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HEADER HYDROLASE 27-MAY-22 8D1D
TITLE PROSS PETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, C, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: PROSS PETASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS PLASTIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.VONGSOUTHI,C.J.JACKSON,L.TAN
REVDAT 1 21-SEP-22 8D1D 0
JRNL AUTH V.VONGSOUTHI,C.J.JACKSON,L.TAN
JRNL TITL PROSS PETASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.42 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 177010
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 8959
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 39.7900 - 4.4200 1.00 5737 303 0.2084 0.2173
REMARK 3 2 4.4200 - 3.5100 1.00 5713 289 0.2017 0.2173
REMARK 3 3 3.5100 - 3.0600 1.00 5702 278 0.2116 0.2298
REMARK 3 4 3.0600 - 2.7800 1.00 5693 299 0.2090 0.2314
REMARK 3 5 2.7800 - 2.5900 1.00 5717 275 0.2004 0.2464
REMARK 3 6 2.5900 - 2.4300 1.00 5657 314 0.1954 0.2131
REMARK 3 7 2.4300 - 2.3100 1.00 5625 345 0.1936 0.2232
REMARK 3 8 2.3100 - 2.2100 1.00 5677 283 0.1958 0.2347
REMARK 3 9 2.2100 - 2.1300 0.99 5638 284 0.1959 0.2399
REMARK 3 10 2.1300 - 2.0500 1.00 5696 276 0.2002 0.2369
REMARK 3 11 2.0500 - 1.9900 0.99 5624 308 0.1981 0.2579
REMARK 3 12 1.9900 - 1.9300 0.99 5610 337 0.1869 0.2385
REMARK 3 13 1.9300 - 1.8800 1.00 5601 297 0.1793 0.2147
REMARK 3 14 1.8800 - 1.8300 0.99 5641 311 0.1723 0.2350
REMARK 3 15 1.8300 - 1.7900 0.99 5586 312 0.1771 0.2399
REMARK 3 16 1.7900 - 1.7500 0.99 5566 321 0.1705 0.2227
REMARK 3 17 1.7500 - 1.7200 0.99 5609 309 0.1688 0.2279
REMARK 3 18 1.7200 - 1.6900 0.99 5568 322 0.1751 0.2329
REMARK 3 19 1.6900 - 1.6600 0.98 5597 284 0.1738 0.2149
REMARK 3 20 1.6600 - 1.6300 0.99 5574 286 0.1757 0.2538
REMARK 3 21 1.6300 - 1.6000 0.99 5558 322 0.1988 0.2709
REMARK 3 22 1.6000 - 1.5800 0.98 5608 292 0.1986 0.2507
REMARK 3 23 1.5800 - 1.5500 0.99 5602 286 0.1841 0.2376
REMARK 3 24 1.5500 - 1.5300 0.97 5525 290 0.1840 0.2392
REMARK 3 25 1.5300 - 1.5100 0.99 5533 324 0.1936 0.2754
REMARK 3 26 1.5100 - 1.4900 0.98 5572 286 0.2017 0.2589
REMARK 3 27 1.4900 - 1.4700 0.97 5546 245 0.2134 0.2667
REMARK 3 28 1.4700 - 1.4600 0.99 5563 290 0.2219 0.2791
REMARK 3 29 1.4600 - 1.4400 0.97 5478 310 0.2373 0.3086
REMARK 3 30 1.4400 - 1.4200 0.92 5235 281 0.3192 0.3628
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.08
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 6060
REMARK 3 ANGLE : 0.946 8274
REMARK 3 CHIRALITY : 0.078 905
REMARK 3 PLANARITY : 0.008 1105
REMARK 3 DIHEDRAL : 12.390 2154
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 8D1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1000265836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 177110
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.420
REMARK 200 RESOLUTION RANGE LOW (A) : 45.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.14700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.92900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
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: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% V/V GLYCEROL, 0.08 M SODIUM
