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HEADER HYDROLASE 09-SEP-22 8GU5
TITLE WILD TYPE POLY(ETHYLENE TEREPHTHALATE) 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
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 BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PETASE, LYASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.J.XIAO,Z.F.WANG
REVDAT 1 30-NOV-22 8GU5 0
JRNL AUTH Z.CHEN,R.DUAN,Y.XIAO,Y.WEI,H.ZHANG,X.SUN,S.WANG,Y.CHENG,
JRNL AUTH 2 X.WANG,S.TONG,Y.YAO,C.ZHU,H.YANG,Y.WANG,Z.WANG
JRNL TITL BIODEGRADATION OF HIGHLY CRYSTALLIZED POLY(ETHYLENE
JRNL TITL 2 TEREPHTHALATE) THROUGH CELL SURFACE CODISPLAY OF BACTERIAL
JRNL TITL 3 PETASE AND HYDROPHOBIN.
JRNL REF NAT COMMUN V. 13 7138 2022
JRNL REFN ESSN 2041-1723
JRNL PMID 36414665
JRNL DOI 10.1038/S41467-022-34908-Z
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19_4092
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) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 16367
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 841
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 46.5200 - 3.6700 0.99 2717 174 0.1639 0.1921
REMARK 3 2 3.6700 - 2.9100 1.00 2631 133 0.1709 0.1939
REMARK 3 3 2.9100 - 2.5500 1.00 2607 150 0.1812 0.2530
REMARK 3 4 2.5500 - 2.3100 1.00 2586 142 0.1937 0.2677
REMARK 3 5 2.3100 - 2.1500 1.00 2594 116 0.2142 0.2861
REMARK 3 6 2.1500 - 2.0200 0.92 2391 126 0.2245 0.2829
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.22
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5095 20.7846 43.1038
REMARK 3 T TENSOR
REMARK 3 T11: 0.1872 T22: 0.1540
REMARK 3 T33: 0.2028 T12: -0.0026
REMARK 3 T13: -0.0088 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 1.9594 L22: 1.7046
REMARK 3 L33: 2.3005 L12: -0.2714
REMARK 3 L13: -0.6214 L23: 1.0132
REMARK 3 S TENSOR
REMARK 3 S11: -0.0288 S12: -0.0128 S13: -0.1671
REMARK 3 S21: 0.0747 S22: -0.0372 S23: -0.0586
REMARK 3 S31: 0.2341 S32: 0.1168 S33: 0.0755
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8464 31.0378 43.8301
REMARK 3 T TENSOR
REMARK 3 T11: 0.1884 T22: 0.2045
REMARK 3 T33: 0.1310 T12: -0.0012
REMARK 3 T13: 0.0166 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 2.2450 L22: 3.6646
REMARK 3 L33: 1.3127 L12: -0.9055
REMARK 3 L13: 0.1226 L23: 0.7231
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.0164 S13: 0.0491
REMARK 3 S21: 0.1521 S22: -0.0659 S23: 0.1416
REMARK 3 S31: -0.0383 S32: -0.2827 S33: 0.0754
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 94 THROUGH 113 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5130 37.0704 45.6123
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.2286
REMARK 3 T33: 0.1363 T12: -0.0299
REMARK 3 T13: 0.0225 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 5.0372 L22: 3.9757
REMARK 3 L33: 2.7906 L12: -2.8062
REMARK 3 L13: 1.5964 L23: -1.8701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0676 S12: 0.3803 S13: -0.0110
REMARK 3 S21: 0.0540 S22: -0.0966 S23: 0.0247
REMARK 3 S31: -0.1403 S32: 0.3659 S33: 0.0497
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 114 THROUGH 220 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6767 33.9472 32.1237
REMARK 3 T TENSOR
REMARK 3 T11: 0.2234 T22: 0.2075
REMARK 3 T33: 0.2255 T12: 0.0048
REMARK 3 T13: 0.0178 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.0046 L22: 1.1413
REMARK 3 L33: 2.4382 L12: 0.1128
REMARK 3 L13: 0.2178 L23: -0.2377
REMARK 3 S TENSOR
REMARK 3 S11: -0.0542 S12: 0.0675 S13: 0.0284
REMARK 3 S21: -0.0002 S22: 0.0560 S23: 0.0718
REMARK 3 S31: 0.0034 S32: -0.0999 S33: 0.0169
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 221 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7988 20.4401 29.2235
REMARK 3 T TENSOR
REMARK 3 T11: 0.2065 T22: 0.1662
REMARK 3 T33: 0.1888 T12: 0.0011
REMARK 3 T13: 0.0045 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 5.8133 L22: 1.4264
REMARK 3 L33: 1.3136 L12: -1.1075
REMARK 3 L13: -0.2236 L23: -0.4004
REMARK 3 S TENSOR
REMARK 3 S11: 0.1974 S12: 0.1924 S13: -0.0855
REMARK 3 S21: -0.0069 S22: -0.1294 S23: -0.1005
REMARK 3 S31: 0.1239 S32: 0.1540 S33: -0.0967
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 248 THROUGH 264 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.9251 24.1235 20.0602
REMARK 3 T TENSOR
REMARK 3 T11: 0.2858 T22: 0.3235
REMARK 3 T33: 0.2350 T12: 0.0095
REMARK 3 T13: 0.0245 T23: -0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 7.1272 L22: 5.8919
