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HEADER HYDROLASE 18-SEP-18 6IEY
TITLE CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZAING ENZYME ESTDL136-
TITLE 2 CHLORAMPHENICOL COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: B, A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: TO MAKE ESTDL136 CRYSTAL, INTERNAL RESIDUES FROM P37
COMPND 8 TO P39 WERE DELETED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: ESTDL136;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS CHLORAMPHENICOL, METAGENOME, HORNOME SENSITIVE LIPASE, HSL, ESTDL136,
KEYWDS 2 ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE
REVDAT 1 06-FEB-19 6IEY 0
JRNL AUTH S.H.KIM,P.A.KANG,K.T.HAN,S.W.LEE,S.K.RHEE
JRNL TITL CRYSTAL STRUCTURE OF CHLORAMPHENICOL-METABOLIZING ENZYME
JRNL TITL 2 ESTDL136 FROM A METAGENOME.
JRNL REF PLOS ONE V. 14 10298 2019
JRNL REFN ESSN 1932-6203
JRNL PMID 30645605
JRNL DOI 10.1371/JOURNAL.PONE.0210298
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 45505
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 29.0426 - 5.0459 1.00 3500 161 0.1746 0.1980
REMARK 3 2 5.0459 - 4.0084 1.00 3337 153 0.1715 0.2170
REMARK 3 3 4.0084 - 3.5027 1.00 3332 153 0.1864 0.2557
REMARK 3 4 3.5027 - 3.1829 1.00 3260 151 0.2122 0.2613
REMARK 3 5 3.1829 - 2.9550 0.99 3206 147 0.2268 0.2888
REMARK 3 6 2.9550 - 2.7809 0.97 3164 145 0.2292 0.2709
REMARK 3 7 2.7809 - 2.6417 0.95 3094 143 0.2300 0.3132
REMARK 3 8 2.6417 - 2.5268 0.94 3058 140 0.2388 0.2895
REMARK 3 9 2.5268 - 2.4296 0.93 2996 138 0.2367 0.3280
REMARK 3 10 2.4296 - 2.3458 0.93 2992 137 0.2338 0.2723
REMARK 3 11 2.3458 - 2.2725 0.93 2997 138 0.2383 0.2977
REMARK 3 12 2.2725 - 2.2075 0.93 2982 137 0.2505 0.3167
REMARK 3 13 2.2075 - 2.1494 0.93 3037 139 0.2615 0.3319
REMARK 3 14 2.1494 - 2.0970 0.80 2550 118 0.2655 0.3109
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.160
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 4781
REMARK 3 ANGLE : 1.161 6536
REMARK 3 CHIRALITY : 0.044 711
REMARK 3 PLANARITY : 0.007 872
REMARK 3 DIHEDRAL : 13.009 1677
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 6IEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1300009077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933
REMARK 200 MONOCHROMATOR : NULL
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 : 46963
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.093
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 (%) : 96.4
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 263.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
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) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 500MM AMMONIUM FLUORIDE (PH6.5), 30%
REMARK 280 PEG 3350, 5% GLYCEOL AND 120MM TCEP., VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 59.23150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.20550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.23150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.20550
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 PRO A 20
REMARK 465 ASP A 21
REMARK 465 PHE A 22
REMARK 465 SER A 23
REMARK 465 VAL A 24
REMARK 465 ALA A 25
REMARK 465 ASN A 26
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
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 MET B 1 CG SD CE
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
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 N MET A 1 O HOH A 501 2.18
REMARK 500 OH TYR A 127 O HOH A 502 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 120 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO B 120 C - N - CD ANGL. DEV. = -25.2 DEGREES
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 PRO B 20 49.87 -105.76
REMARK 500 ASP B 21 66.24 -55.33
REMARK 500 TYR B 119 99.56 -59.19
REMARK 500 ALA B 153 -117.47 59.40
REMARK 500 TYR B 181 65.85 24.73
REMARK 500 TYR B 201 55.84 -115.35
REMARK 500 TYR B 202 -83.80 67.27
