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HEADER HYDROLASE 17-FEB-23 8CLT
TITLE ZEARALENONE LACTONASE OF RHODOCOCCUS ERYTHROPOLIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE LACTONASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS ERYTHROPOLIS;
SOURCE 3 ORGANISM_TAXID: 1833;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ZEARALENONE, MYCOTOXIN, LACTONASE, CARBOXYLESTERASE, ESTERASE,
KEYWDS 2 HYDROLASE, BIODEGRADATION, RHODOCOCCUS ERYTHROPOLIS
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PUEHRINGER,G.MLYNEK
REVDAT 1 21-FEB-24 8CLT 0
JRNL AUTH S.FRUHAUF,D.PUEHRINGER,M.THAMHESL,P.FAJTL,E.KUNZ-VEKIRO,
JRNL AUTH 2 A.HOEBARTNER-GUSSL,J.PANHOELZL,K.PREM,V.KLINGENBRUNNER,
JRNL AUTH 3 G.SCHATZMAYR,G.ADAM,J.DAMBORSKY,K.DJINOVIC-CARUGO,Z.PROKOP,
JRNL AUTH 4 W.D.MOLL
JRNL TITL BACTERIAL LACTONASES ZENA WITH NONCANONICAL STRUCTURAL
JRNL TITL 2 FEATURES HYDROLYSE THE MYCOTOXIN ZEARALENONE
JRNL REF ACS CATALYSIS 2024
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.4C00271
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 109245
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.730
REMARK 3 FREE R VALUE TEST SET COUNT : 1895
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 47.5300 - 3.5200 1.00 8588 153 0.1447 0.1687
REMARK 3 2 3.5200 - 2.7900 1.00 8319 154 0.1373 0.1579
REMARK 3 3 2.7900 - 2.4400 1.00 8298 149 0.1354 0.1753
REMARK 3 4 2.4400 - 2.2200 1.00 8251 138 0.1365 0.1701
REMARK 3 5 2.2200 - 2.0600 1.00 8260 153 0.1375 0.2034
REMARK 3 6 2.0600 - 1.9400 1.00 8191 144 0.1493 0.2212
REMARK 3 7 1.9400 - 1.8400 1.00 8229 140 0.1861 0.2434
REMARK 3 8 1.8400 - 1.7600 1.00 8181 146 0.2383 0.2617
REMARK 3 9 1.7600 - 1.6900 1.00 8196 140 0.2492 0.3203
REMARK 3 10 1.6900 - 1.6300 1.00 8182 141 0.2746 0.3065
REMARK 3 11 1.6300 - 1.5800 1.00 8155 149 0.3055 0.3671
REMARK 3 12 1.5800 - 1.5400 0.95 7786 141 0.3668 0.3878
REMARK 3 13 1.5400 - 1.5000 0.79 6466 105 0.4362 0.4605
REMARK 3 14 1.5000 - 1.4600 0.28 2248 42 0.5025 0.4459
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.58
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 : 0.009 5003
REMARK 3 ANGLE : 1.014 6813
REMARK 3 CHIRALITY : 0.081 717
REMARK 3 PLANARITY : 0.017 895
REMARK 3 DIHEDRAL : 7.486 682
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 8CLT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1292126826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976250
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114638
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 47.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.10140
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 39.3
REMARK 200 DATA REDUNDANCY IN SHELL : 0.18
REMARK 200 R MERGE FOR SHELL (I) : 4.67700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.180
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M BIS-TRIS 5.5 PH, 25%
