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HEADER HYDROLASE 14-DEC-23 8VCE
TITLE CRYSTAL STRUCTURE OF PLANT CARBOXYLESTERASE 20
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE CARBOXYLESTERASE 120;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATCXE20;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: CXE20, AT5G62180, MMI9.26;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE 20, CXE20, STRIGOLACTONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PALAYAM,N.SHABEK
REVDAT 1 07-AUG-24 8VCE 0
JRNL AUTH M.PALAYAM
JRNL TITL STRUCTURAL INSIGHTS INTO STRIGOLACTONE CATABOLISM BY
JRNL TITL 2 CARBOXYLESTERASES REVEAL A CONSERVED ALLOSTERIC REGULATION
JRNL REF NAT COMMUN 2024
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-024-50928-3
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 55318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.630
REMARK 3 FREE R VALUE TEST SET COUNT : 2007
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.0000 - 4.4600 1.00 4042 154 0.1586 0.1586
REMARK 3 2 4.4600 - 3.5400 1.00 3896 149 0.1464 0.1533
REMARK 3 3 3.5400 - 3.0900 1.00 3858 143 0.1654 0.2246
REMARK 3 4 3.0900 - 2.8100 1.00 3819 150 0.1734 0.2006
REMARK 3 5 2.8100 - 2.6100 1.00 3820 143 0.1696 0.2056
REMARK 3 6 2.6100 - 2.4500 1.00 3812 142 0.1650 0.1877
REMARK 3 7 2.4500 - 2.3300 1.00 3789 139 0.1573 0.1810
REMARK 3 8 2.3300 - 2.2300 1.00 3776 138 0.1917 0.2254
REMARK 3 9 2.2300 - 2.1400 1.00 3817 144 0.1737 0.2227
REMARK 3 10 2.1400 - 2.0700 1.00 3752 149 0.1751 0.2405
REMARK 3 11 2.0700 - 2.0000 1.00 3751 133 0.1805 0.2173
REMARK 3 12 2.0000 - 1.9500 1.00 3796 134 0.1923 0.2727
REMARK 3 13 1.9500 - 1.9000 1.00 3762 154 0.2376 0.2922
REMARK 3 14 1.9000 - 1.8500 0.96 3621 135 0.2358 0.2739
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 5096
REMARK 3 ANGLE : 1.027 6936
REMARK 3 CHIRALITY : 0.060 770
REMARK 3 PLANARITY : 0.009 902
REMARK 3 DIHEDRAL : 5.641 698
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8VCE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1000279918.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : 55388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03500
REMARK 200 FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.23000
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 1.19.2_4158
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% W/V PEG8000, 20% V/V ETHYLENE
REMARK 280 GLYCOL, 0.1M IMIDAZOLE, 0.03M SODIUM NITRATE, 0.03M DISODIUM
REMARK 280 HYDROGEN PHOSPHATE AND 0.03M AMMONIUM SULFATE, VAPOR DIFFUSION,
