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HEADER HYDROLASE 04-APR-23 8IYC
TITLE STRUCTURE INSIGHT INTO SUBSTRATE RECOGNITION AND CATALYSIS BY FERULOYL
TITLE 2 ESTERASE FROM ASPERGILLUS SYDOWII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARBOXYLIC ESTER HYDROLASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS SYDOWII;
SOURCE 3 ORGANISM_TAXID: 75750;
SOURCE 4 GENE: ASPSYDRAFT_1158585;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: X-33;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA
KEYWDS FERULOYL ESTERASE, COMPLEX, SINAPIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PHIENLUPHON,K.KONDO,B.MIKAMI,T.NAGATA,M.KATAHIRA
REVDAT 1 25-OCT-23 8IYC 0
JRNL AUTH A.PHIENLUPHON,K.KONDO,B.MIKAMI,T.NAGATA,M.KATAHIRA
JRNL TITL STRUCTURAL INSIGHTS INTO THE MOLECULAR MECHANISMS OF
JRNL TITL 2 SUBSTRATE RECOGNITION AND HYDROLYSIS BY FERULOYL ESTERASE
JRNL TITL 3 FROM ASPERGILLUS SYDOWII.
JRNL REF INT.J.BIOL.MACROMOL. V. 253 27188 2023
JRNL REFN ISSN 0141-8130
JRNL PMID 37783244
JRNL DOI 10.1016/J.IJBIOMAC.2023.127188
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.ARACIL
REMARK 1 TITL [TREATMENT OF VITREOUS HEMORRHAGES. RARE CAUSES].
REMARK 1 REF BULL SOC OPHTALMOL FR V.C NO 137 1987
REMARK 1 REFN ISSN 0081-1270
REMARK 1 PMID 3322595
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 65404
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3272
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 32.6300 - 4.3900 0.99 2831 150 0.1476 0.1826
REMARK 3 2 4.3900 - 3.4900 1.00 2769 145 0.1218 0.1703
REMARK 3 3 3.4900 - 3.0500 1.00 2769 146 0.1312 0.1618
REMARK 3 4 3.0500 - 2.7700 0.99 2741 144 0.1384 0.1796
REMARK 3 5 2.7700 - 2.5700 0.99 2732 144 0.1327 0.1917
REMARK 3 6 2.5700 - 2.4200 0.99 2729 144 0.1289 0.1634
REMARK 3 7 2.4200 - 2.3000 0.99 2755 145 0.1228 0.1663
REMARK 3 8 2.3000 - 2.2000 0.99 2710 142 0.1252 0.1938
REMARK 3 9 2.2000 - 2.1100 0.99 2730 144 0.1226 0.1828
REMARK 3 10 2.1100 - 2.0400 0.99 2717 143 0.1237 0.2043
REMARK 3 11 2.0400 - 1.9800 0.99 2701 143 0.1335 0.2162
REMARK 3 12 1.9800 - 1.9200 0.99 2734 143 0.1317 0.2040
REMARK 3 13 1.9200 - 1.8700 0.99 2688 142 0.1282 0.1679
REMARK 3 14 1.8700 - 1.8200 0.99 2784 147 0.1187 0.2023
REMARK 3 15 1.8200 - 1.7800 0.99 2655 139 0.1266 0.2086
REMARK 3 16 1.7800 - 1.7400 0.99 2746 145 0.1365 0.2367
REMARK 3 17 1.7400 - 1.7100 0.99 2656 140 0.1440 0.2064
REMARK 3 18 1.7100 - 1.6800 0.98 2710 143 0.1414 0.2151
REMARK 3 19 1.6800 - 1.6500 0.98 2717 143 0.1428 0.2110
REMARK 3 20 1.6500 - 1.6200 0.98 2655 139 0.1552 0.2106
REMARK 3 21 1.6200 - 1.5900 0.97 2670 141 0.1728 0.2298
REMARK 3 22 1.5900 - 1.5700 0.96 2608 137 0.1844 0.2655
REMARK 3 23 1.5700 - 1.5500 0.85 2325 123 0.2218 0.2885
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) : 0.166
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.73
