 N ILE A 50
SHEET 4 A 5 ILE A 157 PHE A 163 1 O LYS A 158 N ILE A 130
SHEET 5 A 5 THR A 183 TYR A 186 1 O TYR A 186 N LEU A 162
SHEET 1 B 5 VAL B 84 GLY B 88 0
SHEET 2 B 5 VAL B 49 ALA B 54 1 N TYR B 51 O TRP B 85
SHEET 3 B 5 ALA B 129 TYR B 135 1 O VAL B 131 N ILE B 50
SHEET 4 B 5 ILE B 157 PHE B 163 1 O LYS B 158 N ILE B 130
SHEET 5 B 5 THR B 183 TYR B 186 1 O TYR B 186 N LEU B 162
SSBOND 1 CYS A 46 CYS A 125 1555 1555 2.02
SSBOND 2 CYS A 187 CYS A 194 1555 1555 2.10
SSBOND 3 CYS B 46 CYS B 125 1555 1555 2.06
SSBOND 4 CYS B 187 CYS B 194 1555 1555 2.10
SITE 1 AC1 6 ALA A 56 SER A 57 ASN A 100 SER A 136
SITE 2 AC1 6 GLN A 137 ILE B 200
SITE 1 AC2 7 ALA B 56 SER B 57 ASN B 100 PHE B 101
SITE 2 AC2 7 SER B 136 GLN B 137 THR B 166
CRYST1 43.320 88.320 123.690 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 0.023085 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011322 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008085 0.00000
TER 1363 GLY A 224
TER 2760 GLY B 224
MASTER 341 0 2 21 10 0 4 6 2936 2 40 32
END |