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HEADER BIOSYNTHETIC PROTEIN 30-OCT-23 8QZU
TITLE XHPG HYDROLASE MUTANT S98A OF XENORHABDUS HOMINICKII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OXOPYRROLIZIDINACETAMIDE HYDROLASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENORHABDUS HOMINICKII;
SOURCE 3 ORGANISM_TAXID: 351679;
SOURCE 4 STRAIN: ANU1;
SOURCE 5 GENE: XHOM_00310;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBG102
KEYWDS ALPHA/BETA HYDROLASE, POST-NRPS ENZYME, TAILORING ENZYME,
KEYWDS 2 OXOPYRROLIZIDINACETAMIDE HYDROLASE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CALDERARI,A.GRUEZ,K.J.WEISSMAN
REVDAT 1 06-NOV-24 8QZU 0
JRNL AUTH J.EFFERT,M.WESTPHALEN,A.CALDERARI,Y.M.SHI,I.ELAMRI,S.NAJAH,
JRNL AUTH 2 P.GRUN,Y.LI,A.GRUEZ,K.J.WEISSMAN,H.B.BODE
JRNL TITL PYRROLIZWILLINE, A UNIQUE BACTERIAL ALKALOID ASSEMBLED BY A
JRNL TITL 2 NONRIBOSOMAL PEPTIDE SYNTHETASE AND NON-ENZYMATIC
JRNL TITL 3 DIMERIZATION.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 11258 2024
JRNL REFN ESSN 1521-3773
JRNL PMID 39428351
JRNL DOI 10.1002/ANIE.202411258
REMARK 2
REMARK 2 RESOLUTION. 1.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0405
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) : 1.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 74471
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3920
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) : 1.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5183
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.5310
REMARK 3 BIN FREE R VALUE SET COUNT : 273
REMARK 3 BIN FREE R VALUE : 0.5480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.94000
REMARK 3 B22 (A**2) : -0.89000
REMARK 3 B33 (A**2) : 2.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.042
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.042
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.186
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2081 ; 0.012 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 1890 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2822 ; 1.737 ; 1.634
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4364 ; 0.584 ; 1.557
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 269 ; 6.271 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 16 ;10.673 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 326 ;11.716 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 331 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2353 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 393 ; 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): 1071 ; 1.842 ; 1.781
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1070 ; 1.848 ; 1.781
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1338 ; 2.207 ; 3.204
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1339 ; 2.338 ; 3.211
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1010 ; 3.151 ; 2.115
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1011 ; 3.150 ; 2.116
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1484 ; 3.735 ; 3.714
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2381 ; 3.495 ;19.720
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2321 ; 3.435 ;18.530
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3971 ; 9.532 ; 3.000
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 8QZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-23.
REMARK 100 THE DEPOSITION ID IS D_1292134218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.82656
REMARK 200 MONOCHROMATOR : CHANNEL-CUT
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78411
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.180
REMARK 200 RESOLUTION RANGE LOW (A) : 39.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.21
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 1.48000
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: PRISMATIC
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8K, 200MM MAGNESIUM ACETATE,
REMARK 280 100MM SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 24.41500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 24.41500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.27000