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 : 0.006 4525
REMARK 3 ANGLE : 0.801 6171
REMARK 3 CHIRALITY : 0.056 661
REMARK 3 PLANARITY : 0.006 820
REMARK 3 DIHEDRAL : 8.774 661
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 8IYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1300036778.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JAN10, 2022
REMARK 200 DATA SCALING SOFTWARE : XDS JAN10, 2022
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65419
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.510
REMARK 200 R MERGE (I) : 0.02900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.01
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.610
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.7.01
REMARK 200 STARTING MODEL: 8IY8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M SODIUM
REMARK 280 ACETATE, 30%(W/V) PEG 4000, 10 MM SINAPIC ACID, PH 4.6, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 32.62900
REMARK 290 SMTRY3 2 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
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 ASN A 29 73.04 54.97
REMARK 500 SER A 90 -149.05 53.10
REMARK 500 SER A 119 -115.18 52.21
REMARK 500 SER A 119 -114.42 51.11
REMARK 500 TRP A 185 79.01 -153.84
REMARK 500 SER B 90 -150.15 54.83
REMARK 500 SER B 119 -110.81 49.66
REMARK 500 SER B 119 -108.46 46.15
REMARK 500 TRP B 185 76.51 -152.28
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 A 608 DISTANCE = 6.61 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8IY8 RELATED DB: PDB
REMARK 900 8IY8 CONTAINS THE SAME PROTEIN
REMARK 900 RELATED ID: 8IYB RELATED DB: PDB
REMARK 900 8IYB CONTAINS THE SAME PROTEIN COMPLEXED WITH FERULIC ACID
DBREF1 8IYC A 1 275 UNP A0A1L9T9J3_9EURO
DBREF2 8IYC A A0A1L9T9J3 19 293
DBREF1 8IYC B 1 275 UNP A0A1L9T9J3_9EURO
DBREF2 8IYC B A0A1L9T9J3 19 293
SEQADV 8IYC HIS A -5 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS A -4 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS A -3 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS A -2 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS A -1 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS A 0 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS B -5 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS B -4 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS B -3 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS B -2 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS B -1 UNP A0A1L9T9J EXPRESSION TAG
SEQADV 8IYC HIS B 0 UNP A0A1L9T9J EXPRESSION TAG
SEQRES 1 A 281 HIS HIS HIS HIS HIS HIS ALA THR LEU SER GLN VAL LEU
SEQRES 2 A 281 ASP PHE GLY ASN ASN PRO GLY ASP ASN GLU MET TRP ILE
SEQRES 3 A 281 TYR VAL PRO ASP GLN LEU ALA ALA ASN PRO ALA VAL ILE
SEQRES 4 A 281 VAL ALA LEU HIS GLY CYS LEU GLY SER ALA GLU GLY TYR
SEQRES 5 A 281 TYR SER GLU VAL GLN ASP LEU PRO PRO ALA ALA ASP GLU
