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HEADER LYASE 04-MAR-15 4YK7
TITLE CRYSTAL STRUCTURE OF S-HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA
TITLE 2 (HIS103LEU)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: (S)-ACETONE-CYANOHYDRIN LYASE,OXYNITRILASE;
COMPND 5 EC: 4.1.2.47;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MANIHOT ESCULENTA;
SOURCE 3 ORGANISM_COMMON: CASSAVA;
SOURCE 4 ORGANISM_TAXID: 3983;
SOURCE 5 GENE: HNL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS S-HYDROXYNITRILE LYASE, HYDROLASE FOLD, HIS103LEU VARIANT, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DADASHIPOUR,S.NAKANO,Y.ASANO
REVDAT 1 13-APR-16 4YK7 0
JRNL AUTH M.DADASHIPOUR,S.NAKANO,Y.ASANO
JRNL TITL CRYSTAL STRUCTURE OF S-HYDROXYNITRILE LYASE FROM MANIHOT
JRNL TITL 2 ESCULENTA (HIS103LEU)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 30495
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) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1631
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2014
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 60
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.36000
REMARK 3 B22 (A**2) : 5.47000
REMARK 3 B33 (A**2) : -3.11000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.364
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.247
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.329
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.869
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.840
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8488 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8140 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11512 ; 1.010 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18760 ; 0.781 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1028 ; 7.306 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 384 ;38.911 ;24.583
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1488 ;18.393 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;17.980 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1288 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9472 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1936 ; 0.009 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 258 B 1 258 16628 0.09 0.05
REMARK 3 2 A 1 258 C 1 258 17061 0.07 0.05
REMARK 3 3 A 1 258 D 1 258 16650 0.09 0.05
REMARK 3 4 B 1 258 C 1 258 16578 0.10 0.05
REMARK 3 5 B 1 258 D 1 258 17119 0.07 0.05
REMARK 3 6 C 1 258 D 1 258 16525 0.10 0.05
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 4YK7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32186
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 45.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : 0.14400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 34.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.10
REMARK 200 R MERGE FOR SHELL (I) : 0.38200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 12.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1M DL-MALEIC ACID, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 43.23450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.60650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.04900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.60650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.23450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.04900
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, 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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 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 CYS A 13 -30.73 85.47
REMARK 500 HIS A 14 -148.55 -91.17
