| 4OU4-pdb | HEADER HYDROLASE 15-FEB-14 4OU4
TITLE CRYSTAL STRUCTURE OF ESTERASE RPPE MUTANT S159A COMPLEXED WITH (S)-AC-
TITLE 2 CPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD-3 DOMAIN PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ESTERASE;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS;
SOURCE 3 ORGANISM_TAXID: 657346;
SOURCE 4 STRAIN: ECU1011;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS A/B HYDROLASE FOLD, ESTERASE, HSL-LIKE FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DOU,X.D.KONG,B.D.MA,J.H.XU,J.H.ZHOU
REVDAT 1 30-JUL-14 4OU4 0
JRNL AUTH S.DOU,X.D.KONG,B.D.MA,Q.CHEN,J.ZHANG,J.H.ZHOU,J.H.XU
JRNL TITL CRYSTAL STRUCTURES OF PSEUDOMONAS PUTIDA ESTERASE REVEAL THE
JRNL TITL 2 FUNCTIONAL ROLE OF RESIDUES 187 AND 287 IN SUBSTRATE BINDING
JRNL TITL 3 AND CHIRAL RECOGNITION
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 446 1145 2014
JRNL REFN ISSN 0006-291X
JRNL PMID 24680822
JRNL DOI 10.1016/J.BBRC.2014.03.072
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.3_1479)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 16258
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) : 0.167
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 819
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 42.3237 - 4.3580 1.00 2758 124 0.1640 0.2203
REMARK 3 2 4.3580 - 3.4595 1.00 2598 127 0.1593 0.2145
REMARK 3 3 3.4595 - 3.0224 1.00 2545 144 0.1629 0.2283
REMARK 3 4 3.0224 - 2.7461 1.00 2537 148 0.1761 0.2743
REMARK 3 5 2.7461 - 2.5493 1.00 2512 128 0.1796 0.2560
REMARK 3 6 2.5493 - 2.3990 0.99 2489 148 0.1873 0.2619
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.49
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 2518
REMARK 3 ANGLE : 1.122 3426
REMARK 3 CHIRALITY : 0.042 380
REMARK 3 PLANARITY : 0.006 449
REMARK 3 DIHEDRAL : 14.064 907
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 4OU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-14.
REMARK 100 THE RCSB ID CODE IS RCSB084950.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX-HF
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : 0.16700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
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: PHASER
REMARK 200 STARTING MODEL: 2YH2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) PEG8000, 0.04M KH2PO4, 20%
REMARK 280 GLYCEROL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 44.26650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.31200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.31200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.39975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.31200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.31200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.13325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.31200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.31200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 66.39975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.31200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.31200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 22.13325
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 44.26650
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: DIMERIC
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 BIOMT1 2 0.000000 -1.000000 0.000000 189.24800
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 189.24800
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 44.26650
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 590 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 595 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 583 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 585 LIES ON A SPECIAL POSITION.
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 -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 534 O HOH A 591 2.09
REMARK 500 OE1 GLN A 58 OG SER A 63 2.17
REMARK 500 O HOH A 579 O HOH A 588 2.18
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 TRP A 89 -17.76 70.10
REMARK 500 ASP A 93 -170.30 -177.61
REMARK 500 ALA A 159 -115.66 64.18
REMARK 500 THR A 177 148.35 -173.85
REMARK 500 PHE A 182 149.42 -171.26
REMARK 500 TRP A 187 64.64 34.22
REMARK 500 ALA A 192 47.09 -84.19
REMARK 500 PHE A 207 -70.87 68.18
REMARK 500 THR A 221 139.99 -171.29
REMARK 500 PHE A 255 48.95 -107.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S2T A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OB6 RELATED DB: PDB
REMARK 900 RELATED ID: 4OB7 RELATED DB: PDB
REMARK 900 RELATED ID: 4OB8 RELATED DB: PDB
REMARK 900 RELATED ID: 4OU5 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHOR STATED THE SEQUENCE DATABASE WAS WRONG AT THIS POSITION.
REMARK 999 RESIDUE 10 SHOULD BE GLN.