REMARK 280 W/V PEG 3350, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 86.17800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.17800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.23350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.90150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.23350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.90150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 86.17800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.23350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.90150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 86.17800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.23350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.90150
REMARK 290 SMTRY3 8 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 APPLY THE FOLLOWING TO CHAINS: A, 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 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 761 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 680 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 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 ARG A 7
REMARK 465 SER A 8
REMARK 465 GLU A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 ASP A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 THR A 15
REMARK 465 GLN A 16
REMARK 465 ALA A 17
REMARK 465 ARG A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 PRO A 21
REMARK 465 ASP A 22
REMARK 465 SER A 23
REMARK 465 ARG A 24
REMARK 465 ASN A 25
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 GLY B 5
REMARK 465 THR B 6
REMARK 465 ARG B 7
REMARK 465 SER B 8
REMARK 465 GLU B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 ASP B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 THR B 15
REMARK 465 GLN B 16
REMARK 465 ALA B 17
REMARK 465 ARG B 18
REMARK 465 GLN B 19
REMARK 465 LEU B 20
REMARK 465 PRO B 21
REMARK 465 ASP B 22
REMARK 465 ASN B 327
REMARK 465 ASP B 328
REMARK 465 HIS B 329
REMARK 465 HIS B 330
REMARK 465 HIS B 331
REMARK 465 HIS B 332
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 SER B 23 OG
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 THR A 64 -2.06 76.06
REMARK 500 SER A 128 -125.15 62.75
REMARK 500 PHE A 157 -53.05 73.63
REMARK 500 ALA A 172 -104.28 -137.92
REMARK 500 HIS A 259 -150.23 -91.86
REMARK 500 ASN B 25 41.17 -143.32
REMARK 500 THR B 64 -4.45 77.63
REMARK 500 SER B 128 -123.21 58.98
REMARK 500 PHE B 157 -53.21 71.09
REMARK 500 ALA B 172 -101.72 -143.92
REMARK 500 HIS B 259 -147.07 -92.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 35 0.19 SIDE CHAIN
REMARK 500 ARG B 35 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8CLT A 1 332 PDB 8CLT 8CLT 1 332
DBREF 8CLT B 1 332 PDB 8CLT 8CLT 1 332
SEQRES 1 A 332 MET ALA GLU GLU GLY THR ARG SER GLU ALA ALA ASP ALA
SEQRES 2 A 332 ALA THR GLN ALA ARG GLN LEU PRO ASP SER ARG ASN ILE
SEQRES 3 A 332 PHE VAL SER HIS ARG PHE PRO GLU ARG GLN VAL ASP LEU
SEQRES 4 A 332 GLY GLU VAL VAL MET ASN PHE ALA GLU ALA GLY SER PRO
SEQRES 5 A 332 ASP ASN PRO ALA LEU LEU LEU LEU PRO GLU GLN THR GLY