REMARK 500 SER A 80 -114.79 56.19
REMARK 500 TYR A 93 45.29 -144.61
REMARK 500 ARG A 129 -125.66 74.48
REMARK 500 ILE A 210 -42.48 -132.47
REMARK 500 CYS B 13 -31.55 82.71
REMARK 500 HIS B 14 -152.35 -88.04
REMARK 500 SER B 80 -114.16 55.07
REMARK 500 TYR B 93 47.85 -146.49
REMARK 500 ARG B 129 -124.85 75.69
REMARK 500 ILE B 210 -44.33 -131.73
REMARK 500 LYS B 237 70.65 -101.07
REMARK 500 CYS C 13 -31.79 83.93
REMARK 500 HIS C 14 -148.20 -90.61
REMARK 500 SER C 80 -113.66 54.61
REMARK 500 TYR C 93 43.95 -144.19
REMARK 500 ARG C 129 -123.73 69.96
REMARK 500 ILE C 210 -42.64 -132.81
REMARK 500 LYS C 237 70.10 -100.94
REMARK 500 CYS D 13 -31.31 82.27
REMARK 500 HIS D 14 -152.24 -89.54
REMARK 500 SER D 80 -115.23 53.56
REMARK 500 TYR D 93 44.81 -146.42
REMARK 500 ARG D 129 -122.47 72.43
REMARK 500 ILE D 210 -44.84 -132.34
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 TYR B 257 ALA B 258 132.60
REMARK 500 TYR D 257 ALA D 258 132.74
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4YK7 A 1 258 UNP P52705 HNL_MANES 1 258
DBREF 4YK7 B 1 258 UNP P52705 HNL_MANES 1 258
DBREF 4YK7 C 1 258 UNP P52705 HNL_MANES 1 258
DBREF 4YK7 D 1 258 UNP P52705 HNL_MANES 1 258
SEQADV 4YK7 LEU A 103 UNP P52705 HIS 103 ENGINEERED MUTATION
SEQADV 4YK7 LEU B 103 UNP P52705 HIS 103 ENGINEERED MUTATION
SEQADV 4YK7 LEU C 103 UNP P52705 HIS 103 ENGINEERED MUTATION
SEQADV 4YK7 LEU D 103 UNP P52705 HIS 103 ENGINEERED MUTATION
SEQRES 1 A 258 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 A 258 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 A 258 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 A 258 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 A 258 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 A 258 GLU LYS LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 A 258 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 A 258 ARG TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE LEU ASN
SEQRES 9 A 258 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR THR
SEQRES 10 A 258 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 A 258 THR GLU TYR PHE THR PHE THR ASN ILE THR GLY GLU THR
SEQRES 12 A 258 ILE THR THR MET LYS LEU GLY PHE VAL LEU LEU ARG GLU
SEQRES 13 A 258 ASN LEU PHE THR LYS CYS THR ASP GLY GLU TYR GLU LEU
SEQRES 14 A 258 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 A 258 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 A 258 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 A 258 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 A 258 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 A 258 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 A 258 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA
SEQRES 1 B 258 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 B 258 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 B 258 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 B 258 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 B 258 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 B 258 GLU LYS LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 B 258 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 B 258 ARG TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE LEU ASN
SEQRES 9 B 258 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR THR
SEQRES 10 B 258 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 B 258 THR GLU TYR PHE THR PHE THR ASN ILE THR GLY GLU THR
SEQRES 12 B 258 ILE THR THR MET LYS LEU GLY PHE VAL LEU LEU ARG GLU
SEQRES 13 B 258 ASN LEU PHE THR LYS CYS THR ASP GLY GLU TYR GLU LEU