REMARK 500 ALA B 227 -65.94 -96.91
REMARK 500 ALA A 153 -121.15 56.48
REMARK 500 TYR A 181 70.59 22.33
REMARK 500 ASN A 186 41.49 -109.65
REMARK 500 TYR A 202 -64.49 75.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR B 119 PRO B 120 95.74
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 CLM A 401
DBREF 6IEY B 1 305 UNP G3CR02 G3CR02_9BACT 1 310
DBREF 6IEY A 1 307 UNP G3CR02 G3CR02_9BACT 1 310
SEQADV 6IEY B UNP G3CR02 PRO 37 DELETION
SEQADV 6IEY B UNP G3CR02 MET 38 DELETION
SEQADV 6IEY B UNP G3CR02 PRO 39 DELETION
SEQADV 6IEY ALA B 153 UNP G3CR02 SER 156 ENGINEERED MUTATION
SEQADV 6IEY LEU B 306 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY GLU B 307 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 308 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 309 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 310 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 311 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 312 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 313 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 314 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS B 315 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY A UNP G3CR02 PRO 37 DELETION
SEQADV 6IEY A UNP G3CR02 MET 38 DELETION
SEQADV 6IEY A UNP G3CR02 PRO 39 DELETION
SEQADV 6IEY ALA A 153 UNP G3CR02 SER 156 ENGINEERED MUTATION
SEQADV 6IEY LEU A 308 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY GLU A 309 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 310 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 311 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 312 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 313 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 314 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 315 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 316 UNP G3CR02 EXPRESSION TAG
SEQADV 6IEY HIS A 317 UNP G3CR02 EXPRESSION TAG
SEQRES 1 B 317 MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET
SEQRES 2 B 317 MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN
SEQRES 3 B 317 PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA
SEQRES 4 B 317 PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER
SEQRES 5 B 317 LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO
SEQRES 6 B 317 GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR
SEQRES 7 B 317 HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS
SEQRES 8 B 317 ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS
SEQRES 9 B 317 ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR
SEQRES 10 B 317 ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU
SEQRES 11 B 317 VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP
SEQRES 12 B 317 GLY ASP ARG LEU ALA VAL GLY GLY ASP ALA ALA GLY GLY
SEQRES 13 B 317 ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG
SEQRES 14 B 317 ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO
SEQRES 15 B 317 VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU
SEQRES 16 B 317 ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET
SEQRES 17 B 317 ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA
SEQRES 18 B 317 GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP
SEQRES 19 B 317 LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU
SEQRES 20 B 317 TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS
SEQRES 21 B 317 LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR
SEQRES 22 B 317 ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU
SEQRES 23 B 317 ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA
SEQRES 24 B 317 SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS
SEQRES 25 B 317 HIS HIS HIS HIS HIS
SEQRES 1 A 317 MET PRO LEU ASN PRO HIS VAL GLU ALA LEU LEU GLN MET
SEQRES 2 A 317 MET ALA GLN MET PRO ALA PRO ASP PHE SER VAL ALA ASN
SEQRES 3 A 317 PRO ALA GLU ILE ARG ALA VAL PHE ASP ASN LEU ALA ALA