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: 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 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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 268
REMARK 465 VAL A 269
REMARK 465 PRO A 270
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 7 NZ
REMARK 480 LYS A 22 CG CD CE NZ
REMARK 480 LYS A 69 CE NZ
REMARK 480 LYS A 74 NZ
REMARK 480 ARG A 128 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 166 CG CD CE NZ
REMARK 480 GLU A 182 CG CD OE1 OE2
REMARK 480 GLU A 186 CD OE1 OE2
REMARK 480 GLU A 202 CD OE1 OE2
REMARK 480 GLN A 238 NE2
REMARK 480 GLU A 255 CD OE1 OE2
REMARK 480 GLU A 267 CB CG CD OE1 OE2
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 98 -114.60 61.46
REMARK 500 ARG A 116 -71.81 -100.15
REMARK 500 ASP A 146 80.46 -161.60
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8QZU A 5 270 UNP A0A2G0QDP0_9GAMM
DBREF2 8QZU A A0A2G0QDP0 1 266
SEQADV 8QZU GLY A 1 UNP A0A2G0QDP EXPRESSION TAG
SEQADV 8QZU PRO A 2 UNP A0A2G0QDP EXPRESSION TAG
SEQADV 8QZU GLY A 3 UNP A0A2G0QDP EXPRESSION TAG
SEQADV 8QZU SER A 4 UNP A0A2G0QDP EXPRESSION TAG
SEQADV 8QZU ALA A 98 UNP A0A2G0QDP SER 94 ENGINEERED MUTATION
SEQRES 1 A 270 GLY PRO GLY SER MET ASN LYS VAL LYS VAL GLY ASP ALA
SEQRES 2 A 270 GLN VAL SER TYR CYS ILE ASP GLY LYS GLY PRO GLY LEU
SEQRES 3 A 270 VAL LEU VAL HIS GLY THR GLY GLY ASP SER GLU THR ASN
SEQRES 4 A 270 TRP GLY HIS LEU MET PRO ALA LEU THR ASN ASP TRP THR
SEQRES 5 A 270 VAL VAL ARG PRO ASP TYR SER GLY SER GLY ILE THR SER
SEQRES 6 A 270 ASP GLU GLY LYS GLN LEU GLU VAL LYS GLU ILE ALA ALA
SEQRES 7 A 270 GLN VAL VAL ALA ALA ALA GLU ALA ALA ARG VAL VAL PRO
SEQRES 8 A 270 PHE ASP LEU VAL GLY PHE ALA LEU GLY SER ALA VAL VAL
SEQRES 9 A 270 ILE ALA ILE ALA ALA ASP TYR PRO HIS LEU VAL ARG ARG
SEQRES 10 A 270 ILE VAL LEU LEU GLY ALA PHE LEU SER SER ARG ASP ILE
SEQRES 11 A 270 ARG GLN LYS THR GLN PHE GLU LEU TRP ARG ASP LEU ILE
SEQRES 12 A 270 ARG THR ASP ARG ALA ALA LEU SER ARG LEU ILE LEU LEU
SEQRES 13 A 270 THR GLY PHE SER PRO ASP PHE ILE SER LYS GLN GLY HIS
SEQRES 14 A 270 ASP GLY VAL SER VAL ILE ILE ASN SER PHE VAL SER GLU
SEQRES 15 A 270 ILE ASN TRP GLU GLY MET ALA ARG GLN VAL GLU LEU ASP
SEQRES 16 A 270 LEU SER ILE ASP VAL SER GLU ALA ALA ARG ARG ILE GLU
SEQRES 17 A 270 LYS PRO THR LEU VAL ILE GLY CYS SER HIS ASP HIS ILE
SEQRES 18 A 270 VAL PRO SER SER GLN ALA LYS SER VAL VAL ARG ILE ILE
SEQRES 19 A 270 ARG GLY ALA GLN TYR THR GLU LEU HIS THR GLY HIS LEU
SEQRES 20 A 270 ALA HIS ILE GLU ASN PRO GLU GLU PHE ILE LEU LEU LEU
SEQRES 21 A 270 ARG SER PHE LEU LEU SER GLU ASP VAL PRO
HET ACT A 301 4
HETNAM ACT ACETATE ION
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 HOH *228(H2 O)
HELIX 1 AA1 SER A 36 GLY A 41 1 6
HELIX 2 AA2 HIS A 42 LEU A 47 5 6
HELIX 3 AA3 VAL A 73 ALA A 87 1 15
HELIX 4 AA4 LEU A 99 ASP A 110 1 12
HELIX 5 AA5 PRO A 112 LEU A 114 5 3
HELIX 6 AA6 ILE A 130 THR A 145 1 16
HELIX 7 AA7 ARG A 147 GLY A 158 1 12
HELIX 8 AA8 PRO A 161 GLN A 167 1 7
HELIX 9 AA9 ASP A 170 GLU A 182 1 13
HELIX 10 AB1 TRP A 185 SER A 197 1 13
HELIX 11 AB2 SER A 201 ARG A 206 1 6
HELIX 12 AB3 SER A 224 ILE A 233 1 10
HELIX 13 AB4 ALA A 248 GLU A 251 1 4
HELIX 14 AB5 PRO A 253 LEU A 265 1 13
SHEET 1 AA1 8 SER A 4 VAL A 10 0
SHEET 2 AA1 8 ALA A 13 ASP A 20 -1 O VAL A 15 N VAL A 8
SHEET 3 AA1 8 THR A 52 PRO A 56 -1 O VAL A 53 N ASP A 20
SHEET 4 AA1 8 GLY A 25 VAL A 29 1 N LEU A 26 O VAL A 54
SHEET 5 AA1 8 ASP A 93 PHE A 97 1 O VAL A 95 N VAL A 29
SHEET 6 AA1 8 ARG A 117 LEU A 121 1 O LEU A 121 N GLY A 96
SHEET 7 AA1 8 THR A 211 CYS A 216 1 O LEU A 212 N LEU A 120
SHEET 8 AA1 8 GLN A 238 LEU A 242 1 O GLN A 238 N VAL A 213
CISPEP 1 VAL A 90 PRO A 91 0 -9.12
CRYST1 48.830 68.540 75.480 90.00 98.11 90.00 C 1 2 1 4
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 0.020479 0.000000 0.002918 0.00000
SCALE2 0.000000 0.014590 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013382 0.00000
TER 2051 GLU A 267
MASTER 286 0 1 14 8 0 0 6 2266 1 4 21
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