SEQRES 6 A 332 SER TRP TRP SER TYR GLU PRO VAL MET GLY LEU LEU ALA
SEQRES 7 A 332 GLU ASN PHE HIS VAL PHE ALA VAL ASP ILE ARG GLY GLN
SEQRES 8 A 332 GLY ARG SER THR TRP THR PRO ARG ARG TYR SER LEU ASP
SEQRES 9 A 332 ASN PHE GLY ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL
SEQRES 10 A 332 ILE LYS ARG PRO VAL VAL VAL ALA GLY ASN SER SER GLY
SEQRES 11 A 332 GLY LEU LEU ALA ALA TRP LEU SER ALA TYR ALA MET PRO
SEQRES 12 A 332 GLY GLN ILE ARG ALA ALA LEU CYS GLU ASP ALA PRO PHE
SEQRES 13 A 332 PHE ALA SER GLU LEU VAL PRO ALA TYR GLY HIS SER VAL
SEQRES 14 A 332 LEU GLN ALA ALA GLY PRO ALA PHE GLU LEU TYR ARG ASP
SEQRES 15 A 332 PHE LEU GLY ASP GLN TRP SER ILE GLY ASP TRP LYS GLY
SEQRES 16 A 332 PHE VAL GLU ALA ALA LYS ALA SER PRO ALA LYS ALA MET
SEQRES 17 A 332 GLN LEU PHE PRO THR PRO ASP GLU ALA PRO GLN ASN LEU
SEQRES 18 A 332 LYS GLU TYR ASP PRO GLU TRP GLY ARG ALA PHE PHE GLU
SEQRES 19 A 332 GLY THR VAL ALA LEU HIS CYS PRO HIS ASP ARG MET LEU
SEQRES 20 A 332 SER GLN VAL LYS THR PRO ILE LEU ILE THR HIS HIS ALA
SEQRES 21 A 332 ARG THR ILE ASP PRO GLU THR GLY GLU LEU LEU GLY ALA
SEQRES 22 A 332 LEU SER ASP LEU GLN ALA GLU HIS ALA GLN ASP ILE ILE
SEQRES 23 A 332 ARG SER ALA GLY VAL ARG VAL ASP TYR GLN SER HIS PRO
SEQRES 24 A 332 ASP ALA LEU HIS MET MET HIS LEU PHE ASP PRO ALA ARG
SEQRES 25 A 332 TYR ALA GLU ILE LEU THR SER TRP SER ALA THR LEU PRO
SEQRES 26 A 332 ALA ASN ASP HIS HIS HIS HIS
SEQRES 1 B 332 MET ALA GLU GLU GLY THR ARG SER GLU ALA ALA ASP ALA
SEQRES 2 B 332 ALA THR GLN ALA ARG GLN LEU PRO ASP SER ARG ASN ILE
SEQRES 3 B 332 PHE VAL SER HIS ARG PHE PRO GLU ARG GLN VAL ASP LEU
SEQRES 4 B 332 GLY GLU VAL VAL MET ASN PHE ALA GLU ALA GLY SER PRO
SEQRES 5 B 332 ASP ASN PRO ALA LEU LEU LEU LEU PRO GLU GLN THR GLY
SEQRES 6 B 332 SER TRP TRP SER TYR GLU PRO VAL MET GLY LEU LEU ALA
SEQRES 7 B 332 GLU ASN PHE HIS VAL PHE ALA VAL ASP ILE ARG GLY GLN
SEQRES 8 B 332 GLY ARG SER THR TRP THR PRO ARG ARG TYR SER LEU ASP
SEQRES 9 B 332 ASN PHE GLY ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL
SEQRES 10 B 332 ILE LYS ARG PRO VAL VAL VAL ALA GLY ASN SER SER GLY
SEQRES 11 B 332 GLY LEU LEU ALA ALA TRP LEU SER ALA TYR ALA MET PRO
SEQRES 12 B 332 GLY GLN ILE ARG ALA ALA LEU CYS GLU ASP ALA PRO PHE
SEQRES 13 B 332 PHE ALA SER GLU LEU VAL PRO ALA TYR GLY HIS SER VAL
SEQRES 14 B 332 LEU GLN ALA ALA GLY PRO ALA PHE GLU LEU TYR ARG ASP
SEQRES 15 B 332 PHE LEU GLY ASP GLN TRP SER ILE GLY ASP TRP LYS GLY
SEQRES 16 B 332 PHE VAL GLU ALA ALA LYS ALA SER PRO ALA LYS ALA MET
SEQRES 17 B 332 GLN LEU PHE PRO THR PRO ASP GLU ALA PRO GLN ASN LEU
SEQRES 18 B 332 LYS GLU TYR ASP PRO GLU TRP GLY ARG ALA PHE PHE GLU
SEQRES 19 B 332 GLY THR VAL ALA LEU HIS CYS PRO HIS ASP ARG MET LEU
SEQRES 20 B 332 SER GLN VAL LYS THR PRO ILE LEU ILE THR HIS HIS ALA
SEQRES 21 B 332 ARG THR ILE ASP PRO GLU THR GLY GLU LEU LEU GLY ALA
SEQRES 22 B 332 LEU SER ASP LEU GLN ALA GLU HIS ALA GLN ASP ILE ILE
SEQRES 23 B 332 ARG SER ALA GLY VAL ARG VAL ASP TYR GLN SER HIS PRO
