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HEADER HYDROLASE 01-NOV-19 6L7M
TITLE CHARACTERIZATION AND STRUCTURAL ANALYSIS OF A THERMOSTABLE
TITLE 2 ZEARALENONE-DEGRADING ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ZHDF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MONOSPORASCUS SP. MG133;
SOURCE 3 ORGANISM_TAXID: 2211645;
SOURCE 4 GENE: DL767_010056;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 042;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 216592
KEYWDS MYCOTOXIN, ZEN-DEGRADING ENZYME ZHDF, THERMOSTABLITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.H.WEI,G.MENG
REVDAT 1 04-NOV-20 6L7M 0
JRNL AUTH X.H.WEI,G.MENG
JRNL TITL CHARACTERIZATION AND STRUCTURAL ANALYSIS OF A THERMOSTABLE
JRNL TITL 2 ZEARALENONE-DEGRADING ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC CCP4 7.0.077
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 57634
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NONE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.162
REMARK 3 FREE R VALUE TEST SET COUNT : 2975
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8368
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 579
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06700
REMARK 3 B22 (A**2) : 0.93700
REMARK 3 B33 (A**2) : -0.87000
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): 0.245
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.272
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.001
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 6L7M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-19.
REMARK 100 THE DEPOSITION ID IS D_1300014223.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : 0.20000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.00
REMARK 200 R MERGE FOR SHELL (I) : 0.73300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.900
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: 5XO6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 AND 0.2 M POTASSIUM
REMARK 280 FLUORIDE, PH 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 281K
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 48.00500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.09500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.16000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.09500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.00500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.16000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 GLY A 132 C PRO A 133 N 0.114
REMARK 500 PRO A 133 N PRO A 133 CA 0.232
REMARK 500 PRO A 158 N PRO A 158 CA 0.190