SEQRES 6 A 281 ASN GLY PHE ILE LEU VAL TYR PRO GLY SER ASN ASP ASP
SEQRES 7 A 281 PHE HIS CYS TRP ASP VAL ALA THR ALA GLU SER LEU THR
SEQRES 8 A 281 HIS ASP GLY GLY SER ASP SER ARG SER ILE VAL ASN MET
SEQRES 9 A 281 VAL GLN TYR THR LEU ASP LYS TYR SER GLY ASP SER SER
SEQRES 10 A 281 LYS VAL PHE THR THR GLY SER SER SER GLY ALA MET MET
SEQRES 11 A 281 SER LEU VAL LEU ALA ALA ALA TYR PRO ASP VAL PHE SER
SEQRES 12 A 281 GLY VAL ALA ALA TYR SER GLY VAL PRO TYR GLY CYS LEU
SEQRES 13 A 281 ARG GLY SER PRO GLY SER SER PRO PHE THR ALA ASP GLN
SEQRES 14 A 281 ALA CYS ALA ASN GLY GLU VAL SER ARG THR ALA GLN GLU
SEQRES 15 A 281 TRP LYS ASP GLU VAL LYS MET ALA TRP PRO GLY TYR ASN
SEQRES 16 A 281 GLY THR TYR PRO LYS VAL GLN VAL TRP HIS GLY THR ALA
SEQRES 17 A 281 ASP SER VAL ILE SER PRO ASN ASN PHE ASP GLU GLU VAL
SEQRES 18 A 281 LYS GLN TRP SER ALA VAL PHE GLY VAL ASN VAL THR LYS
SEQRES 19 A 281 GLU GLU GLN ASP SER PRO LEU ASP GLY TYR THR ARG SER
SEQRES 20 A 281 ILE PHE GLY ASP GLY SER HIS PHE GLU ALA TYR LEU ALA
SEQRES 21 A 281 GLU GLY VAL GLY HIS VAL VAL PRO THR GLN VAL ASP SER
SEQRES 22 A 281 THR LEU ARG TRP PHE GLY LEU ILE
SEQRES 1 B 281 HIS HIS HIS HIS HIS HIS ALA THR LEU SER GLN VAL LEU
SEQRES 2 B 281 ASP PHE GLY ASN ASN PRO GLY ASP ASN GLU MET TRP ILE
SEQRES 3 B 281 TYR VAL PRO ASP GLN LEU ALA ALA ASN PRO ALA VAL ILE
SEQRES 4 B 281 VAL ALA LEU HIS GLY CYS LEU GLY SER ALA GLU GLY TYR
SEQRES 5 B 281 TYR SER GLU VAL GLN ASP LEU PRO PRO ALA ALA ASP GLU
SEQRES 6 B 281 ASN GLY PHE ILE LEU VAL TYR PRO GLY SER ASN ASP ASP
SEQRES 7 B 281 PHE HIS CYS TRP ASP VAL ALA THR ALA GLU SER LEU THR
SEQRES 8 B 281 HIS ASP GLY GLY SER ASP SER ARG SER ILE VAL ASN MET
SEQRES 9 B 281 VAL GLN TYR THR LEU ASP LYS TYR SER GLY ASP SER SER
SEQRES 10 B 281 LYS VAL PHE THR THR GLY SER SER SER GLY ALA MET MET
SEQRES 11 B 281 SER LEU VAL LEU ALA ALA ALA TYR PRO ASP VAL PHE SER
SEQRES 12 B 281 GLY VAL ALA ALA TYR SER GLY VAL PRO TYR GLY CYS LEU
SEQRES 13 B 281 ARG GLY SER PRO GLY SER SER PRO PHE THR ALA ASP GLN
SEQRES 14 B 281 ALA CYS ALA ASN GLY GLU VAL SER ARG THR ALA GLN GLU
SEQRES 15 B 281 TRP LYS ASP GLU VAL LYS MET ALA TRP PRO GLY TYR ASN
SEQRES 16 B 281 GLY THR TYR PRO LYS VAL GLN VAL TRP HIS GLY THR ALA
SEQRES 17 B 281 ASP SER VAL ILE SER PRO ASN ASN PHE ASP GLU GLU VAL
SEQRES 18 B 281 LYS GLN TRP SER ALA VAL PHE GLY VAL ASN VAL THR LYS
SEQRES 19 B 281 GLU GLU GLN ASP SER PRO LEU ASP GLY TYR THR ARG SER
SEQRES 20 B 281 ILE PHE GLY ASP GLY SER HIS PHE GLU ALA TYR LEU ALA
SEQRES 21 B 281 GLU GLY VAL GLY HIS VAL VAL PRO THR GLN VAL ASP SER
SEQRES 22 B 281 THR LEU ARG TRP PHE GLY LEU ILE
HET SXX A 301 16
HET NAG A 302 14
HET NAG A 303 14
HET EDO A 304 4
HET EDO A 305 4
HET EDO A 306 4
HET EDO A 307 4
HET EDO A 308 4
HET EDO A 309 4
HET EDO A 310 4
HET ACT A 311 4
HET ACT A 312 4
HET ACT A 313 4
HET SXX B 301 16
HET NAG B 302 14
HET NAG B 303 14
HET EDO B 304 4
HET EDO B 305 4
