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HEADER HYDROLASE 11-FEB-11 3QPA
TITLE STRUCTURE OF FUSARIUM SOLANI CUTINASE EXPRESSED IN PICHIA PASTORIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 32-228;
COMPND 5 SYNONYM: CUTIN HYDROLASE 1;
COMPND 6 EC: 3.1.1.74;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NECTRIA HAEMATOCOCCA;
SOURCE 3 ORGANISM_TAXID: 660122;
SOURCE 4 STRAIN: 77-13-4 / FGSC 9596 / MPVI;
SOURCE 5 GENE: CUT1, CUTA, NECHADRAFT_81019;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS ALPHA-BETA HYDROLASE FOLD, ESTERASE, HYDROLASE, CUTIN, MONO-ETHYL
KEYWDS 2 PHOSPHORYLATED SERINE RESIDUE, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GOSSER,A.LU,X.KONG,J.K.MONTCLARE,Z.LIU
REVDAT 1 29-FEB-12 3QPA 0
JRNL AUTH Y.GOSSER,A.LU,X.KONG,J.K.MONTCLARE,Z.LIU
JRNL TITL STRUCTURE OF FUSARIUM SOLANI CUTINASE EXPRESSED IN PICHIA
JRNL TITL 2 PASTORIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 0.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 141550
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.110
REMARK 3 R VALUE (WORKING SET) : 0.110
REMARK 3 FREE R VALUE : 0.117
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 7113
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 13.6922 - 2.6359 0.88 4156 212 0.1724 0.1702
REMARK 3 2 2.6359 - 2.0946 0.98 4554 267 0.1298 0.1233
REMARK 3 3 2.0946 - 1.8305 0.99 4596 248 0.1230 0.1264
REMARK 3 4 1.8305 - 1.6635 1.00 4635 227 0.1126 0.1146
REMARK 3 5 1.6635 - 1.5444 1.00 4608 264 0.1025 0.1136
REMARK 3 6 1.5444 - 1.4535 0.99 4616 204 0.0995 0.1039
REMARK 3 7 1.4535 - 1.3808 0.99 4659 217 0.0989 0.1149
REMARK 3 8 1.3808 - 1.3207 0.99 4585 216 0.0922 0.0951
REMARK 3 9 1.3207 - 1.2699 0.99 4567 243 0.0845 0.0980
REMARK 3 10 1.2699 - 1.2261 0.99 4543 251 0.0815 0.0873
REMARK 3 11 1.2261 - 1.1878 0.98 4576 224 0.0777 0.0847
REMARK 3 12 1.1878 - 1.1539 0.98 4546 263 0.0719 0.0806
REMARK 3 13 1.1539 - 1.1235 0.98 4470 267 0.0702 0.0821
REMARK 3 14 1.1235 - 1.0961 0.98 4526 216 0.0716 0.0773
REMARK 3 15 1.0961 - 1.0712 0.98 4494 251 0.0730 0.0802
REMARK 3 16 1.0712 - 1.0484 0.97 4486 253 0.0760 0.0776
REMARK 3 17 1.0484 - 1.0274 0.97 4460 234 0.0783 0.0907
REMARK 3 18 1.0274 - 1.0081 0.97 4490 250 0.0784 0.1044
REMARK 3 19 1.0081 - 0.9901 0.97 4467 249 0.0791 0.0861
REMARK 3 20 0.9901 - 0.9733 0.97 4411 246 0.0800 0.0862
REMARK 3 21 0.9733 - 0.9576 0.96 4511 217 0.0848 0.0955
REMARK 3 22 0.9576 - 0.9429 0.96 4391 243 0.0865 0.0893
REMARK 3 23 0.9429 - 0.9290 0.96 4474 242 0.0889 0.1061
REMARK 3 24 0.9290 - 0.9159 0.96 4406 225 0.0922 0.1066
REMARK 3 25 0.9159 - 0.9035 0.96 4387 241 0.0981 0.1042
REMARK 3 26 0.9035 - 0.8918 0.95 4374 234 0.1018 0.1191
REMARK 3 27 0.8918 - 0.8807 0.95 4397 219 0.1053 0.1219
REMARK 3 28 0.8807 - 0.8700 0.95 4414 230 0.1153 0.1367
REMARK 3 29 0.8700 - 0.8599 0.95 4344 231 0.1156 0.1328
REMARK 3 30 0.8599 - 0.8503 0.93 4294 229 0.1220 0.1231
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 : 0.39
REMARK 3 B_SOL : 48.16
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.080
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 7.290
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) : 0.52510
REMARK 3 B22 (A**2) : -0.65440
REMARK 3 B33 (A**2) : 0.12930
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.27090
REMARK 3 B23 (A**2) : -0.00000
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 : 0.010 1572
REMARK 3 ANGLE : 1.499 2155
REMARK 3 CHIRALITY : 0.087 244
REMARK 3 PLANARITY : 0.009 291
REMARK 3 DIHEDRAL : 11.642 607
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 3QPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB063931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.77009
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141550
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.850
REMARK 200 RESOLUTION RANGE LOW (A) : 13.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PDB ENTRY 1CEX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG6000, 0.1M CITRIC ACID,
REMARK 280 PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 33.08250
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HG1 THR A 43 HH22 ARG A 166 1655 1.30
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 MIR A 120 -119.94 62.66
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 320 DISTANCE = 6.01 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CEX RELATED DB: PDB
REMARK 900 ORIGINAL STRUCTURE OF F. SOLANI CUTINASE ENZYME EXPRESSED
REMARK 900 IN E. COLI.
