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HEADER BIOSYNTHETIC PROTEIN 12-OCT-21 7VO5
TITLE PIMARICIN TYPE I PKS THIOESTERASE DOMAIN (HOLO PIM TE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCNS4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PIMARICIN TYPE I PKS THIOESTERASE DOMAIN (PIM TE);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CHATTANOOGENSIS;
SOURCE 3 ORGANISM_TAXID: 66876;
SOURCE 4 GENE: SCNS4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS THIOESTERASE, TYPE I THIOESTERASE, PIMARICIN, POLYKETIDE SYNTHASE
KEYWDS 2 THIOESTERASE DOMAIN, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.BAI,Y.ZHOU
REVDAT 1 19-JAN-22 7VO5 0
JRNL AUTH Y.ZHOU,W.TAO,Z.QI,J.WEI,T.SHI,Q.KANG,J.ZHENG,Y.ZHAO,L.BAI
JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHTS INTO CHAIN RELEASE OF
JRNL TITL 2 THE POLYENE PKS THIOESTERASE DOMAIN
JRNL REF ACS CATALYSIS V. 12 762 2022
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.1C04991
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19907
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 992
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1479
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.4620
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.5280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 53
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.69000
REMARK 3 B12 (A**2) : 0.11000
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): 0.217
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.150
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2176 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2068 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2963 ; 2.058 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4743 ; 1.150 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 275 ; 7.047 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;30.951 ;22.637
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 329 ;19.716 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;23.208 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 345 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2448 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 493 ; 0.002 ; 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 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7VO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1300025028.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97774
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20938
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 82.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.20
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.8000
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) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : 1.23800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 7VO4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 1.5M SODIUM CITRATE
REMARK 280 TRIBASIC DIHYDRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.23600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.47200
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 34.23600
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.47200
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 95.44900
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 PHE A 235
REMARK 465 GLY A 236
REMARK 465 ILE A 237
REMARK 465 GLY A 238
REMARK 465 THR A 239
REMARK 465 ASP A 240
REMARK 465 THR A 241
REMARK 465 GLY A 284
REMARK 465 ASN A 285
REMARK 465 ALA A 286
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 GLU A 49 CG CD OE1 OE2
REMARK 470 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 175 CG OD1 ND2
REMARK 470 GLU A 176 CG CD OE1 OE2
