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HEADER HYDROLASE 15-SEP-03 1QZ3
TITLE CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE
TITLE 2 EST2 COMPLEXED WITH HEXADECANESULFONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE EST2;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALICYCLOBACILLUS ACIDOCALDARIUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7SCII
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.DE SIMONE,L.MANDRICH,V.MENCHISE,V.GIORDANO,F.FEBBRAIO,
AUTHOR 2 M.ROSSI,C.PEDONE,G.MANCO
REVDAT 1 23-MAR-04 1QZ3 0
JRNL AUTH G.DE SIMONE,L.MANDRICH,V.MENCHISE,V.GIORDANO,
JRNL AUTH 2 F.FEBBRAIO,M.ROSSI,C.PEDONE,G.MANCO
JRNL TITL A SUBSTRATE-INDUCED SWITCH IN THE REACTION
JRNL TITL 2 MECHANISM OF A THERMOPHILIC ESTERASE: KINETIC
JRNL TITL 3 EVIDENCES AND STRUCTURAL BASIS.
JRNL REF J.BIOL.CHEM. V. 279 6815 2004
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.DE SIMONE,S.GALDIERO,G.MANCO,D.LANG,M.ROSSI,
REMARK 1 AUTH 2 C.PEDONE
REMARK 1 TITL A SNAPSHOT OF THE TRANSITION STATE ANALOGUE OF A
REMARK 1 TITL 2 NOVEL THERMOPHILIC ESTERASE BELONGING TO THE
REMARK 1 TITL 3 SUBFAMILY OF MAMMALIAN HORMONE-SENSITIVE LIPASE
REMARK 1 REF J.MOL.BIOL. V. 303 761 2000
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 16467
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 SET) : 0.174
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 789
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2412
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 253
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.53
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.175 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.835 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.180 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.137 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : P_HEP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QZ3 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-2003.
REMARK 100 THE RCSB ID CODE IS RCSB020244.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8015
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17707
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42600
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EVQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, TRIS BUFFER, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 3555 1/2-Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,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 51.79250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.59650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.59650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.89625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.59650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.59650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.68875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.59650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.59650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.89625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.59650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.59650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.68875
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 51.79250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 MET A 1
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 PRO A 2 CG CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 44 CB PRO A 44 CG 0.055
REMARK 500 SER A 155 CB SER A 155 OG 0.084
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 3 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
REMARK 500 PRO A 56 C - N - CA ANGL. DEV. = -9.0 DEGREES
REMARK 500 PRO A 75 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 VAL A 78 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 GLU A 278 N - CA - C ANGL. DEV. = 11.4 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 155 -118.77 46.10