SEQRES 14 B 258 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 B 258 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 B 258 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 B 258 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 B 258 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 B 258 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 B 258 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA
SEQRES 1 C 258 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 C 258 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 C 258 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 C 258 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 C 258 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 C 258 GLU LYS LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 C 258 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 C 258 ARG TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE LEU ASN
SEQRES 9 C 258 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR THR
SEQRES 10 C 258 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 C 258 THR GLU TYR PHE THR PHE THR ASN ILE THR GLY GLU THR
SEQRES 12 C 258 ILE THR THR MET LYS LEU GLY PHE VAL LEU LEU ARG GLU
SEQRES 13 C 258 ASN LEU PHE THR LYS CYS THR ASP GLY GLU TYR GLU LEU
SEQRES 14 C 258 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 C 258 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 C 258 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 C 258 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 C 258 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 C 258 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 C 258 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA
SEQRES 1 D 258 MET VAL THR ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 D 258 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO ALA LEU
SEQRES 3 D 258 GLU ARG ALA GLY HIS LYS VAL THR ALA LEU ASP MET ALA
SEQRES 4 D 258 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 D 258 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 D 258 GLU LYS LEU PRO GLN GLY GLU LYS VAL ILE ILE VAL GLY
SEQRES 7 D 258 GLU SER CYS ALA GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 D 258 ARG TYR VAL ASP LYS ILE ALA ALA GLY VAL PHE LEU ASN
SEQRES 9 D 258 SER LEU LEU PRO ASP THR VAL HIS SER PRO SER TYR THR
SEQRES 10 D 258 VAL GLU LYS LEU LEU GLU SER PHE PRO ASP TRP ARG ASP
SEQRES 11 D 258 THR GLU TYR PHE THR PHE THR ASN ILE THR GLY GLU THR
SEQRES 12 D 258 ILE THR THR MET LYS LEU GLY PHE VAL LEU LEU ARG GLU
SEQRES 13 D 258 ASN LEU PHE THR LYS CYS THR ASP GLY GLU TYR GLU LEU
SEQRES 14 D 258 ALA LYS MET VAL MET ARG LYS GLY SER LEU PHE GLN ASN
SEQRES 15 D 258 VAL LEU ALA GLN ARG PRO LYS PHE THR GLU LYS GLY TYR
SEQRES 16 D 258 GLY SER ILE LYS LYS VAL TYR ILE TRP THR ASP GLN ASP
SEQRES 17 D 258 LYS ILE PHE LEU PRO ASP PHE GLN ARG TRP GLN ILE ALA
SEQRES 18 D 258 ASN TYR LYS PRO ASP LYS VAL TYR GLN VAL GLN GLY GLY
SEQRES 19 D 258 ASP HIS LYS LEU GLN LEU THR LYS THR GLU GLU VAL ALA
SEQRES 20 D 258 HIS ILE LEU GLN GLU VAL ALA ASP ALA TYR ALA
FORMUL 5 HOH *60(H2 O)
HELIX 1 AA1 GLY A 15 HIS A 20 5 6
HELIX 2 AA2 LYS A 21 ALA A 29 1 9
HELIX 3 AA3 GLN A 47 ILE A 51 5 5
HELIX 4 AA4 SER A 53 SER A 58 1 6
HELIX 5 AA5 SER A 58 LEU A 68 1 11
HELIX 6 AA6 ALA A 82 ASP A 91 1 10
HELIX 7 AA7 TYR A 93 ASP A 95 5 3
HELIX 8 AA8 SER A 115 PHE A 125 1 11
HELIX 9 AA9 GLY A 150 ASN A 157 1 8
HELIX 10 AB1 THR A 163 MET A 174 1 12
HELIX 11 AB2 PHE A 180 GLN A 186 1 7
HELIX 12 AB3 GLY A 194 ILE A 198 5 5
HELIX 13 AB4 LEU A 212 TYR A 223 1 12
HELIX 14 AB5 LYS A 237 LYS A 242 1 6
HELIX 15 AB6 LYS A 242 ALA A 258 1 17
HELIX 16 AB7 GLY B 15 HIS B 20 5 6
HELIX 17 AB8 LYS B 21 ALA B 29 1 9
HELIX 18 AB9 GLN B 47 ILE B 51 5 5