SEQRES 24 B 332 ASP ALA LEU HIS MET MET HIS LEU PHE ASP PRO ALA ARG
SEQRES 25 B 332 TYR ALA GLU ILE LEU THR SER TRP SER ALA THR LEU PRO
SEQRES 26 B 332 ALA ASN ASP HIS HIS HIS HIS
HET GOL A 401 12
HET GOL A 402 14
HET GOL A 403 13
HET GOL A 404 14
HET GOL A 405 13
HET GOL B 401 14
HET GOL B 402 14
HET GOL B 403 13
HET GOL B 404 14
HET GOL B 405 12
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 10(C3 H8 O3)
FORMUL 13 HOH *569(H2 O)
HELIX 1 AA1 SER A 66 SER A 69 5 4
HELIX 2 AA2 TYR A 70 GLU A 79 1 10
HELIX 3 AA3 SER A 102 VAL A 117 1 16
HELIX 4 AA4 SER A 128 ALA A 141 1 14
HELIX 5 AA5 SER A 168 ALA A 172 5 5
HELIX 6 AA6 ALA A 173 LEU A 184 1 12
HELIX 7 AA7 GLY A 185 SER A 189 5 5
HELIX 8 AA8 ASP A 192 SER A 203 1 12
HELIX 9 AA9 ALA A 205 GLN A 209 5 5
HELIX 10 AB1 PRO A 218 GLU A 223 1 6
HELIX 11 AB2 PRO A 226 GLU A 234 1 9
HELIX 12 AB3 PRO A 242 GLN A 249 1 8
HELIX 13 AB4 SER A 275 ALA A 289 1 15
HELIX 14 AB5 MET A 304 ASP A 309 1 6
HELIX 15 AB6 ASP A 309 ALA A 322 1 14
HELIX 16 AB7 ASN A 327 HIS A 331 5 5
HELIX 17 AB8 SER B 66 SER B 69 5 4
HELIX 18 AB9 TYR B 70 ALA B 78 1 9
HELIX 19 AC1 SER B 102 VAL B 117 1 16
HELIX 20 AC2 SER B 128 ALA B 141 1 14
HELIX 21 AC3 SER B 168 ALA B 172 5 5
HELIX 22 AC4 ALA B 173 LEU B 184 1 12
HELIX 23 AC5 GLY B 185 SER B 189 5 5
HELIX 24 AC6 ASP B 192 SER B 203 1 12
HELIX 25 AC7 ALA B 205 GLN B 209 5 5
HELIX 26 AC8 PRO B 218 GLU B 223 1 6
HELIX 27 AC9 PRO B 226 GLU B 234 1 9
HELIX 28 AD1 PRO B 242 GLN B 249 1 8
HELIX 29 AD2 SER B 275 ALA B 289 1 15
HELIX 30 AD3 MET B 304 ASP B 309 1 6
HELIX 31 AD4 ASP B 309 ALA B 322 1 14
SHEET 1 AA1 8 GLU A 34 ASP A 38 0
SHEET 2 AA1 8 VAL A 43 ALA A 49 -1 O MET A 44 N VAL A 37
SHEET 3 AA1 8 HIS A 82 VAL A 86 -1 O ALA A 85 N ALA A 47
SHEET 4 AA1 8 ALA A 56 LEU A 60 1 N LEU A 59 O PHE A 84
SHEET 5 AA1 8 VAL A 122 ASN A 127 1 O ALA A 125 N LEU A 58
SHEET 6 AA1 8 ILE A 146 GLU A 152 1 O ARG A 147 N VAL A 122
SHEET 7 AA1 8 ILE A 254 HIS A 258 1 O LEU A 255 N CYS A 151
SHEET 8 AA1 8 VAL A 293 SER A 297 1 O ASP A 294 N ILE A 256
SHEET 1 AA2 2 ARG A 261 ILE A 263 0
SHEET 2 AA2 2 LEU A 270 GLY A 272 -1 O LEU A 271 N THR A 262
SHEET 1 AA3 8 GLU B 34 ASP B 38 0
SHEET 2 AA3 8 VAL B 43 ALA B 49 -1 O PHE B 46 N ARG B 35
SHEET 3 AA3 8 HIS B 82 VAL B 86 -1 O ALA B 85 N ALA B 47
SHEET 4 AA3 8 ALA B 56 LEU B 60 1 N LEU B 57 O PHE B 84
SHEET 5 AA3 8 VAL B 122 ASN B 127 1 O VAL B 123 N LEU B 58
SHEET 6 AA3 8 ILE B 146 GLU B 152 1 O ARG B 147 N VAL B 122
SHEET 7 AA3 8 ILE B 254 HIS B 258 1 O LEU B 255 N CYS B 151
SHEET 8 AA3 8 VAL B 293 SER B 297 1 O ASP B 294 N ILE B 256
SHEET 1 AA4 2 ARG B 261 ILE B 263 0
SHEET 2 AA4 2 LEU B 270 GLY B 272 -1 O LEU B 271 N THR B 262
CRYST1 64.467 121.803 172.356 90.00 90.00 90.00 C 2 2 21 16
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 0.015512 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008210 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005802 0.00000
TER 4717 HIS A 332
TER 9413 ALA B 326
MASTER 338 0 10 31 20 0 0 6 5415 2 133 52
END |