REMARK 500 TYR A 191 C PRO A 192 N 0.119
REMARK 500 PRO A 192 N PRO A 192 CA 0.238
REMARK 500 ILE B 29 C PRO B 30 N 0.118
REMARK 500 PRO B 30 N PRO B 30 CA 0.198
REMARK 500 PRO C 192 N PRO C 192 CA 0.234
REMARK 500 LEU C 195 C PRO C 196 N 0.147
REMARK 500 MET D 157 C PRO D 158 N 0.118
REMARK 500 PRO D 158 N PRO D 158 CA 0.186
REMARK 500 PRO D 158 C PRO D 158 O -0.226
REMARK 500 PRO D 192 N PRO D 192 CA 0.240
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 PRO A 133 C - N - CA ANGL. DEV. = 20.8 DEGREES
REMARK 500 PRO A 133 CA - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO A 158 C - N - CA ANGL. DEV. = 20.3 DEGREES
REMARK 500 PRO A 158 CA - N - CD ANGL. DEV. = -17.1 DEGREES
REMARK 500 PRO A 158 N - CD - CG ANGL. DEV. = 12.9 DEGREES
REMARK 500 PRO A 192 C - N - CA ANGL. DEV. = 18.3 DEGREES
REMARK 500 PRO A 192 CA - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 PRO B 30 C - N - CA ANGL. DEV. = 17.0 DEGREES
REMARK 500 HIS B 134 C - N - CA ANGL. DEV. = 15.6 DEGREES
REMARK 500 TYR B 191 O - C - N ANGL. DEV. = -11.8 DEGREES
REMARK 500 PRO C 192 C - N - CA ANGL. DEV. = 17.0 DEGREES
REMARK 500 PRO C 192 CA - N - CD ANGL. DEV. = -11.3 DEGREES
REMARK 500 HIS C 193 CB - CA - C ANGL. DEV. = -14.1 DEGREES
REMARK 500 PRO C 196 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO D 158 C - N - CA ANGL. DEV. = 22.0 DEGREES
REMARK 500 PRO D 158 CA - N - CD ANGL. DEV. = -30.3 DEGREES
REMARK 500 PRO D 158 N - CD - CG ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO D 192 C - N - CA ANGL. DEV. = 15.6 DEGREES
REMARK 500 PRO D 192 CA - N - CD ANGL. DEV. = -9.9 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 SER A 62 -126.15 51.66
REMARK 500 SER A 102 -124.69 59.16
REMARK 500 HIS A 134 -29.33 -141.14
REMARK 500 PHE A 135 -62.04 -139.81
REMARK 500 LEU A 138 106.72 -57.72
REMARK 500 PHE A 162 -39.76 -140.81
REMARK 500 HIS A 164 52.35 -92.45
REMARK 500 MET A 244 -95.66 -129.05
REMARK 500 SER B 62 -126.27 52.03
REMARK 500 SER B 102 -123.94 59.20
REMARK 500 PRO B 133 36.88 -94.53
REMARK 500 HIS B 134 -169.16 -119.82
REMARK 500 HIS B 164 62.45 -103.68
REMARK 500 MET B 244 -96.84 -128.01
REMARK 500 SER C 62 -126.74 52.09
REMARK 500 SER C 102 -123.46 58.53
REMARK 500 GLN C 137 75.64 -153.91
REMARK 500 MET C 244 -91.21 -131.63
REMARK 500 SER D 62 -126.80 51.64
REMARK 500 SER D 102 -124.37 59.32
REMARK 500 PRO D 158 -53.28 -26.30
REMARK 500 MET D 244 -96.21 -128.89
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 B 454 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C 425 DISTANCE = 6.17 ANGSTROMS
