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HEADER HYDROLASE 12-FEB-14 4OYL
TITLE HUMICOLA INSOLENS CUTINASE IN COMPLEX WITH MONO-ETHYLPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMICOLA INSOLENS;
SOURCE 3 ORGANISM_TAXID: 34413;
SOURCE 4 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 5062
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.D.DAUTER,A.M.BRZOZOWSKI,J.P.TURKENBURG,K.S.WILSON
REVDAT 1 25-JUN-14 4OYL 0
JRNL AUTH D.KOLD,Z.DAUTER,A.K.LAUSTSEN,A.M.BRZOZOWSKI,J.P.TURKENBURG,
JRNL AUTH 2 A.D.NIELSEN,H.KOLDS,E.PETERSEN,B.SCHITT,L.DE MARIA,
JRNL AUTH 3 K.S.WILSON,A.SVENDSEN,R.WIMMER
JRNL TITL THERMODYNAMIC AND STRUCTURAL INVESTIGATION OF THE SPECIFIC
JRNL TITL 2 SDS BINDING OF HUMICOLA INSOLENS CUTINASE.
JRNL REF PROTEIN SCI. 2014
JRNL REFN ESSN 1469-896X
JRNL PMID 24832484
JRNL DOI 10.1002/PRO.2489
REMARK 2
REMARK 2 RESOLUTION. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 34332
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1801
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2351
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 132
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4211
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65000
REMARK 3 B22 (A**2) : 3.25000
REMARK 3 B33 (A**2) : -0.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.160
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.688
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4318 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4145 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5859 ; 1.683 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9480 ; 0.888 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 570 ; 5.337 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;39.447 ;24.101
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 645 ;15.222 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;16.212 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 658 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5030 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 977 ; 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): 2297 ; 1.499 ; 1.717
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2296 ; 1.494 ; 1.716
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2848 ; 2.372 ; 2.567
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2849 ; 2.372 ; 2.568
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2021 ; 2.381 ; 2.046
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2022 ; 2.380 ; 2.048
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3008 ; 3.777 ; 2.937
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4850 ; 5.870 ;14.528
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4829 ; 5.862 ;14.471
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 4OYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000200259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.89
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SCALEPACK
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36134
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.11500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CONCENTRATION 30 MG ML-1, 0.1
REMARK 280 M TRIS/HCL PH 8.5, 50 MM LYSINE, PEG MME 2K 11% V/V OF 50% W/V
REMARK 280 STOCK SOLUTIONS OR PEG MME 550 16% V/V OF 50 % W/V STOCK
REMARK 280 SOLUTIONS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 33.20000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 1
REMARK 465 LEU A 2
REMARK 465 ALA A 194
REMARK 465 GLN B 1
REMARK 465 LEU B 2
