| content |
HEADER HYDROLASE 18-MAY-22 7XTW
TITLE THE STRUCTURE OF ISPETASE IN COMPLEX WITH MHET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PETASE;
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;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PET HYDROLASE, PBAT HYDROLASE, ENZYME ENGINEERING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YANG,P.C.JIANG,J.-W.HUANG,C.-C.CHEN,R.-T.GUO
REVDAT 1 29-MAR-23 7XTW 0
JRNL AUTH Y.YANG,P.C.JIANG,J.-W.HUANG,C.-C.CHEN,R.-T.GUO
JRNL TITL COMPLETE BIO-DEGRADATION OF POLY(BUTYLENE
JRNL TITL 2 ADIPATE-CO-TEREPHTHALATE) VIA ENGINEERED CUTINASES
JRNL REF NAT COMMUN
JRNL REFN ESSN 2041-1723
JRNL DOI HTTPS://DOI.ORG/10.1038/S41467-023-37374-3
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 32588
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.149
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3285
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 35.9700 - 5.4300 0.99 1274 144 0.1909 0.1502
REMARK 3 2 5.4200 - 4.3100 1.00 1265 156 0.1327 0.1389
REMARK 3 3 4.3100 - 3.7700 1.00 1287 136 0.1223 0.1333
REMARK 3 4 3.7600 - 3.4200 1.00 1256 142 0.1190 0.1210
REMARK 3 5 3.4200 - 3.1800 1.00 1286 137 0.1290 0.1250
REMARK 3 6 3.1800 - 2.9900 1.00 1250 143 0.1296 0.1475
REMARK 3 7 2.9900 - 2.8400 1.00 1303 146 0.1385 0.1397
REMARK 3 8 2.8400 - 2.7200 1.00 1282 151 0.1462 0.1554
REMARK 3 9 2.7200 - 2.6100 1.00 1309 144 0.1377 0.1725
REMARK 3 10 2.6100 - 2.5200 1.00 1247 128 0.1439 0.1955
REMARK 3 11 2.5200 - 2.4400 1.00 1294 146 0.1344 0.1949
REMARK 3 12 2.4400 - 2.3700 1.00 1298 149 0.1315 0.1542
REMARK 3 13 2.3700 - 2.3100 1.00 1228 132 0.1329 0.1517
REMARK 3 14 2.3100 - 2.2500 1.00 1313 150 0.1292 0.1136
REMARK 3 15 2.2500 - 2.2000 1.00 1267 129 0.1296 0.1499
REMARK 3 16 2.2000 - 2.1600 1.00 1304 148 0.1318 0.1631
REMARK 3 17 2.1600 - 2.1100 1.00 1228 141 0.1315 0.1745
REMARK 3 18 2.1100 - 2.0700 1.00 1328 150 0.1389 0.1623
REMARK 3 19 2.0700 - 2.0400 1.00 1217 140 0.1411 0.1516
REMARK 3 20 2.0400 - 2.0000 1.00 1286 144 0.1214 0.1563
REMARK 3 21 2.0000 - 1.9700 1.00 1297 144 0.1310 0.1556
REMARK 3 22 1.9700 - 1.9400 0.99 1260 140 0.1361 0.1562
REMARK 3 23 1.9400 - 1.9100 0.97 1224 145 0.1572 0.1815
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.11
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 : 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 7XTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300029558.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : LIQUID ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER METALJET
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.34138
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : BRUKER PHOTON III
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32588
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 35.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.120
REMARK 200 R MERGE (I) : 0.05250
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.47
REMARK 200 R MERGE FOR SHELL (I) : 0.14210
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.500
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: 5XG0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE; 0.1 M TRIS PH
REMARK 280 8.0; 15% GLYCEROL, EVAPORATION, TEMPERATURE 298K
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 25.41800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.04850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.44450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.04850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.41800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.44450
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 29
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 552 O HOH A 603 1.76
REMARK 500 O HOH A 590 O HOH A 617 2.00
REMARK 500 O HOH A 561 O HOH A 639 2.15
REMARK 500 N ASN A 30 O HOH A 401 2.16
REMARK 500 O2 SO4 A 307 O HOH A 402 2.17
REMARK 500 O2 SO4 A 303 O HOH A 403 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 590 O HOH A 614 3555 1.72
REMARK 500 O HOH A 644 O HOH A 649 2455 2.15
REMARK 500 O HOH A 549 O HOH A 599 4555 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 ASN A 73 37.01 -140.44
REMARK 500 THR A 88 -10.43 68.37
REMARK 500 ALA A 160 -120.22 63.37
REMARK 500 SER A 214 -84.20 -130.52
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7XTW A 30 290 UNP PETH_IDESA
DBREF2 7XTW A A0A0K8P6T7 30 290
SEQADV 7XTW MET A 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7XTW GLY A 132 UNP A0A0K8P6T ARG 132 ENGINEERED MUTATION
SEQADV 7XTW ALA A 160 UNP A0A0K8P6T SER 160 ENGINEERED MUTATION
SEQRES 1 A 262 MET ASN PRO TYR ALA ARG GLY PRO ASN PRO THR ALA ALA
SEQRES 2 A 262 SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER
SEQRES 3 A 262 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 A 262 VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA
SEQRES 5 A 262 ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER
SEQRES 6 A 262 ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 A 262 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 A 262 PRO SER SER ARG SER SER GLN GLN MET ALA ALA LEU GLY
SEQRES 9 A 262 GLN VAL ALA SER LEU ASN GLY THR SER SER SER PRO ILE
SEQRES 10 A 262 TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY
SEQRES 11 A 262 TRP ALA MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA
SEQRES 12 A 262 ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN ALA PRO
SEQRES 13 A 262 TRP ASP SER SER THR ASN PHE SER SER VAL THR VAL PRO
SEQRES 14 A 262 THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO
SEQRES 15 A 262 VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER MET SER
SEQRES 16 A 262 ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER
SEQRES 17 A 262 HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU
SEQRES 18 A 262 ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET
SEQRES 19 A 262 ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN
SEQRES 20 A 262 PRO ASN SER THR ARG VAL SER ASP PHE ARG THR ALA ASN
SEQRES 21 A 262 CYS SER
HET GOL A 301 6
HET C9C A 302 15
HET SO4 A 303 5
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HET SO4 A 307 5
HET GOL A 308 6
HET TRS A 309 8
HETNAM GOL GLYCEROL
HETNAM C9C 4-(2-HYDROXYETHYLOXYCARBONYL)BENZOIC ACID
HETNAM SO4 SULFATE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN C9C MONOHYDROXYETHYL TEREPHTHALATE
HETSYN TRS TRIS BUFFER
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 3 C9C C10 H10 O5
FORMUL 4 SO4 5(O4 S 2-)
FORMUL 10 TRS C4 H12 N O3 1+
FORMUL 11 HOH *253(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS 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 ALA A 160 ASN A 173 1 14
HELIX 6 AA6 SER 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 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 81 O ILE A 109
SHEET 5 AA1 6 VAL A 149 TRP A 159 1 O MET A 157 N ALA A 82
SHEET 6 AA1 6 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.02
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.01
CRYST1 50.836 50.889 84.097 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 0.019671 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019651 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011891 0.00000
TER 1923 SER A 290
MASTER 274 0 9 9 9 0 0 6 2224 1 64 21
END |