REMARK 3 L33: 3.1465 L12: 1.0025
REMARK 3 L13: -0.5527 L23: -0.4443
REMARK 3 S TENSOR
REMARK 3 S11: 0.0963 S12: -0.1748 S13: -0.0561
REMARK 3 S21: -0.2561 S22: 0.0310 S23: -0.1018
REMARK 3 S31: 0.2854 S32: 0.0157 S33: -0.1634
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 8GU5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1300032141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97861
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16412
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.17200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.88800
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: PHENIX
REMARK 200 STARTING MODEL: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM CHLORIDE DIHYDRATE, 0.1
REMARK 280 M HEPES SODIUM PH 7.5, 28 % V/V POLYETHYLENE GLYCOL 400, BATCH
REMARK 280 MODE, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.71900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.72900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.72700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.72900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.71900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.72700
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 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 465 LEU A 265
REMARK 465 GLU A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
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 ASN A 47 51.27 -143.03
REMARK 500 THR A 62 -3.58 70.42
REMARK 500 SER A 134 -119.89 64.50
REMARK 500 SER A 188 -71.42 -136.70
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8GU5 A 2 264 UNP PETH_IDESA
DBREF2 8GU5 A A0A0K8P6T7 28 290
SEQADV 8GU5 MET A 1 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 8GU5 LEU A 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU5 GLU A 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU5 HIS A 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU5 HIS A 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU5 HIS A 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU5 HIS A 270 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU5 HIS A 271 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 8GU5 HIS A 272 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 A 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 A 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 A 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 A 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 A 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 A 272 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 A 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 A 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 A 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 A 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 A 272 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 A 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 A 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 A 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 A 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *159(H2 O)
HELIX 1 AA1 THR A 13 ALA A 19 1 7
HELIX 2 AA2 ARG A 64 LYS A 69 5 6
HELIX 3 AA3 TRP A 70 SER A 77 1 8
HELIX 4 AA4 GLN A 93 GLY A 113 1 21
HELIX 5 AA5 SER A 134 ASN A 147 1 14
HELIX 6 AA6 SER A 188 MET A 196 1 9
HELIX 7 AA7 ASN A 220 ASP A 237 1 18
HELIX 8 AA8 ASP A 239 ARG A 241 5 3
HELIX 9 AA9 TYR A 242 GLU A 248 1 7
SHEET 1 AA1 6 VAL A 26 THR A 30 0
SHEET 2 AA1 6 ALA A 39 PRO A 45 -1 O VAL A 42 N PHE A 29
SHEET 3 AA1 6 VAL A 81 ASP A 86 -1 O VAL A 82 N TYR A 43
SHEET 4 AA1 6 VAL A 52 VAL A 58 1 N ILE A 55 O ILE A 83
SHEET 5 AA1 6 VAL A 123 TRP A 133 1 O ASP A 124 N VAL A 52
SHEET 6 AA1 6 ALA A 152 GLN A 156 1 O GLN A 156 N GLY A 132
SHEET 1 AA2 3 THR A 172 CYS A 177 0
SHEET 2 AA2 3 LYS A 201 ILE A 206 1 O ILE A 206 N ALA A 176
SHEET 3 AA2 3 VAL A 255 ALA A 261 -1 O ARG A 259 N PHE A 203
SSBOND 1 CYS A 177 CYS A 213 1555 1555 2.05
CRYST1 51.438 55.454 85.458 90.00 90.00 90.00 P 21 21 21 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 0.019441 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018033 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011702 0.00000
TER 1935 SER A 264
MASTER 320 0 0 9 9 0 0 6 2093 1 2 21
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