REMARK 465 ALA B 194
REMARK 465 GLN C 1
REMARK 465 LEU C 2
REMARK 465 ALA C 194
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 ARG A 51 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG A 141 CD NE CZ NH1 NH2
REMARK 470 ASN B 15 OD1 ND2
REMARK 470 ARG B 141 CD NE CZ NH1 NH2
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 151 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 26 NE - CZ - NH1 ANGL. DEV. = 3.4 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 37 -92.88 -124.12
REMARK 500 ARG A 73 -5.26 75.24
REMARK 500 MIR A 105 -122.95 56.30
REMARK 500 THR B 37 -96.14 -119.24
REMARK 500 MIR B 105 -120.66 62.89
REMARK 500 ALA C 16 52.55 -141.60
REMARK 500 THR C 29 -0.81 70.65
REMARK 500 THR C 37 -90.63 -119.84
REMARK 500 ARG C 73 -2.47 75.01
REMARK 500 MIR C 105 -120.30 58.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 40YY RELATED DB: PDB
DBREF 4OYL A 1 194 PDB PDB 4OYL 1 194
DBREF 4OYL B 1 194 PDB PDB 4OYL 1 194
DBREF 4OYL C 1 194 PDB PDB 4OYL 1 194
SEQRES 1 A 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 A 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 A 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 A 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 A 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 A 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 A 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 A 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 A 194 MIR GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 A 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 A 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 A 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 A 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 A 194 THR PRO ALA OYL LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 A 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 B 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 B 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 B 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 B 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 B 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 B 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 B 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 B 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 B 194 MIR GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 B 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 B 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 B 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 B 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 B 194 THR PRO ALA OYL LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 B 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
SEQRES 1 C 194 GLN LEU GLY ALA ILE GLU ASN GLY LEU GLU SER GLY SER
SEQRES 2 C 194 ALA ASN ALA CYS PRO ASP ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 C 194 GLY SER THR GLU PRO GLY ASN MET GLY ILE THR VAL GLY
SEQRES 4 C 194 PRO ALA LEU ALA ASN GLY LEU GLU SER HIS ILE ARG ASN
SEQRES 5 C 194 ILE TRP ILE GLN GLY VAL GLY GLY PRO TYR ASP ALA ALA
SEQRES 6 C 194 LEU ALA THR ASN PHE LEU PRO ARG GLY THR SER GLN ALA
SEQRES 7 C 194 ASN ILE ASP GLU GLY LYS ARG LEU PHE ALA LEU ALA ASN
SEQRES 8 C 194 GLN LYS CYS PRO ASN THR PRO VAL VAL ALA GLY GLY TYR
SEQRES 9 C 194 MIR GLN GLY ALA ALA LEU ILE ALA ALA ALA VAL SER GLU
SEQRES 10 C 194 LEU SER GLY ALA VAL LYS GLU GLN VAL LYS GLY VAL ALA
SEQRES 11 C 194 LEU PHE GLY TYR THR GLN ASN LEU GLN ASN ARG GLY GLY
SEQRES 12 C 194 ILE PRO ASN TYR PRO ARG GLU ARG THR LYS VAL PHE CYS