REMARK 280 HANGING 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 33.29350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.15650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.85050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.15650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.29350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.85050
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
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 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 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 PRO A 4
REMARK 465 SER A 5
REMARK 465 ASN A 71
REMARK 465 GLU A 72
REMARK 465 GLY A 73
REMARK 465 ASN A 74
REMARK 465 VAL A 75
REMARK 465 SER A 76
REMARK 465 SER A 77
REMARK 465 LEU A 327
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 PRO B 4
REMARK 465 ASP B 21
REMARK 465 GLY B 22
REMARK 465 ASN B 71
REMARK 465 GLU B 72
REMARK 465 GLY B 73
REMARK 465 ASN B 74
REMARK 465 VAL B 75
REMARK 465 SER B 76
REMARK 465 SER B 77
REMARK 465 LEU B 327
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 ASP A 21 14.73 -159.33
REMARK 500 CYS A 94 152.74 79.61
REMARK 500 SER A 166 -121.30 57.75
REMARK 500 ASP A 237 -169.83 -110.58
REMARK 500 CYS B 94 151.80 76.77
REMARK 500 SER B 166 -117.81 56.93
REMARK 500 CYS B 219 64.09 -150.02
REMARK 500 CYS B 219 67.85 -151.81
REMARK 500 ASP B 239 45.53 -86.61
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8VCE A 1 327 UNP Q9LVB8 CXE20_ARATH 1 327
DBREF 8VCE B 1 327 UNP Q9LVB8 CXE20_ARATH 1 327
SEQRES 1 A 327 MET SER GLU PRO SER PRO ILE ALA ASP PRO TYR ALA TYR
SEQRES 2 A 327 LEU ASN ILE VAL ASN ASN PRO ASP GLY SER ILE THR ARG
SEQRES 3 A 327 ASP LEU SER ASN PHE PRO CYS THR ALA ALA THR PRO ASP
SEQRES 4 A 327 PRO SER PRO LEU ASN PRO ALA VAL SER LYS ASP LEU PRO
SEQRES 5 A 327 VAL ASN GLN LEU LYS SER THR TRP LEU ARG LEU TYR LEU
SEQRES 6 A 327 PRO SER SER ALA VAL ASN GLU GLY ASN VAL SER SER GLN
SEQRES 7 A 327 LYS LEU PRO ILE VAL VAL TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 A 327 ILE LEU CYS SER VAL ASP MET GLN LEU PHE HIS ASP PHE
SEQRES 9 A 327 CYS SER GLU VAL ALA ARG ASP LEU ASN ALA ILE VAL VAL
SEQRES 10 A 327 SER PRO SER TYR ARG LEU ALA PRO GLU HIS ARG LEU PRO
SEQRES 11 A 327 ALA ALA TYR ASP ASP GLY VAL GLU ALA LEU ASP TRP ILE
SEQRES 12 A 327 LYS THR SER ASP ASP GLU TRP ILE LYS SER HIS ALA ASP
SEQRES 13 A 327 PHE SER ASN VAL PHE LEU MET GLY THR SER ALA GLY GLY
SEQRES 14 A 327 ASN LEU ALA TYR ASN VAL GLY LEU ARG SER VAL ASP SER
SEQRES 15 A 327 VAL SER ASP LEU SER PRO LEU GLN ILE ARG GLY LEU ILE
SEQRES 16 A 327 LEU HIS HIS PRO PHE PHE GLY GLY GLU GLU ARG SER GLU
SEQRES 17 A 327 SER GLU ILE ARG LEU MET ASN ASP GLN VAL CYS PRO PRO