REMARK 900 RELATED ID: 3QPC RELATED DB: PDB
REMARK 900 RELATED ID: 3QPD RELATED DB: PDB
DBREF 3QPA A 16 212 UNP C7ZGJ1 C7ZGJ1_NECH7 32 228
SEQRES 1 A 197 GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY ASN SER
SEQRES 2 A 197 ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA ARG GLY
SEQRES 3 A 197 SER THR GLU THR GLY ASN LEU GLY THR LEU GLY PRO SER
SEQRES 4 A 197 ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS ASP GLY
SEQRES 5 A 197 VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG ALA THR
SEQRES 6 A 197 LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER SER ALA
SEQRES 7 A 197 ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN ALA ASN
SEQRES 8 A 197 THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY GLY TYR
SEQRES 9 A 197 MIR GLN GLY ALA ALA LEU ALA ALA ALA SER ILE GLU ASP
SEQRES 10 A 197 LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY THR VAL
SEQRES 11 A 197 LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG GLY ARG
SEQRES 12 A 197 ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL PHE CYS
SEQRES 13 A 197 ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU ILE VAL
SEQRES 14 A 197 ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA ARG GLY
SEQRES 15 A 197 PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG ALA VAL
SEQRES 16 A 197 ARG GLY
MODRES 3QPA MIR A 120 SER MONOETHYLPHOSPHORYLSERINE
HET MIR A 120 21
HETNAM MIR MONOETHYLPHOSPHORYLSERINE
HETSYN MIR O-[(S)-ETHOXY(HYDROXY)PHOSPHORYL]-L-SERINE
FORMUL 1 MIR C5 H12 N O6 P
FORMUL 2 HOH *327(H2 O)
HELIX 1 1 LEU A 51 GLY A 64 1 14
HELIX 2 2 THR A 80 LEU A 86 5 7
HELIX 3 3 SER A 91 CYS A 109 1 19
HELIX 4 4 MIR A 120 LEU A 133 1 14
HELIX 5 5 ASP A 134 ASP A 139 1 6
HELIX 6 6 PRO A 163 ASP A 165 5 3
HELIX 7 7 ASP A 175 GLY A 180 5 6
HELIX 8 8 ALA A 185 ALA A 190 5 6
HELIX 9 9 TYR A 191 GLY A 197 1 7
HELIX 10 10 GLY A 197 GLY A 212 1 16
SHEET 1 A 5 VAL A 68 GLY A 72 0
SHEET 2 A 5 VAL A 34 ALA A 39 1 N PHE A 36 O TRP A 69
SHEET 3 A 5 THR A 113 TYR A 119 1 O GLY A 117 N ALA A 39
SHEET 4 A 5 ILE A 141 PHE A 147 1 O PHE A 147 N GLY A 118
SHEET 5 A 5 THR A 167 PHE A 170 1 O PHE A 170 N LEU A 146
SSBOND 1 CYS A 31 CYS A 109 1555 1555 2.06
SSBOND 2 CYS A 171 CYS A 178 1555 1555 2.08
CISPEP 1 GLY A 16 ARG A 17 0 -0.34
CRYST1 35.006 66.165 36.755 90.00 93.93 90.00 P 1 21 1 2
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 0.028567 0.000000 0.001962 0.00000
SCALE2 0.000000 0.015114 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027271 0.00000
TER 3082 GLY A 212
MASTER 268 0 1 10 5 0 0 6 1771 1 25 16
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