REMARK 500 LEU A 205 -72.25 70.22
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EVQ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE
REMARK 900 EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 IN THE DATABASE SEQUENCE, X REPRESENTS ANY AMINO ACID.
DBREF 1QZ3 A 1 310 GB 11513478 1EVQ_A 1 310
SEQADV 1QZ3 MET A 53 GB 11513478 X 53 SEE REMARK 999
SEQADV 1QZ3 MET A 64 GB 11513478 X 64 SEE REMARK 999
SEQADV 1QZ3 MET A 210 GB 11513478 X 210 SEE REMARK 999
SEQADV 1QZ3 SER A 211 GB 11513478 X 211 ENGINEERED
SEQADV 1QZ3 LEU A 215 GB 11513478 ARG 215 ENGINEERED
SEQRES 1 A 310 MET PRO LEU ASP PRO VAL ILE GLN GLN VAL LEU ASP GLN
SEQRES 2 A 310 LEU ASN ARG MET PRO ALA PRO ASP TYR LYS HIS LEU SER
SEQRES 3 A 310 ALA GLN GLN PHE ARG SER GLN GLN SER LEU PHE PRO PRO
SEQRES 4 A 310 VAL LYS LYS GLU PRO VAL ALA GLU VAL ARG GLU PHE ASP
SEQRES 5 A 310 MET ASP LEU PRO GLY ARG THR LEU LYS VAL ARG MET TYR
SEQRES 6 A 310 ARG PRO GLU GLY VAL GLU PRO PRO TYR PRO ALA LEU VAL
SEQRES 7 A 310 TYR TYR HIS GLY GLY GLY TRP VAL VAL GLY ASP LEU GLU
SEQRES 8 A 310 THR HIS ASP PRO VAL CYS ARG VAL LEU ALA LYS ASP GLY
SEQRES 9 A 310 ARG ALA VAL VAL PHE SER VAL ASP TYR ARG LEU ALA PRO
SEQRES 10 A 310 GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA TYR ASP
SEQRES 11 A 310 ALA LEU GLN TRP ILE ALA GLU ARG ALA ALA ASP PHE HIS
SEQRES 12 A 310 LEU ASP PRO ALA ARG ILE ALA VAL GLY GLY ASP SER ALA
SEQRES 13 A 310 GLY GLY ASN LEU ALA ALA VAL THR SER ILE LEU ALA LYS
SEQRES 14 A 310 GLU ARG GLY GLY PRO ALA LEU ALA PHE GLN LEU LEU ILE
SEQRES 15 A 310 TYR PRO SER THR GLY TYR ASP PRO ALA HIS PRO PRO ALA
SEQRES 16 A 310 SER ILE GLU GLU ASN ALA GLU GLY TYR LEU LEU THR GLY
SEQRES 17 A 310 GLY MET SER LEU TRP PHE LEU ASP GLN TYR LEU ASN SER
SEQRES 18 A 310 LEU GLU GLU LEU THR HIS PRO TRP PHE SER PRO VAL LEU
SEQRES 19 A 310 TYR PRO ASP LEU SER GLY LEU PRO PRO ALA TYR ILE ALA
SEQRES 20 A 310 THR ALA GLN TYR ASP PRO LEU ARG ASP VAL GLY LYS LEU
SEQRES 21 A 310 TYR ALA GLU ALA LEU ASN LYS ALA GLY VAL LYS VAL GLU
SEQRES 22 A 310 ILE GLU ASN PHE GLU ASP LEU ILE HIS GLY PHE ALA GLN
SEQRES 23 A 310 PHE TYR SER LEU SER PRO GLY ALA THR LYS ALA LEU VAL
SEQRES 24 A 310 ARG ILE ALA GLU LYS LEU ARG ASP ALA LEU ALA
HET HDS A 400 19
HETNAM HDS 1-HEXADECANOSULFONIC ACID
FORMUL 2 HDS C16 H34 O3 S1
FORMUL 3 HOH *253(H2 O1)
HELIX 1 1 ASP A 4 ASN A 15 1 12
HELIX 2 2 SER A 26 GLN A 34 1 9
HELIX 3 3 SER A 35 PHE A 37 5 3
HELIX 4 4 HIS A 93 ARG A 105 1 13
HELIX 5 5 PRO A 122 ARG A 138 1 17
HELIX 6 6 ALA A 139 PHE A 142 5 4
HELIX 7 7 SER A 155 ARG A 171 1 17
HELIX 8 8 ALA A 195 ASN A 200 1 6
HELIX 9 9 THR A 207 LEU A 219 1 13
HELIX 10 10 SER A 221 HIS A 227 5 7
HELIX 11 11 SER A 231 TYR A 235 5 5
HELIX 12 12 LEU A 254 ALA A 268 1 15
HELIX 13 13 GLY A 283 TYR A 288 5 6
HELIX 14 14 SER A 291 ALA A 310 1 20
SHEET 1 A 8 GLU A 47 LEU A 55 0
SHEET 2 A 8 ARG A 58 ARG A 66 -1 O MET A 64 N ARG A 49
SHEET 3 A 8 VAL A 107 ASP A 112 -1 O SER A 110 N ARG A 63
SHEET 4 A 8 TYR A 74 TYR A 80 1 N LEU A 77 O PHE A 109
SHEET 5 A 8 LEU A 144 ASP A 154 1 O ALA A 150 N ALA A 76
SHEET 6 A 8 GLN A 179 ILE A 182 1 O ILE A 182 N GLY A 153
SHEET 7 A 8 ALA A 244 ALA A 249 1 O TYR A 245 N GLN A 179
SHEET 8 A 8 VAL A 272 PHE A 277 1 O PHE A 277 N THR A 248
LINK S1 HDS A 400 OG SER A 155
CISPEP 1 PRO A 72 PRO A 73 0 -0.36
CISPEP 2 ALA A 116 PRO A 117 0 0.42
CISPEP 3 PHE A 121 PRO A 122 0 0.62
CISPEP 4 GLY A 173 PRO A 174 0 -0.28
CRYST1 85.193 85.193 103.585 90.00 90.00 90.00 P 41 21 2 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 0.011738 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011738 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009654 0.00000
TER 2413 ALA A 310
MASTER 310 0 1 14 8 0 0 6 2684 1 20 24
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