DBREF1 6L7M A 1 267 UNP A0A4Q4UBE4_9PEZI
DBREF2 6L7M A A0A4Q4UBE4 1 267
DBREF1 6L7M B 1 267 UNP A0A4Q4UBE4_9PEZI
DBREF2 6L7M B A0A4Q4UBE4 1 267
DBREF1 6L7M C 1 267 UNP A0A4Q4UBE4_9PEZI
DBREF2 6L7M C A0A4Q4UBE4 1 267
DBREF1 6L7M D 1 267 UNP A0A4Q4UBE4_9PEZI
DBREF2 6L7M D A0A4Q4UBE4 1 267
SEQRES 1 A 267 MET ARG THR ARG SER THR LEU THR ASP LYS ASN GLY ILE
SEQRES 2 A 267 THR TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 A 267 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS HIS MET MET
SEQRES 4 A 267 ASP LYS PRO MET SER MET ILE ALA GLY MET GLY PHE THR
SEQRES 5 A 267 CYS THR THR PHE ASP MET PRO GLY PHE SER ARG SER TRP
SEQRES 6 A 267 ASP ALA PRO PRO GLU THR TYR GLN ASP VAL THR ALA GLN
SEQRES 7 A 267 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP GLU LEU
SEQRES 8 A 267 HIS ILE ASP TYR ALA THR PHE TRP GLY CYS SER SER GLY
SEQRES 9 A 267 GLY ALA THR VAL LEU ALA LEU ALA ALA ASP TYR PRO GLU
SEQRES 10 A 267 ARG MET ARG ASN GLY LEU PRO HIS GLU VAL PRO THR ALA
SEQRES 11 A 267 ALA GLY PRO HIS PHE GLY GLN LEU LEU LYS LEU ALA GLU
SEQRES 12 A 267 MET GLU ASP GLU ALA ILE VAL LYS MET LEU GLY GLU GLU
SEQRES 13 A 267 MET PRO LYS LEU GLY PHE GLY HIS ASP PHE THR ALA TRP
SEQRES 14 A 267 HIS GLU LEU GLY GLU GLU ALA HIS ALA ARG MET ARG LYS
SEQRES 15 A 267 ASN TYR PRO ARG TRP ALA ARG GLY TYR PRO HIS THR LEU
SEQRES 16 A 267 PRO LEU SER SER PRO THR GLY LYS GLU ASP LEU ILE LYS
SEQRES 17 A 267 ARG PRO LEU ASP TRP THR VAL GLY GLY ASP THR PRO THR
SEQRES 18 A 267 ARG MET PHE PHE ASP ASN ILE VAL THR ALA SER LYS ALA
SEQRES 19 A 267 GLY ILE PRO ILE ALA THR LEU PRO GLY MET HIS PHE PRO
SEQRES 20 A 267 TYR VAL SER HIS PRO GLU VAL LEU VAL LYS HIS ILE VAL
SEQRES 21 A 267 ASP THR THR ARG LYS TYR LEU
SEQRES 1 B 267 MET ARG THR ARG SER THR LEU THR ASP LYS ASN GLY ILE
SEQRES 2 B 267 THR TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 B 267 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS HIS MET MET
SEQRES 4 B 267 ASP LYS PRO MET SER MET ILE ALA GLY MET GLY PHE THR
SEQRES 5 B 267 CYS THR THR PHE ASP MET PRO GLY PHE SER ARG SER TRP
SEQRES 6 B 267 ASP ALA PRO PRO GLU THR TYR GLN ASP VAL THR ALA GLN
SEQRES 7 B 267 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP GLU LEU
SEQRES 8 B 267 HIS ILE ASP TYR ALA THR PHE TRP GLY CYS SER SER GLY
SEQRES 9 B 267 GLY ALA THR VAL LEU ALA LEU ALA ALA ASP TYR PRO GLU
SEQRES 10 B 267 ARG MET ARG ASN GLY LEU PRO HIS GLU VAL PRO THR ALA
SEQRES 11 B 267 ALA GLY PRO HIS PHE GLY GLN LEU LEU LYS LEU ALA GLU
SEQRES 12 B 267 MET GLU ASP GLU ALA ILE VAL LYS MET LEU GLY GLU GLU
SEQRES 13 B 267 MET PRO LYS LEU GLY PHE GLY HIS ASP PHE THR ALA TRP