SEQRES 18 A 327 ILE VAL THR ASP VAL MET TRP ASP LEU SER LEU PRO VAL
SEQRES 19 A 327 GLY VAL ASP ARG ASP HIS GLU TYR SER ASN PRO THR VAL
SEQRES 20 A 327 GLY ASP GLY SER GLU LYS LEU GLU LYS ILE GLY ARG LEU
SEQRES 21 A 327 ARG TRP LYS VAL MET MET ILE GLY GLY GLU ASP ASP PRO
SEQRES 22 A 327 MET ILE ASP LEU GLN LYS ASP VAL ALA LYS LEU MET LYS
SEQRES 23 A 327 LYS LYS GLY VAL GLU VAL VAL GLU HIS TYR THR GLY GLY
SEQRES 24 A 327 HIS VAL HIS GLY ALA GLU ILE ARG ASP PRO SER LYS ARG
SEQRES 25 A 327 LYS THR LEU PHE LEU SER ILE LYS ASN PHE ILE PHE SER
SEQRES 26 A 327 VAL LEU
SEQRES 1 B 327 MET SER GLU PRO SER PRO ILE ALA ASP PRO TYR ALA TYR
SEQRES 2 B 327 LEU ASN ILE VAL ASN ASN PRO ASP GLY SER ILE THR ARG
SEQRES 3 B 327 ASP LEU SER ASN PHE PRO CYS THR ALA ALA THR PRO ASP
SEQRES 4 B 327 PRO SER PRO LEU ASN PRO ALA VAL SER LYS ASP LEU PRO
SEQRES 5 B 327 VAL ASN GLN LEU LYS SER THR TRP LEU ARG LEU TYR LEU
SEQRES 6 B 327 PRO SER SER ALA VAL ASN GLU GLY ASN VAL SER SER GLN
SEQRES 7 B 327 LYS LEU PRO ILE VAL VAL TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 B 327 ILE LEU CYS SER VAL ASP MET GLN LEU PHE HIS ASP PHE
SEQRES 9 B 327 CYS SER GLU VAL ALA ARG ASP LEU ASN ALA ILE VAL VAL
SEQRES 10 B 327 SER PRO SER TYR ARG LEU ALA PRO GLU HIS ARG LEU PRO
SEQRES 11 B 327 ALA ALA TYR ASP ASP GLY VAL GLU ALA LEU ASP TRP ILE
SEQRES 12 B 327 LYS THR SER ASP ASP GLU TRP ILE LYS SER HIS ALA ASP
SEQRES 13 B 327 PHE SER ASN VAL PHE LEU MET GLY THR SER ALA GLY GLY
SEQRES 14 B 327 ASN LEU ALA TYR ASN VAL GLY LEU ARG SER VAL ASP SER
SEQRES 15 B 327 VAL SER ASP LEU SER PRO LEU GLN ILE ARG GLY LEU ILE
SEQRES 16 B 327 LEU HIS HIS PRO PHE PHE GLY GLY GLU GLU ARG SER GLU
SEQRES 17 B 327 SER GLU ILE ARG LEU MET ASN ASP GLN VAL CYS PRO PRO
SEQRES 18 B 327 ILE VAL THR ASP VAL MET TRP ASP LEU SER LEU PRO VAL
SEQRES 19 B 327 GLY VAL ASP ARG ASP HIS GLU TYR SER ASN PRO THR VAL
SEQRES 20 B 327 GLY ASP GLY SER GLU LYS LEU GLU LYS ILE GLY ARG LEU
SEQRES 21 B 327 ARG TRP LYS VAL MET MET ILE GLY GLY GLU ASP ASP PRO
SEQRES 22 B 327 MET ILE ASP LEU GLN LYS ASP VAL ALA LYS LEU MET LYS
SEQRES 23 B 327 LYS LYS GLY VAL GLU VAL VAL GLU HIS TYR THR GLY GLY
SEQRES 24 B 327 HIS VAL HIS GLY ALA GLU ILE ARG ASP PRO SER LYS ARG
SEQRES 25 B 327 LYS THR LEU PHE LEU SER ILE LYS ASN PHE ILE PHE SER
SEQRES 26 B 327 VAL LEU
HET IMD A 401 5
HET EDO A 402 4
HET IMD B 401 5
HET EDO B 402 4
HETNAM IMD IMIDAZOLE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 IMD 2(C3 H5 N2 1+)
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 7 HOH *390(H2 O)
HELIX 1 AA1 ASP A 9 ASN A 15 1 7
HELIX 2 AA2 LEU A 28 PHE A 31 5 4