HET EDO B 306 4
HET EDO B 307 4
HET EDO B 308 4
HET EDO B 309 4
HET ACT B 310 4
HET ACT B 311 4
HET ACT B 312 4
HET ACT B 313 4
HET ACT B 314 4
HETNAM SXX SINAPINATE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SXX 2(C11 H12 O5)
FORMUL 4 NAG 4(C8 H15 N O6)
FORMUL 6 EDO 13(C2 H6 O2)
FORMUL 13 ACT 8(C2 H3 O2 1-)
FORMUL 30 HOH *378(H2 O)
HELIX 1 AA1 SER A 42 VAL A 50 1 9
HELIX 2 AA2 ASP A 52 GLY A 61 1 10
HELIX 3 AA3 THR A 80 THR A 85 1 6
HELIX 4 AA4 GLY A 89 SER A 107 1 19
HELIX 5 AA5 SER A 119 TYR A 132 1 14
HELIX 6 AA6 THR A 173 ALA A 184 1 12
HELIX 7 AA7 PRO A 208 GLY A 223 1 16
HELIX 8 AA8 GLN A 264 PHE A 272 1 9
HELIX 9 AA9 SER B 42 VAL B 50 1 9
HELIX 10 AB1 ASP B 52 GLY B 61 1 10
HELIX 11 AB2 THR B 80 THR B 85 1 6
HELIX 12 AB3 GLY B 89 SER B 107 1 19
HELIX 13 AB4 SER B 119 TYR B 132 1 14
HELIX 14 AB5 THR B 173 ALA B 184 1 12
HELIX 15 AB6 PRO B 208 GLY B 223 1 16
HELIX 16 AB7 GLN B 264 PHE B 272 1 9
SHEET 1 AA110 LEU A 3 GLN A 5 0
SHEET 2 AA110 GLU A 17 TYR A 21 -1 O ILE A 20 N SER A 4
SHEET 3 AA110 ILE A 63 GLY A 68 -1 O TYR A 66 N TRP A 19
SHEET 4 AA110 VAL A 32 LEU A 36 1 N ALA A 35 O VAL A 65
SHEET 5 AA110 VAL A 113 SER A 118 1 O PHE A 114 N VAL A 34
SHEET 6 AA110 GLY A 138 TYR A 142 1 O TYR A 142 N GLY A 117
SHEET 7 AA110 LYS A 194 GLY A 200 1 O GLN A 196 N ALA A 141
SHEET 8 AA110 PHE A 249 ALA A 254 1 O ALA A 254 N HIS A 199
SHEET 9 AA110 TYR A 238 PHE A 243 -1 N SER A 241 O ALA A 251
SHEET 10 AA110 VAL A 226 GLU A 230 -1 N LYS A 228 O ILE A 242
SHEET 1 AA210 SER B 4 VAL B 6 0
SHEET 2 AA210 GLU B 17 TYR B 21 -1 O ILE B 20 N SER B 4
SHEET 3 AA210 ILE B 63 GLY B 68 -1 O TYR B 66 N TRP B 19
SHEET 4 AA210 VAL B 32 LEU B 36 1 N ALA B 35 O VAL B 65
SHEET 5 AA210 VAL B 113 SER B 118 1 O THR B 116 N VAL B 34
SHEET 6 AA210 GLY B 138 TYR B 142 1 O TYR B 142 N GLY B 117
SHEET 7 AA210 LYS B 194 GLY B 200 1 O GLN B 196 N ALA B 141
SHEET 8 AA210 PHE B 249 ALA B 254 1 O ALA B 254 N HIS B 199
SHEET 9 AA210 TYR B 238 PHE B 243 -1 N SER B 241 O ALA B 251
SHEET 10 AA210 VAL B 226 GLU B 230 -1 N LYS B 228 O ILE B 242
SSBOND 1 CYS A 39 CYS A 75 1555 1555 2.03
SSBOND 2 CYS A 149 CYS A 165 1555 1555 2.05
SSBOND 3 CYS B 39 CYS B 75 1555 1555 2.04
SSBOND 4 CYS B 149 CYS B 165 1555 1555 2.04
LINK ND2 ASN A 189 C1 NAG A 302 1555 1555 1.44
LINK ND2 ASN A 225 C1 NAG A 303 1555 1555 1.43
LINK ND2 ASN B 189 C1 NAG B 302 1555 1555 1.45
LINK ND2 ASN B 225 C1 NAG B 303 1555 1555 1.44
CISPEP 1 SER A 233 PRO A 234 0 5.53
CISPEP 2 HIS A 259 VAL A 260 0 -2.34
CISPEP 3 SER B 233 PRO B 234 0 7.15
CISPEP 4 HIS B 259 VAL B 260 0 -4.56
CRYST1 37.378 65.258 95.381 90.00 97.00 90.00 P 1 21 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 0.026754 0.000000 0.003283 0.00000
SCALE2 0.000000 0.015324 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010563 0.00000
TER 2133 ILE A 275
TER 4244 ILE B 275
MASTER 280 0 27 16 20 0 0 6 4708 2 184 44
END |