HELIX 19 AC1 SER B 53 SER B 58 1 6
HELIX 20 AC2 SER B 58 LEU B 68 1 11
HELIX 21 AC3 ALA B 82 VAL B 94 1 13
HELIX 22 AC4 SER B 115 PHE B 125 1 11
HELIX 23 AC5 GLY B 150 ASN B 157 1 8
HELIX 24 AC6 THR B 163 MET B 174 1 12
HELIX 25 AC7 PHE B 180 GLN B 186 1 7
HELIX 26 AC8 GLY B 194 ILE B 198 5 5
HELIX 27 AC9 LEU B 212 TYR B 223 1 12
HELIX 28 AD1 LYS B 237 LYS B 242 1 6
HELIX 29 AD2 LYS B 242 ALA B 258 1 17
HELIX 30 AD3 GLY C 15 HIS C 20 5 6
HELIX 31 AD4 LYS C 21 ARG C 28 1 8
HELIX 32 AD5 GLN C 47 ILE C 51 5 5
HELIX 33 AD6 SER C 53 SER C 58 1 6
HELIX 34 AD7 SER C 58 LEU C 68 1 11
HELIX 35 AD8 ALA C 82 ASP C 91 1 10
HELIX 36 AD9 TYR C 93 ASP C 95 5 3
HELIX 37 AE1 SER C 115 PHE C 125 1 11
HELIX 38 AE2 GLY C 150 ASN C 157 1 8
HELIX 39 AE3 THR C 163 MET C 174 1 12
HELIX 40 AE4 PHE C 180 GLN C 186 1 7
HELIX 41 AE5 GLY C 194 ILE C 198 5 5
HELIX 42 AE6 LEU C 212 TYR C 223 1 12
HELIX 43 AE7 LYS C 237 LYS C 242 1 6
HELIX 44 AE8 LYS C 242 ALA C 258 1 17
HELIX 45 AE9 GLY D 15 HIS D 20 5 6
HELIX 46 AF1 LYS D 21 ALA D 29 1 9
HELIX 47 AF2 GLN D 47 ILE D 51 5 5
HELIX 48 AF3 SER D 53 SER D 58 1 6
HELIX 49 AF4 SER D 58 LEU D 68 1 11
HELIX 50 AF5 ALA D 82 ASP D 91 1 10
HELIX 51 AF6 TYR D 93 ASP D 95 5 3
HELIX 52 AF7 SER D 115 PHE D 125 1 11
HELIX 53 AF8 GLY D 150 ASN D 157 1 8
HELIX 54 AF9 THR D 163 MET D 174 1 12
HELIX 55 AG1 PHE D 180 GLN D 186 1 7
HELIX 56 AG2 GLY D 194 ILE D 198 5 5
HELIX 57 AG3 LEU D 212 TYR D 223 1 12
HELIX 58 AG4 LYS D 237 LYS D 242 1 6
HELIX 59 AG5 LYS D 242 ALA D 258 1 17
SHEET 1 AA1 6 LYS A 32 LEU A 36 0
SHEET 2 AA1 6 HIS A 5 ILE A 9 1 N LEU A 8 O THR A 34
SHEET 3 AA1 6 VAL A 74 GLU A 79 1 O VAL A 77 N ILE A 9
SHEET 4 AA1 6 ILE A 97 LEU A 103 1 O VAL A 101 N ILE A 76
SHEET 5 AA1 6 LYS A 200 TRP A 204 1 O ILE A 203 N PHE A 102
SHEET 6 AA1 6 LYS A 227 GLN A 230 1 O TYR A 229 N TYR A 202
SHEET 1 AA2 2 GLU A 132 THR A 137 0
SHEET 2 AA2 2 THR A 143 LYS A 148 -1 O ILE A 144 N PHE A 136
SHEET 1 AA3 6 LYS B 32 LEU B 36 0
SHEET 2 AA3 6 HIS B 5 ILE B 9 1 N LEU B 8 O THR B 34
SHEET 3 AA3 6 VAL B 74 GLU B 79 1 O VAL B 77 N ILE B 9
SHEET 4 AA3 6 ILE B 97 LEU B 103 1 O VAL B 101 N ILE B 76
SHEET 5 AA3 6 LYS B 200 TRP B 204 1 O ILE B 203 N PHE B 102
SHEET 6 AA3 6 LYS B 227 GLN B 230 1 O TYR B 229 N TYR B 202
SHEET 1 AA4 3 GLU B 132 THR B 137 0
SHEET 2 AA4 3 THR B 143 LYS B 148 -1 O ILE B 144 N PHE B 136
SHEET 3 AA4 3 GLY B 177 SER B 178 -1 O GLY B 177 N MET B 147
SHEET 1 AA5 6 LYS C 32 LEU C 36 0
SHEET 2 AA5 6 HIS C 5 ILE C 9 1 N LEU C 8 O THR C 34
SHEET 3 AA5 6 VAL C 74 GLU C 79 1 O VAL C 77 N ILE C 9
SHEET 4 AA5 6 ILE C 97 LEU C 103 1 O VAL C 101 N ILE C 76
SHEET 5 AA5 6 LYS C 200 TRP C 204 1 O ILE C 203 N PHE C 102
SHEET 6 AA5 6 LYS C 227 GLN C 230 1 O TYR C 229 N TYR C 202
SHEET 1 AA6 3 GLU C 132 THR C 137 0
SHEET 2 AA6 3 THR C 143 LYS C 148 -1 O ILE C 144 N PHE C 136
SHEET 3 AA6 3 GLY C 177 SER C 178 -1 O GLY C 177 N MET C 147
SHEET 1 AA7 6 LYS D 32 LEU D 36 0
SHEET 2 AA7 6 HIS D 5 ILE D 9 1 N LEU D 8 O THR D 34
SHEET 3 AA7 6 VAL D 74 GLU D 79 1 O VAL D 77 N ILE D 9
SHEET 4 AA7 6 ILE D 97 LEU D 103 1 O VAL D 101 N ILE D 76
SHEET 5 AA7 6 LYS D 200 TRP D 204 1 O ILE D 203 N PHE D 102
SHEET 6 AA7 6 LYS D 227 GLN D 230 1 O TYR D 229 N TYR D 202
SHEET 1 AA8 3 GLU D 132 THR D 137 0
SHEET 2 AA8 3 THR D 143 LYS D 148 -1 O ILE D 144 N PHE D 136
SHEET 3 AA8 3 GLY D 177 SER D 178 -1 O GLY D 177 N MET D 147
CRYST1 86.469 88.098 135.213 90.00 90.00 90.00 P 21 21 21 16
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 0.011565 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007396 0.00000
TER 2073 ALA A 258
TER 4146 ALA B 258
TER 6219 ALA C 258
TER 8292 ALA D 258
MASTER 319 0 0 59 35 0 0 6 8348 4 0 80
END |