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HEADER HYDROLASE 11-NOV-21 7VWN
TITLE THE STRUCTURE OF AN ENGINEERED PET HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PET HYDROLASE,PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN NBRC 110686 /
SOURCE 3 TISTR 2288 / 201-F6);
SOURCE 4 ORGANISM_TAXID: 1547922;
SOURCE 5 STRAIN: NBRC 110686 / TISTR 2288 / 201-F6;
SOURCE 6 GENE: ISF6_4831;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE, PETASE, BIODEGRADATION OF MICROPLASTICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XIE,Q.JIA
REVDAT 1 16-NOV-22 7VWN 0
JRNL AUTH W.XIE,Q.JIA
JRNL TITL AN ENGINEERED PET HYDROLASE FOR BIODEGRADATION OF
JRNL TITL 2 MICROPLASTICS IN OCEAN WATER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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 : CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 41548
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.210
REMARK 3 FREE R VALUE TEST SET COUNT : 2165
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 32.9500 - 3.5800 1.00 2753 152 0.1449 0.1750
REMARK 3 2 3.5800 - 2.8400 1.00 2654 157 0.1424 0.1617
REMARK 3 3 2.8400 - 2.4800 1.00 2691 147 0.1494 0.1585
REMARK 3 4 2.4800 - 2.2600 1.00 2639 149 0.1498 0.1617
REMARK 3 5 2.2600 - 2.1000 0.99 2668 137 0.1496 0.1810
REMARK 3 6 2.1000 - 1.9700 0.99 2629 139 0.1518 0.1685
REMARK 3 7 1.9700 - 1.8700 0.99 2639 140 0.1583 0.1871
REMARK 3 8 1.8700 - 1.7900 0.99 2624 148 0.1588 0.1853
REMARK 3 9 1.7900 - 1.7200 0.99 2615 131 0.1642 0.2110
REMARK 3 10 1.7200 - 1.6600 0.99 2629 133 0.1750 0.1985
REMARK 3 11 1.6600 - 1.6100 0.98 2603 155 0.1796 0.2014
REMARK 3 12 1.6100 - 1.5600 0.98 2591 142 0.1870 0.2274
REMARK 3 13 1.5600 - 1.5200 0.98 2576 161 0.1859 0.2252
REMARK 3 14 1.5200 - 1.4900 0.98 2582 141 0.1984 0.2527
REMARK 3 15 1.4900 - 1.4500 0.94 2490 133 0.2170 0.2555
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) : 0.126
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.451
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.81
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 : 0.014 1985
REMARK 3 ANGLE : 1.392 2711
REMARK 3 CHIRALITY : 0.124 300
REMARK 3 PLANARITY : 0.011 359
REMARK 3 DIHEDRAL : 3.969 1102
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3143 0.0270 11.5592
REMARK 3 T TENSOR
REMARK 3 T11: 0.1328 T22: 0.1151
REMARK 3 T33: 0.0771 T12: 0.0205
REMARK 3 T13: 0.0076 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.5741 L22: 1.3950
REMARK 3 L33: 1.1490 L12: -0.2023
REMARK 3 L13: 0.4371 L23: -0.1088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0626 S12: 0.3325 S13: -0.0260
REMARK 3 S21: -0.2348 S22: -0.0596 S23: 0.0199
REMARK 3 S31: -0.0373 S32: -0.0402 S33: -0.0080
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 7VWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1300024908.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD ONYX CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42326
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
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 (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 6EQE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M (NH4)2SO4, 0.1 M NACL AND 0.1 M
REMARK 280 MES PH6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 57.79400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.26800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.79400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.26800
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 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 644 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 662 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 GLU A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
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 ARG A 59 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 O HOH A 404 O HOH A 604 1.99
REMARK 500 O HOH A 408 O HOH A 516 2.00
REMARK 500 O HOH A 634 O HOH A 649 2.11
REMARK 500 OD1 ASP A 186 O HOH A 401 2.15
REMARK 500 O HOH A 402 O HOH A 647 2.16
REMARK 500 OG1 THR A 189 O HOH A 402 2.16
REMARK 500 O HOH A 416 O HOH A 550 2.17
REMARK 500 O HOH A 515 O HOH A 669 2.19
REMARK 500 OE2 GLU A 274 O HOH A 403 2.19