SEQRES 14 B 267 HIS GLU LEU GLY GLU GLU ALA HIS ALA ARG MET ARG LYS
SEQRES 15 B 267 ASN TYR PRO ARG TRP ALA ARG GLY TYR PRO HIS THR LEU
SEQRES 16 B 267 PRO LEU SER SER PRO THR GLY LYS GLU ASP LEU ILE LYS
SEQRES 17 B 267 ARG PRO LEU ASP TRP THR VAL GLY GLY ASP THR PRO THR
SEQRES 18 B 267 ARG MET PHE PHE ASP ASN ILE VAL THR ALA SER LYS ALA
SEQRES 19 B 267 GLY ILE PRO ILE ALA THR LEU PRO GLY MET HIS PHE PRO
SEQRES 20 B 267 TYR VAL SER HIS PRO GLU VAL LEU VAL LYS HIS ILE VAL
SEQRES 21 B 267 ASP THR THR ARG LYS TYR LEU
SEQRES 1 C 267 MET ARG THR ARG SER THR LEU THR ASP LYS ASN GLY ILE
SEQRES 2 C 267 THR TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 C 267 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS HIS MET MET
SEQRES 4 C 267 ASP LYS PRO MET SER MET ILE ALA GLY MET GLY PHE THR
SEQRES 5 C 267 CYS THR THR PHE ASP MET PRO GLY PHE SER ARG SER TRP
SEQRES 6 C 267 ASP ALA PRO PRO GLU THR TYR GLN ASP VAL THR ALA GLN
SEQRES 7 C 267 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP GLU LEU
SEQRES 8 C 267 HIS ILE ASP TYR ALA THR PHE TRP GLY CYS SER SER GLY
SEQRES 9 C 267 GLY ALA THR VAL LEU ALA LEU ALA ALA ASP TYR PRO GLU
SEQRES 10 C 267 ARG MET ARG ASN GLY LEU PRO HIS GLU VAL PRO THR ALA
SEQRES 11 C 267 ALA GLY PRO HIS PHE GLY GLN LEU LEU LYS LEU ALA GLU
SEQRES 12 C 267 MET GLU ASP GLU ALA ILE VAL LYS MET LEU GLY GLU GLU
SEQRES 13 C 267 MET PRO LYS LEU GLY PHE GLY HIS ASP PHE THR ALA TRP
SEQRES 14 C 267 HIS GLU LEU GLY GLU GLU ALA HIS ALA ARG MET ARG LYS
SEQRES 15 C 267 ASN TYR PRO ARG TRP ALA ARG GLY TYR PRO HIS THR LEU
SEQRES 16 C 267 PRO LEU SER SER PRO THR GLY LYS GLU ASP LEU ILE LYS
SEQRES 17 C 267 ARG PRO LEU ASP TRP THR VAL GLY GLY ASP THR PRO THR
SEQRES 18 C 267 ARG MET PHE PHE ASP ASN ILE VAL THR ALA SER LYS ALA
SEQRES 19 C 267 GLY ILE PRO ILE ALA THR LEU PRO GLY MET HIS PHE PRO
SEQRES 20 C 267 TYR VAL SER HIS PRO GLU VAL LEU VAL LYS HIS ILE VAL
SEQRES 21 C 267 ASP THR THR ARG LYS TYR LEU
SEQRES 1 D 267 MET ARG THR ARG SER THR LEU THR ASP LYS ASN GLY ILE
SEQRES 2 D 267 THR TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 D 267 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS HIS MET MET
SEQRES 4 D 267 ASP LYS PRO MET SER MET ILE ALA GLY MET GLY PHE THR
SEQRES 5 D 267 CYS THR THR PHE ASP MET PRO GLY PHE SER ARG SER TRP
SEQRES 6 D 267 ASP ALA PRO PRO GLU THR TYR GLN ASP VAL THR ALA GLN
SEQRES 7 D 267 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP GLU LEU
SEQRES 8 D 267 HIS ILE ASP TYR ALA THR PHE TRP GLY CYS SER SER GLY
SEQRES 9 D 267 GLY ALA THR VAL LEU ALA LEU ALA ALA ASP TYR PRO GLU