SEQRES 13 C 194 ASN VAL GLY ASP ALA VAL CYS THR GLY THR LEU ILE ILE
SEQRES 14 C 194 THR PRO ALA OYL LEU SER TYR THR ILE GLU ALA ARG GLY
SEQRES 15 C 194 GLU ALA ALA ARG PHE LEU ARG ASP ARG ILE ARG ALA
HET MIR A 105 12
HET OYL A 173 12
HET MIR B 105 12
HET OYL B 173 21
HET MIR C 105 12
HET OYL C 173 12
HETNAM MIR MONOETHYLPHOSPHORYLSERINE
HETNAM OYL 1-ETHYL-L-HISTIDINE
HETSYN MIR O-[(S)-ETHOXY(HYDROXY)PHOSPHORYL]-L-SERINE
FORMUL 1 MIR 3(C5 H12 N O6 P)
FORMUL 1 OYL 3(C8 H13 N3 O2)
FORMUL 4 HOH *294(H2 O)
HELIX 1 AA1 ASN A 7 GLY A 12 1 6
HELIX 2 AA2 THR A 37 ILE A 50 1 14
HELIX 3 AA3 LEU A 66 THR A 75 5 10
HELIX 4 AA4 SER A 76 CYS A 94 1 19
HELIX 5 AA5 MIR A 105 GLU A 117 1 13
HELIX 6 AA6 SER A 119 GLN A 125 1 7
HELIX 7 AA7 PRO A 148 GLU A 150 5 3
HELIX 8 AA8 ASP A 160 GLY A 165 5 6
HELIX 9 AA9 ALA A 172 GLY A 182 1 11
HELIX 10 AB1 GLY A 182 ARG A 193 1 12
HELIX 11 AB2 ASN B 7 GLY B 12 1 6
HELIX 12 AB3 THR B 37 SER B 48 1 12
HELIX 13 AB4 ALA B 65 THR B 75 5 11
HELIX 14 AB5 SER B 76 CYS B 94 1 19
HELIX 15 AB6 MIR B 105 GLU B 117 1 13
HELIX 16 AB7 SER B 119 GLN B 125 1 7
HELIX 17 AB8 PRO B 148 GLU B 150 5 3
HELIX 18 AB9 ASP B 160 GLY B 165 5 6
HELIX 19 AC1 ALA B 172 GLY B 182 1 11
HELIX 20 AC2 GLY B 182 ARG B 193 1 12
HELIX 21 AC3 ASN C 7 GLY C 12 1 6
HELIX 22 AC4 THR C 37 ILE C 50 1 14
HELIX 23 AC5 LEU C 66 THR C 75 5 10
HELIX 24 AC6 SER C 76 CYS C 94 1 19
HELIX 25 AC7 MIR C 105 GLU C 117 1 13
HELIX 26 AC8 SER C 119 GLN C 125 1 7
HELIX 27 AC9 PRO C 148 GLU C 150 5 3
HELIX 28 AD1 ASP C 160 GLY C 165 5 6
HELIX 29 AD2 ALA C 172 GLY C 182 1 11
HELIX 30 AD3 GLY C 182 ARG C 193 1 12
SHEET 1 AA1 5 ILE A 53 GLY A 57 0
SHEET 2 AA1 5 ALA A 20 ALA A 25 1 N LEU A 22 O GLN A 56
SHEET 3 AA1 5 VAL A 99 TYR A 104 1 O VAL A 100 N ILE A 21
SHEET 4 AA1 5 VAL A 126 PHE A 132 1 O PHE A 132 N GLY A 103
SHEET 5 AA1 5 THR A 152 PHE A 155 1 O PHE A 155 N LEU A 131
SHEET 1 AA2 5 ILE B 53 GLY B 57 0
SHEET 2 AA2 5 ALA B 20 ALA B 25 1 N LEU B 22 O TRP B 54
SHEET 3 AA2 5 VAL B 99 TYR B 104 1 O VAL B 100 N ILE B 21
SHEET 4 AA2 5 VAL B 126 PHE B 132 1 O LYS B 127 N VAL B 99
SHEET 5 AA2 5 THR B 152 PHE B 155 1 O PHE B 155 N LEU B 131
SHEET 1 AA3 5 ILE C 53 GLY C 57 0
SHEET 2 AA3 5 ALA C 20 ALA C 25 1 N LEU C 22 O TRP C 54
SHEET 3 AA3 5 VAL C 99 TYR C 104 1 O VAL C 100 N ILE C 21
SHEET 4 AA3 5 VAL C 126 PHE C 132 1 O LYS C 127 N VAL C 99
SHEET 5 AA3 5 THR C 152 PHE C 155 1 O PHE C 155 N LEU C 131
SSBOND 1 CYS A 17 CYS A 94 1555 1555 2.09
SSBOND 2 CYS A 156 CYS A 163 1555 1555 1.98
SSBOND 3 CYS B 17 CYS B 94 1555 1555 2.08
SSBOND 4 CYS B 156 CYS B 163 1555 1555 2.01
SSBOND 5 CYS C 17 CYS C 94 1555 1555 2.08
SSBOND 6 CYS C 156 CYS C 163 1555 1555 2.04
LINK C TYR A 104 N MIR A 105 1555 1555 1.34
LINK C MIR A 105 N GLN A 106 1555 1555 1.33
LINK C ALA A 172 N OYL A 173 1555 1555 1.36
LINK C OYL A 173 N LEU A 174 1555 1555 1.36
LINK C TYR B 104 N MIR B 105 1555 1555 1.33
LINK C MIR B 105 N GLN B 106 1555 1555 1.33
LINK C ALA B 172 N OYL B 173 1555 1555 1.36
LINK C OYL B 173 N LEU B 174 1555 1555 1.34
LINK C TYR C 104 N MIR C 105 1555 1555 1.34
LINK C MIR C 105 N GLN C 106 1555 1555 1.34
LINK C ALA C 172 N OYL C 173 1555 1555 1.34
LINK C OYL C 173 N LEU C 174 1555 1555 1.37
CRYST1 71.630 66.400 71.980 90.00 119.30 90.00 P 1 21 1 6
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 0.013961 0.000000 0.007834 0.00000
SCALE2 0.000000 0.015060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015931 0.00000
TER 1399 ARG A 193
TER 2817 ARG B 193
TER 4238 ARG C 193
MASTER 318 0 6 30 15 0 0 6 4505 3 105 45
END |