REMARK 470 THR A 234 OG1 CG2
REMARK 470 GLU A 246 CG CD OE1 OE2
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 ALA A 63 N - CA - C ANGL. DEV. = -24.6 DEGREES
REMARK 500 LEU A 216 CA - CB - CG ANGL. DEV. = 14.1 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 ALA A 63 -152.45 150.13
REMARK 500 PRO A 72 35.64 -68.67
REMARK 500 SER A 138 -123.54 45.85
REMARK 500 SER A 169 -178.83 -170.38
REMARK 500 ASN A 175 60.25 -161.14
REMARK 500 GLU A 176 1.01 46.73
REMARK 500 ALA A 259 155.71 176.08
REMARK 500 ARG A 266 -104.62 -113.97
REMARK 500 SER A 282 36.11 -88.31
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7VO5 A 1 286 UNP F1CLA7 F1CLA7_9ACTN 1736 2021
SEQRES 1 A 286 PHE LEU PRO ALA ALA ALA PRO GLU THR ASP SER LEU GLU
SEQRES 2 A 286 ARG MET PHE LEU ASP ALA LEU GLU SER GLY ARG ILE PRO
SEQRES 3 A 286 GLU ALA GLN ARG MET LEU SER ALA LEU GLY ALA LEU ARG
SEQRES 4 A 286 PRO SER PHE GLU ASN THR ALA GLU LEU GLU ASP LEU PRO
SEQRES 5 A 286 LEU PRO ALA THR LEU ALA GLU GLY PRO GLY ALA PRO ARG
SEQRES 6 A 286 LEU ILE CYS VAL SER THR PRO THR ALA ASN GLY GLY VAL
SEQRES 7 A 286 HIS GLU TYR ALA ARG LEU ALA ALA SER PHE ARG GLY GLU
SEQRES 8 A 286 ARG HIS VAL SER ALA LEU PRO LEU VAL GLY PHE ALA ALA
SEQRES 9 A 286 GLY GLU ARG LEU PRO ALA THR PRO GLU THR ALA VAL ARG
SEQRES 10 A 286 VAL VAL ALA GLU SER THR LEU ARG ALA SER ASP GLY ASN
SEQRES 11 A 286 PRO PHE VAL LEU VAL GLY HIS SER SER ALA GLY ALA PHE
SEQRES 12 A 286 ALA TYR LEU ALA ALA ALA LEU LEU GLU ASN THR TRP GLY
SEQRES 13 A 286 ILE ARG PRO GLU ALA VAL VAL LEU LEU ASP THR LEU SER
SEQRES 14 A 286 LEU ARG HIS GLU GLN ASN GLU THR ILE ASP TYR ALA GLY
SEQRES 15 A 286 LEU MET ARG ARG HIS PHE MET VAL ASP GLU VAL SER PRO
SEQRES 16 A 286 VAL ARG MET THR ASN SER ARG LEU SER ALA MET ALA ARG
SEQRES 17 A 286 TRP MET GLY MET LEU ASN GLN LEU GLU VAL ARG HIS THR
SEQRES 18 A 286 THR VAL PRO VAL LEU ILE ILE ARG ALA ALA LYS GLU THR
SEQRES 19 A 286 PHE GLY ILE GLY THR ASP THR GLY ILE TYR GLY GLU ASP
SEQRES 20 A 286 HIS GLY SER PRO VAL ASP VAL ARG SER VAL ASP ALA ASP
SEQRES 21 A 286 HIS PHE SER MET VAL ARG ASP ASP ALA PRO GLU THR ALA
SEQRES 22 A 286 ARG ILE VAL LYS GLU TRP LEU ASP SER LEU GLY ASN ALA
HET 81E A 301 35
HETNAM 81E (1R,3S,5E,7S,11R,13E,15E,17E,19E,21R,23S,24R,25S)-11,
HETNAM 2 81E 24-DIMETHYL-1,3,7,21,25-PENTAKIS(OXIDANYL)-10,27-
HETNAM 3 81E DIOXABICYCLO[21.3.1]HEPTACOSA-5,13,15,17,19-PENTAEN-9-
HETNAM 4 81E ONE
FORMUL 2 81E C27 H40 O8
FORMUL 3 HOH *53(H2 O)
HELIX 1 AA1 SER A 11 SER A 22 1 12
HELIX 2 AA2 ARG A 24 ARG A 39 1 16
HELIX 3 AA3 ASN A 44 LEU A 48 5 5
HELIX 4 AA4 GLY A 77 GLU A 80 5 4
HELIX 5 AA5 TYR A 81 SER A 87 1 7
HELIX 6 AA6 THR A 111 ASP A 128 1 18
HELIX 7 AA7 SER A 139 GLY A 156 1 18
HELIX 8 AA8 ASP A 179 VAL A 190 1 12
HELIX 9 AA9 THR A 199 LEU A 213 1 15
HELIX 10 AB1 ASN A 214 LEU A 216 5 3
HELIX 11 AB2 GLY A 245 GLY A 249 5 5
HELIX 12 AB3 PHE A 262 ARG A 266 5 5
HELIX 13 AB4 ASP A 268 SER A 282 1 15
SHEET 1 AA1 2 SER A 41 PHE A 42 0
SHEET 2 AA1 2 LEU A 108 PRO A 109 1 O LEU A 108 N PHE A 42
SHEET 1 AA2 7 ALA A 55 ALA A 58 0
SHEET 2 AA2 7 VAL A 94 LEU A 97 -1 O VAL A 94 N LEU A 57
SHEET 3 AA2 7 ARG A 65 VAL A 69 1 N CYS A 68 O SER A 95
SHEET 4 AA2 7 PHE A 132 HIS A 137 1 O VAL A 133 N ILE A 67
SHEET 5 AA2 7 ALA A 161 LEU A 165 1 O VAL A 163 N LEU A 134
SHEET 6 AA2 7 VAL A 225 ALA A 230 1 O LEU A 226 N LEU A 164
SHEET 7 AA2 7 VAL A 252 VAL A 257 1 O ARG A 255 N ARG A 229
CRYST1 95.449 95.449 102.708 90.00 90.00 120.00 P 64 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 0.010477 0.006049 0.000000 0.00000
SCALE2 0.000000 0.012098 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009736 0.00000
TER 2075 LEU A 283
MASTER 327 0 1 13 9 0 0 6 2162 1 35 22
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