SEQRES 10 D 267 ARG MET ARG ASN GLY LEU PRO HIS GLU VAL PRO THR ALA
SEQRES 11 D 267 ALA GLY PRO HIS PHE GLY GLN LEU LEU LYS LEU ALA GLU
SEQRES 12 D 267 MET GLU ASP GLU ALA ILE VAL LYS MET LEU GLY GLU GLU
SEQRES 13 D 267 MET PRO LYS LEU GLY PHE GLY HIS ASP PHE THR ALA TRP
SEQRES 14 D 267 HIS GLU LEU GLY GLU GLU ALA HIS ALA ARG MET ARG LYS
SEQRES 15 D 267 ASN TYR PRO ARG TRP ALA ARG GLY TYR PRO HIS THR LEU
SEQRES 16 D 267 PRO LEU SER SER PRO THR GLY LYS GLU ASP LEU ILE LYS
SEQRES 17 D 267 ARG PRO LEU ASP TRP THR VAL GLY GLY ASP THR PRO THR
SEQRES 18 D 267 ARG MET PHE PHE ASP ASN ILE VAL THR ALA SER LYS ALA
SEQRES 19 D 267 GLY ILE PRO ILE ALA THR LEU PRO GLY MET HIS PHE PRO
SEQRES 20 D 267 TYR VAL SER HIS PRO GLU VAL LEU VAL LYS HIS ILE VAL
SEQRES 21 D 267 ASP THR THR ARG LYS TYR LEU
FORMUL 5 HOH *579(H2 O)
HELIX 1 AA1 GLU A 35 MET A 38 5 4
HELIX 2 AA2 MET A 39 GLY A 48 1 10
HELIX 3 AA3 PHE A 61 TRP A 65 5 5
HELIX 4 AA4 PRO A 68 TYR A 72 5 5
HELIX 5 AA5 THR A 76 LEU A 91 1 16
HELIX 6 AA6 SER A 102 TYR A 115 1 14
HELIX 7 AA7 LEU A 138 GLU A 145 5 8
HELIX 8 AA8 ASP A 146 MET A 157 1 12
HELIX 9 AA9 MET A 157 PHE A 162 1 6
HELIX 10 AB1 ASP A 165 LEU A 172 1 8
HELIX 11 AB2 GLY A 173 TYR A 191 1 19
HELIX 12 AB3 LEU A 195 SER A 199 5 5
HELIX 13 AB4 GLY A 202 LYS A 208 1 7
HELIX 14 AB5 PHE A 224 GLY A 235 1 12
HELIX 15 AB6 PHE A 246 HIS A 251 1 6
HELIX 16 AB7 HIS A 251 LYS A 265 1 15
HELIX 17 AB8 GLU B 35 MET B 38 5 4
HELIX 18 AB9 MET B 39 GLY B 48 1 10
HELIX 19 AC1 PHE B 61 TRP B 65 5 5
HELIX 20 AC2 PRO B 68 TYR B 72 5 5
HELIX 21 AC3 THR B 76 LEU B 91 1 16
HELIX 22 AC4 SER B 102 TYR B 115 1 14
HELIX 23 AC5 LEU B 138 GLU B 145 5 8
HELIX 24 AC6 ASP B 146 MET B 157 1 12
HELIX 25 AC7 MET B 157 PHE B 162 1 6
HELIX 26 AC8 ASP B 165 LEU B 172 1 8
HELIX 27 AC9 GLY B 173 TYR B 191 1 19
HELIX 28 AD1 LEU B 195 SER B 199 5 5
HELIX 29 AD2 GLY B 202 ILE B 207 1 6
HELIX 30 AD3 PHE B 224 GLY B 235 1 12
HELIX 31 AD4 PHE B 246 HIS B 251 1 6
HELIX 32 AD5 HIS B 251 LYS B 265 1 15
HELIX 33 AD6 GLU C 35 MET C 38 5 4
HELIX 34 AD7 MET C 39 GLY C 48 1 10
HELIX 35 AD8 PHE C 61 TRP C 65 5 5
HELIX 36 AD9 PRO C 68 TYR C 72 5 5
HELIX 37 AE1 THR C 76 LEU C 91 1 16
HELIX 38 AE2 SER C 102 TYR C 115 1 14
HELIX 39 AE3 LEU C 138 GLU C 145 5 8
HELIX 40 AE4 ASP C 146 MET C 157 1 12
HELIX 41 AE5 MET C 157 PHE C 162 1 6
HELIX 42 AE6 ASP C 165 LEU C 172 1 8
HELIX 43 AE7 GLY C 173 TYR C 191 1 19
HELIX 44 AE8 LEU C 195 SER C 199 5 5
HELIX 45 AE9 GLY C 202 ILE C 207 1 6
HELIX 46 AF1 PHE C 224 GLY C 235 1 12
HELIX 47 AF2 PHE C 246 HIS C 251 1 6
HELIX 48 AF3 HIS C 251 LYS C 265 1 15