HELIX 3 AA3 SER A 68 VAL A 70 5 3
HELIX 4 AA4 MET A 98 ASN A 113 1 16
HELIX 5 AA5 PRO A 130 SER A 146 1 17
HELIX 6 AA6 ASP A 148 HIS A 154 1 7
HELIX 7 AA7 SER A 166 ASP A 181 1 16
HELIX 8 AA8 SER A 182 SER A 187 1 6
HELIX 9 AA9 SER A 207 LEU A 213 1 7
HELIX 10 AB1 PRO A 220 LEU A 232 1 13
HELIX 11 AB2 LYS A 253 LEU A 260 1 8
HELIX 12 AB3 MET A 274 LYS A 288 1 15
HELIX 13 AB4 GLY A 303 ASP A 308 1 6
HELIX 14 AB5 LYS A 311 SER A 325 1 15
HELIX 15 AB6 ASP B 9 ASN B 15 1 7
HELIX 16 AB7 SER B 68 VAL B 70 5 3
HELIX 17 AB8 MET B 98 ASN B 113 1 16
HELIX 18 AB9 PRO B 130 THR B 145 1 16
HELIX 19 AC1 ASP B 148 HIS B 154 1 7
HELIX 20 AC2 SER B 166 VAL B 180 1 15
HELIX 21 AC3 SER B 182 SER B 187 1 6
HELIX 22 AC4 SER B 207 LEU B 213 1 7
HELIX 23 AC5 PRO B 220 LEU B 232 1 13
HELIX 24 AC6 LYS B 253 LEU B 260 1 8
HELIX 25 AC7 MET B 274 LYS B 288 1 15
HELIX 26 AC8 GLY B 303 ASP B 308 1 6
HELIX 27 AC9 LYS B 311 SER B 325 1 15
SHEET 1 AA1 2 ILE A 16 ASN A 18 0
SHEET 2 AA1 2 ILE A 24 ARG A 26 -1 O THR A 25 N VAL A 17
SHEET 1 AA2 8 ALA A 46 ASN A 54 0
SHEET 2 AA2 8 THR A 59 PRO A 66 -1 O THR A 59 N VAL A 53
SHEET 3 AA2 8 ILE A 115 PRO A 119 -1 O SER A 118 N ARG A 62
SHEET 4 AA2 8 LEU A 80 TYR A 86 1 N TYR A 85 O VAL A 117
SHEET 5 AA2 8 ALA A 155 THR A 165 1 O MET A 163 N VAL A 84
SHEET 6 AA2 8 ILE A 191 HIS A 197 1 O ILE A 195 N LEU A 162
SHEET 7 AA2 8 LYS A 263 GLY A 269 1 O MET A 265 N LEU A 196
SHEET 8 AA2 8 VAL A 292 THR A 297 1 O VAL A 293 N VAL A 264
SHEET 1 AA3 2 ILE B 16 ASN B 18 0
SHEET 2 AA3 2 ILE B 24 ARG B 26 -1 O THR B 25 N VAL B 17
SHEET 1 AA4 8 ALA B 46 ASN B 54 0
SHEET 2 AA4 8 THR B 59 PRO B 66 -1 O LEU B 63 N LYS B 49
SHEET 3 AA4 8 ILE B 115 PRO B 119 -1 O SER B 118 N ARG B 62
SHEET 4 AA4 8 LEU B 80 TYR B 86 1 N TYR B 85 O VAL B 117
SHEET 5 AA4 8 ALA B 155 THR B 165 1 O MET B 163 N VAL B 84
SHEET 6 AA4 8 ILE B 191 HIS B 197 1 O ARG B 192 N VAL B 160
SHEET 7 AA4 8 LYS B 263 GLY B 269 1 O MET B 265 N LEU B 196
SHEET 8 AA4 8 GLU B 291 THR B 297 1 O VAL B 293 N VAL B 264
CISPEP 1 ALA A 124 PRO A 125 0 3.08
CISPEP 2 LEU A 129 PRO A 130 0 9.21
CISPEP 3 SER A 187 PRO A 188 0 8.91
CISPEP 4 ALA B 124 PRO B 125 0 3.71
CISPEP 5 LEU B 129 PRO B 130 0 7.49
CISPEP 6 SER B 187 PRO B 188 0 9.33
CRYST1 66.587 95.701 100.313 90.00 90.00 90.00 P 21 21 21 8
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 0.015018 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010449 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009969 0.00000
TER 2477 VAL A 326
TER 4952 VAL B 326
MASTER 269 0 4 27 20 0 0 6 5308 2 18 52
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