SEQRES 4 A 317 PRO PRO GLN VAL ALA ARG VAL GLU ASN ILE ALA ILE SER
SEQRES 5 A 317 LEU ASP GLY ARG ASP LEU ASP ALA ARG LEU TYR VAL PRO
SEQRES 6 A 317 GLU ASP ALA ASP GLU ARG PRO ALA LEU MET VAL TYR TYR
SEQRES 7 A 317 HIS GLY GLY GLY TRP VAL ILE GLY THR LEU ASP THR HIS
SEQRES 8 A 317 ASP GLY THR CYS ARG ALA LEU ALA GLN LYS SER GLY CYS
SEQRES 9 A 317 ALA VAL LEU SER ILE ALA TYR ARG LEU ALA PRO GLU TYR
SEQRES 10 A 317 ARG TYR PRO ALA PRO ALA GLU ASP CYS TYR ASP ALA LEU
SEQRES 11 A 317 VAL TRP ALA LYS GLN ASN ALA ALA THR LEU GLY VAL ASP
SEQRES 12 A 317 GLY ASP ARG LEU ALA VAL GLY GLY ASP ALA ALA GLY GLY
SEQRES 13 A 317 ASN LEU ALA ALA ALA VAL ALA ILE MET ALA ARG ASP ARG
SEQRES 14 A 317 ASN GLY PRO ALA LEU ARG HIS GLN LEU LEU ILE TYR PRO
SEQRES 15 A 317 VAL THR ASP ASN ASP PHE THR LEU ALA SER TYR ALA GLU
SEQRES 16 A 317 ASN GLY GLY GLY GLU TYR TYR LEU SER THR ASP GLY MET
SEQRES 17 A 317 ARG TRP PHE TRP GLY HIS TYR LEU GLY ASP THR ALA ALA
SEQRES 18 A 317 GLU ASN ALA PRO LEU ALA ALA VAL LEU ASN VAL ALA ASP
SEQRES 19 A 317 LEU SER GLY LEU ALA PRO ALA THR VAL ILE THR ALA GLU
SEQRES 20 A 317 TYR ASP PRO LEU ARG ASP GLU GLY ILE ALA TYR ALA LYS
SEQRES 21 A 317 LYS LEU ASP ALA ALA GLY VAL PRO VAL ASP ALA ALA THR
SEQRES 22 A 317 ALA PRO GLY MET ILE HIS GLY PHE PHE SER MET PHE GLU
SEQRES 23 A 317 ALA VAL PRO ASP SER TRP GLU TRP ILE GLU ARG GLY ALA
SEQRES 24 A 317 SER ASN LEU LYS ARG ASP LEU ALA LEU GLU HIS HIS HIS
SEQRES 25 A 317 HIS HIS HIS HIS HIS
HET CLM A 401 20
HETNAM CLM CHLORAMPHENICOL
FORMUL 3 CLM C11 H12 CL2 N2 O5
FORMUL 4 HOH *204(H2 O)
HELIX 1 AA1 ASN B 4 GLN B 16 1 13
HELIX 2 AA2 ASN B 26 ALA B 39 1 14
HELIX 3 AA3 HIS B 91 GLY B 103 1 13
HELIX 4 AA4 PRO B 120 ASN B 136 1 17
HELIX 5 AA5 ASN B 136 GLY B 141 1 6
HELIX 6 AA6 ALA B 153 ARG B 169 1 17
HELIX 7 AA7 LEU B 190 GLY B 197 1 8
HELIX 8 AA8 SER B 204 GLY B 217 1 14
HELIX 9 AA9 ALA B 220 ALA B 224 5 5
HELIX 10 AB1 ALA B 228 VAL B 232 5 5
HELIX 11 AB2 LEU B 251 ALA B 265 1 15
HELIX 12 AB3 GLY B 278 PHE B 283 5 6
HELIX 13 AB4 ASP B 288 LEU B 304 1 17
HELIX 14 AB5 ASN A 4 GLN A 16 1 13
HELIX 15 AB6 ALA A 28 ASP A 35 1 8
HELIX 16 AB7 HIS A 91 GLY A 103 1 13
HELIX 17 AB8 PRO A 120 ASN A 136 1 17
HELIX 18 AB9 ASN A 136 GLY A 141 1 6
HELIX 19 AC1 ALA A 153 ARG A 169 1 17
HELIX 20 AC2 LEU A 190 GLY A 197 1 8
HELIX 21 AC3 SER A 204 GLY A 217 1 14
HELIX 22 AC4 ALA A 220 ALA A 224 5 5
HELIX 23 AC5 ALA A 228 VAL A 232 5 5
HELIX 24 AC6 LEU A 251 ALA A 265 1 15
HELIX 25 AC7 GLY A 280 PHE A 285 5 6
HELIX 26 AC8 ASP A 290 LEU A 306 1 17
SHEET 1 AA1 8 ARG B 45 LEU B 53 0
SHEET 2 AA1 8 ARG B 56 VAL B 64 -1 O VAL B 64 N ARG B 45
SHEET 3 AA1 8 ALA B 105 ILE B 109 -1 O SER B 108 N ARG B 61
SHEET 4 AA1 8 ALA B 73 TYR B 78 1 N TYR B 77 O LEU B 107
SHEET 5 AA1 8 ASP B 143 ASP B 152 1 O ALA B 148 N VAL B 76
SHEET 6 AA1 8 LEU B 174 ILE B 180 1 O ARG B 175 N LEU B 147
SHEET 7 AA1 8 ALA B 241 ALA B 246 1 O THR B 242 N LEU B 179
SHEET 8 AA1 8 VAL B 269 ALA B 272 1 O ALA B 272 N THR B 245
SHEET 1 AA2 8 ARG A 45 SER A 52 0
SHEET 2 AA2 8 ASP A 57 VAL A 64 -1 O LEU A 58 N ILE A 51
SHEET 3 AA2 8 ALA A 105 ILE A 109 -1 O SER A 108 N ARG A 61
SHEET 4 AA2 8 LEU A 74 TYR A 78 1 N MET A 75 O LEU A 107
SHEET 5 AA2 8 LEU A 147 ASP A 152 1 O ALA A 148 N VAL A 76
SHEET 6 AA2 8 HIS A 176 ILE A 180 1 O ILE A 180 N GLY A 151
SHEET 7 AA2 8 ALA A 241 ALA A 246 1 O THR A 242 N LEU A 179
SHEET 8 AA2 8 VAL A 269 ALA A 274 1 O ASP A 270 N VAL A 243
CISPEP 1 ALA B 114 PRO B 115 0 -2.74
CISPEP 2 ALA A 114 PRO A 115 0 1.27
CISPEP 3 TYR A 119 PRO A 120 0 5.33
SITE 1 AC1 11 HIS A 91 ASP A 152 TYR A 181 TYR A 202
SITE 2 AC1 11 LEU A 203 HIS A 279 GLY A 280 SER A 283
SITE 3 AC1 11 HOH A 542 PHE B 34 ALA B 38
CRYST1 118.463 152.411 44.137 90.00 90.00 90.00 P 21 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 0.008441 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022657 0.00000
TER 2327 GLU B 307
TER 4645 HIS A 314
MASTER 317 0 1 26 16 0 3 6 4867 2 20 50
END |