REMARK 500 O HOH A 481 O HOH A 601 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 ASP A 248 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU A 249 CA - CB - CG ANGL. DEV. = -16.5 DEGREES
REMARK 500 MET A 258 CG - SD - CE ANGL. DEV. = -10.7 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 THR A 88 -8.73 75.04
REMARK 500 SER A 160 -124.07 61.98
REMARK 500 VAL A 214 -65.51 -125.29
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 123 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7VWN A 29 290 UNP PETH_IDESA
DBREF2 7VWN A A0A0K8P6T7 29 290
SEQADV 7VWN SER A 29 UNP A0A0K8P6T THR 29 ENGINEERED MUTATION
SEQADV 7VWN ASN A 95 UNP A0A0K8P6T LYS 95 ENGINEERED MUTATION
SEQADV 7VWN ARG A 168 UNP A0A0K8P6T ILE 168 ENGINEERED MUTATION
SEQADV 7VWN VAL A 181 UNP A0A0K8P6T PRO 181 ENGINEERED MUTATION
SEQADV 7VWN VAL A 214 UNP A0A0K8P6T SER 214 ENGINEERED MUTATION
SEQADV 7VWN CYS A 233 UNP A0A0K8P6T ASN 233 ENGINEERED MUTATION
SEQADV 7VWN ASP A 248 UNP A0A0K8P6T ALA 248 ENGINEERED MUTATION
SEQADV 7VWN ALA A 280 UNP A0A0K8P6T ARG 280 ENGINEERED MUTATION
SEQADV 7VWN CYS A 282 UNP A0A0K8P6T SER 282 ENGINEERED MUTATION
SEQADV 7VWN LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7VWN GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7VWN HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7VWN HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7VWN HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7VWN HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7VWN HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7VWN HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 270 SER ASN PRO TYR ALA ARG GLY PRO ASN PRO THR ALA ALA
SEQRES 2 A 270 SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER
SEQRES 3 A 270 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 A 270 VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA
SEQRES 5 A 270 ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER
SEQRES 6 A 270 ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 A 270 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 A 270 PRO SER SER ARG SER SER GLN GLN MET ALA ALA LEU ARG
SEQRES 9 A 270 GLN VAL ALA SER LEU ASN GLY THR SER SER SER PRO ILE
SEQRES 10 A 270 TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY
SEQRES 11 A 270 TRP SER MET GLY GLY GLY GLY SER LEU ARG SER ALA ALA
SEQRES 12 A 270 ASN ASN PRO SER LEU LYS ALA ALA ALA VAL GLN ALA PRO
SEQRES 13 A 270 TRP ASP SER SER THR ASN PHE SER SER VAL THR VAL PRO
SEQRES 14 A 270 THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO
SEQRES 15 A 270 VAL ASN SER VAL ALA LEU PRO ILE TYR ASP SER MET SER
SEQRES 16 A 270 ARG ASN ALA LYS GLN PHE LEU GLU ILE CYS GLY GLY SER
SEQRES 17 A 270 HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ASP LEU
SEQRES 18 A 270 ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET
SEQRES 19 A 270 ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN
SEQRES 20 A 270 PRO ASN SER THR ALA VAL CYS ASP PHE ARG THR ALA ASN
SEQRES 21 A 270 CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET CL A 302 1
HET CL A 303 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL 3(CL 1-)
FORMUL 5 HOH *282(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 ASN A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 VAL A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
SHEET 1 AA1 9 VAL A 52 THR A 56 0
SHEET 2 AA1 9 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 9 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 9 VAL A 78 VAL A 84 1 N ILE A 81 O ILE A 109
SHEET 5 AA1 9 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 9 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 7 AA1 9 THR A 198 CYS A 203 1 O LEU A 199 N VAL A 181
SHEET 8 AA1 9 LYS A 227 ILE A 232 1 O ILE A 232 N ALA A 202
SHEET 9 AA1 9 VAL A 281 ALA A 287 -1 O CYS A 282 N GLU A 231
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.03
SSBOND 2 CYS A 233 CYS A 282 1555 1555 2.03
SSBOND 3 CYS A 273 CYS A 289 1555 1555 2.01
CRYST1 115.588 50.536 41.370 90.00 92.46 90.00 C 1 2 1 4
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 0.008651 0.000000 0.000371 0.00000
SCALE2 0.000000 0.019788 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024194 0.00000
TER 1937 LEU A 291
MASTER 327 0 3 9 9 0 0 6 2209 1 6 21
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