DBREF 4OU4 A 1 316 UNP L7PYQ2 L7PYQ2_9PSED 1 316
SEQADV 4OU4 MET A -13 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 ALA A -12 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 SER A -11 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 MET A -10 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 THR A -9 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLY A -8 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLY A -7 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLN A -6 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLN A -5 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 MET A -4 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLY A -3 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 ARG A -2 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLY A -1 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 SER A 0 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLN A 10 UNP L7PYQ2 LYS 10 SEE REMARK 999
SEQADV 4OU4 ALA A 159 UNP L7PYQ2 SER 159 ENGINEERED MUTATION
SEQADV 4OU4 LEU A 317 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 GLU A 318 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 HIS A 319 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 HIS A 320 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 HIS A 321 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 HIS A 322 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 HIS A 323 UNP L7PYQ2 EXPRESSION TAG
SEQADV 4OU4 HIS A 324 UNP L7PYQ2 EXPRESSION TAG
SEQRES 1 A 338 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 A 338 SER GLY SER PRO GLY VAL GLU GLN HIS THR GLN ALA PHE
SEQRES 3 A 338 LEU GLU ALA LEU GLU GLN GLY GLY GLY LYS PRO LEU GLU
SEQRES 4 A 338 GLN LEU SER PRO LYS ASP ALA ARG ALA VAL LEU THR GLY
SEQRES 5 A 338 ALA GLN ALA SER VAL LYS VAL ASP LEU SER GLY ILE GLU
SEQRES 6 A 338 VAL LYS GLU ARG THR ILE GLN ALA ASN GLY GLN SER ILE
SEQRES 7 A 338 LYS LEU GLN VAL VAL ARG PRO ALA ASN VAL LYS GLY GLU
SEQRES 8 A 338 LEU PRO VAL PHE MET PHE PHE HIS GLY GLY GLY TRP VAL
SEQRES 9 A 338 LEU GLY ASP PHE PRO THR HIS GLN ARG LEU ILE ARG ASP
SEQRES 10 A 338 LEU VAL VAL GLY SER GLY ALA VAL ALA VAL TYR VAL ASP
SEQRES 11 A 338 TYR THR PRO SER PRO GLU SER HIS TYR PRO THR ALA ILE
SEQRES 12 A 338 ASN GLN ALA TYR ALA ALA THR GLN TRP VAL ALA GLU HIS
SEQRES 13 A 338 GLY LYS GLU ILE GLY VAL ASP GLY LYS ARG LEU ALA VAL
SEQRES 14 A 338 ALA GLY ASN ALA VAL GLY GLY ASN MET ALA ALA VAL VAL
SEQRES 15 A 338 ALA LEU LYS ALA LYS GLU ALA GLY THR PRO ALA LEU ARG
SEQRES 16 A 338 PHE GLN LEU LEU LEU TRP PRO VAL THR ASP ALA SER PHE
SEQRES 17 A 338 GLU THR ALA SER TYR LYS GLN PHE ALA ASP GLY HIS PHE
SEQRES 18 A 338 LEU THR THR GLY MET MET LYS TRP PHE TRP ASP ASN TYR
SEQRES 19 A 338 THR THR ASP ALA LYS ALA ARG GLU GLN ILE TYR ALA SER
SEQRES 20 A 338 PRO LEU ARG ALA SER SER GLU GLN LEU LYS GLY LEU PRO
SEQRES 21 A 338 PRO ALA LEU VAL GLN THR ALA GLU PHE ASP VAL LEU ARG
SEQRES 22 A 338 ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ASN ALA ALA
SEQRES 23 A 338 GLY VAL THR VAL THR SER VAL ARG TYR ASN GLY MET ILE
SEQRES 24 A 338 HIS ASP TYR GLY LEU LEU ASN PRO LEU SER GLN VAL PRO
SEQRES 25 A 338 ALA VAL LYS ALA ALA MET ARG GLN ALA GLY THR GLU LEU
SEQRES 26 A 338 LYS VAL HIS LEU GLN LEU GLU HIS HIS HIS HIS HIS HIS
HET S2T A 401 15
HETNAM S2T (2S)-(ACETYLOXY)(2-CHLOROPHENYL)ETHANOIC ACID
FORMUL 2 S2T C10 H9 CL O4
FORMUL 3 HOH *98(H2 O)
HELIX 1 1 GLU A 6 GLN A 18 1 13
HELIX 2 2 PRO A 23 LEU A 27 5 5
HELIX 3 3 SER A 28 SER A 42 1 15
HELIX 4 4 ASP A 93 GLY A 109 1 17
HELIX 5 5 PRO A 126 GLY A 143 1 18
HELIX 6 6 LYS A 144 ILE A 146 5 3
HELIX 7 7 ALA A 159 GLY A 176 1 18
HELIX 8 8 THR A 196 PHE A 202 1 7
HELIX 9 9 THR A 209 THR A 221 1 13
HELIX 10 10 ASP A 223 GLU A 228 1 6
HELIX 11 11 SER A 233 ALA A 237 5 5
HELIX 12 12 SER A 238 LYS A 243 1 6
HELIX 13 13 LEU A 258 ALA A 272 1 15
HELIX 14 14 LEU A 291 SER A 295 5 5
HELIX 15 15 VAL A 297 LEU A 315 1 19
SHEET 1 A 8 ILE A 50 ALA A 59 0
SHEET 2 A 8 GLN A 62 PRO A 71 -1 O ARG A 70 N GLU A 51
SHEET 3 A 8 VAL A 111 VAL A 115 -1 O ALA A 112 N VAL A 69
SHEET 4 A 8 LEU A 78 PHE A 84 1 N PHE A 81 O VAL A 111
SHEET 5 A 8 VAL A 148 ASN A 158 1 O ALA A 154 N MET A 82
SHEET 6 A 8 PHE A 182 LEU A 186 1 O LEU A 184 N VAL A 155
SHEET 7 A 8 ALA A 248 PHE A 255 1 O LEU A 249 N LEU A 185
SHEET 8 A 8 VAL A 276 ILE A 285 1 O THR A 277 N VAL A 250
CISPEP 1 SER A 120 PRO A 121 0 3.31
CISPEP 2 TYR A 125 PRO A 126 0 5.06
CISPEP 3 THR A 177 PRO A 178 0 -5.43
SITE 1 AC1 4 PRO A 298 LYS A 301 ARG A 305 HIS A 314
CRYST1 94.624 94.624 88.533 90.00 90.00 90.00 P 43 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 0.010568 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010568 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011295 0.00000
TER 2447 GLU A 318
MASTER 303 0 1 15 8 0 1 6 2539 1 15 26
END
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