HELIX 49 AF4 GLU D 35 MET D 38 5 4
HELIX 50 AF5 MET D 39 GLY D 48 1 10
HELIX 51 AF6 PHE D 61 TRP D 65 5 5
HELIX 52 AF7 PRO D 68 TYR D 72 5 5
HELIX 53 AF8 THR D 76 LEU D 91 1 16
HELIX 54 AF9 SER D 102 TYR D 115 1 14
HELIX 55 AG1 LEU D 138 GLU D 145 5 8
HELIX 56 AG2 ASP D 146 MET D 157 1 12
HELIX 57 AG3 MET D 157 GLY D 163 1 7
HELIX 58 AG4 ASP D 165 GLU D 171 1 7
HELIX 59 AG5 GLY D 173 TYR D 191 1 19
HELIX 60 AG6 LEU D 195 SER D 199 5 5
HELIX 61 AG7 GLY D 202 LYS D 208 1 7
HELIX 62 AG8 PHE D 224 GLY D 235 1 12
HELIX 63 AG9 PHE D 246 HIS D 251 1 6
HELIX 64 AH1 HIS D 251 LYS D 265 1 15
SHEET 1 AA1 6 THR A 3 THR A 8 0
SHEET 2 AA1 6 THR A 14 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA1 6 THR A 52 PHE A 56 -1 O CYS A 53 N GLU A 20
SHEET 4 AA1 6 HIS A 25 ILE A 29 1 N VAL A 26 O THR A 54
SHEET 5 AA1 6 ALA A 96 CYS A 101 1 O THR A 97 N VAL A 27
SHEET 6 AA1 6 MET A 119 HIS A 125 1 O LEU A 123 N PHE A 98
SHEET 1 AA2 2 TRP A 213 GLY A 216 0
SHEET 2 AA2 2 ILE A 238 LEU A 241 1 O LEU A 241 N VAL A 215
SHEET 1 AA3 6 THR B 3 THR B 8 0
SHEET 2 AA3 6 THR B 14 GLU B 20 -1 O GLN B 19 N THR B 3
SHEET 3 AA3 6 THR B 52 PHE B 56 -1 O CYS B 53 N GLU B 20
SHEET 4 AA3 6 HIS B 25 ILE B 29 1 N VAL B 26 O THR B 54
SHEET 5 AA3 6 ALA B 96 CYS B 101 1 O THR B 97 N VAL B 27
SHEET 6 AA3 6 MET B 119 HIS B 125 1 O LEU B 123 N PHE B 98
SHEET 1 AA4 2 TRP B 213 GLY B 216 0
SHEET 2 AA4 2 ILE B 238 LEU B 241 1 O ALA B 239 N TRP B 213
SHEET 1 AA5 6 THR C 3 THR C 8 0
SHEET 2 AA5 6 THR C 14 GLU C 20 -1 O GLN C 19 N THR C 3
SHEET 3 AA5 6 THR C 52 PHE C 56 -1 O CYS C 53 N GLU C 20
SHEET 4 AA5 6 HIS C 25 ILE C 29 1 N VAL C 26 O THR C 54
SHEET 5 AA5 6 ALA C 96 CYS C 101 1 O THR C 97 N VAL C 27
SHEET 6 AA5 6 MET C 119 HIS C 125 1 O LEU C 123 N PHE C 98
SHEET 1 AA6 2 TRP C 213 GLY C 216 0
SHEET 2 AA6 2 ILE C 238 LEU C 241 1 O LEU C 241 N VAL C 215
SHEET 1 AA7 6 ARG D 2 THR D 8 0
SHEET 2 AA7 6 THR D 14 GLU D 20 -1 O GLN D 19 N THR D 3
SHEET 3 AA7 6 THR D 52 PHE D 56 -1 O CYS D 53 N GLU D 20
SHEET 4 AA7 6 HIS D 25 ILE D 29 1 N LEU D 28 O THR D 54
SHEET 5 AA7 6 ALA D 96 CYS D 101 1 O THR D 97 N VAL D 27
SHEET 6 AA7 6 MET D 119 HIS D 125 1 O LEU D 123 N PHE D 98
SHEET 1 AA8 2 TRP D 213 GLY D 216 0
SHEET 2 AA8 2 ILE D 238 LEU D 241 1 O ALA D 239 N TRP D 213
CRYST1 96.010 116.320 130.190 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 0.010416 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008597 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007681 0.00000
TER 2093 LEU A 267
TER 4186 LEU B 267
TER 6279 LEU C 267
TER 8372 LEU D 267
MASTER 309 0 0 64 32 0 0 6 8947 4 0 84
END |