REMARK 280 CACODYLATE, 14.4% W/V PEG 8K, 0.16M CALCIUM ACETATE, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 68.29300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.58650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.29300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 79.58650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 CA CA A 301 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 585 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 LEU A 291
REMARK 465 GLU A 292
REMARK 465 ASP A 293
REMARK 465 GLY C 29
REMARK 465 LEU C 291
REMARK 465 GLU C 292
REMARK 465 ASP C 293
REMARK 465 LEU E 291
REMARK 465 GLU E 292
REMARK 465 ASP E 293
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 562 O HOH A 582 2.04
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 HIS A 32 57.51 -140.76
REMARK 500 ASN A 73 46.23 -140.13
REMARK 500 SER A 160 -121.89 66.14
REMARK 500 HIS A 214 -85.19 -122.88
REMARK 500 HIS C 32 57.55 -140.66
REMARK 500 ASN C 73 42.99 -146.69
REMARK 500 SER C 160 -119.88 57.31
REMARK 500 ALA C 183 56.65 39.22
REMARK 500 HIS C 214 -87.50 -125.33
REMARK 500 HIS E 32 57.27 -141.87
REMARK 500 SER E 160 -122.26 67.15
REMARK 500 SER E 160 -123.30 67.15
REMARK 500 HIS E 214 -87.89 -126.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 583 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A 584 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH A 585 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH C 545 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH C 546 DISTANCE = 11.27 ANGSTROMS
REMARK 525 HOH C 547 DISTANCE = 12.08 ANGSTROMS
REMARK 525 HOH E 411 DISTANCE = 16.98 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 204 OE1
REMARK 620 2 GLU A 204 OE2 50.6
REMARK 620 3 GLU A 204 OE1 0.0 50.6
REMARK 620 4 GLU A 204 OE2 50.6 0.0 50.6
REMARK 620 5 ASN A 233 OD1 77.6 106.2 77.6 106.2
REMARK 620 6 ASN A 233 OD1 77.6 106.2 77.6 106.2 0.0
REMARK 620 7 HOH A 540 O 109.1 75.3 109.1 75.3 78.1 78.1
REMARK 620 8 HOH A 540 O 85.2 130.4 85.2 130.4 80.2 80.2 150.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 204 OE1
REMARK 620 2 GLU C 204 OE2 50.9
REMARK 620 3 ASN C 233 OD1 75.8 108.4
REMARK 620 4 HOH C 503 O 106.2 73.6 81.7
REMARK 620 5 GLU E 204 OE1 71.3 50.6 71.4 35.0
REMARK 620 6 GLU E 204 OE2 68.7 49.1 71.1 37.6 2.6
REMARK 620 7 ASN E 233 OD1 71.9 54.0 67.8 34.9 3.9 5.0
REMARK 620 8 HOH E 374 O 85.2 127.9 80.5 155.7 146.8 145.0 144.2
REMARK 620 N 1 2 3 4 5 6 7
DBREF 8D1D A 29 293 PDB 8D1D 8D1D 29 293
DBREF 8D1D C 29 293 PDB 8D1D 8D1D 29 293
DBREF 8D1D E 29 293 PDB 8D1D 8D1D 29 293
SEQRES 1 A 265 GLY GLY SER HIS MET ARG GLY PRO ASN PRO THR ALA ALA
SEQRES 2 A 265 SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER
SEQRES 3 A 265 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 A 265 VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA
SEQRES 5 A 265 ILE ALA ILE VAL PRO GLY TYR THR ALA THR GLN SER SER
SEQRES 6 A 265 ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 A 265 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 A 265 PRO SER SER ARG SER ASP GLN GLN MET ALA ALA LEU ASP
SEQRES 9 A 265 GLN LEU ALA SER LEU ASN ASN ASP SER SER SER PRO ILE
SEQRES 10 A 265 TYR GLY LYS VAL ASP THR SER ARG MET GLY VAL MET GLY
SEQRES 11 A 265 TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA
SEQRES 12 A 265 ASN ASN PRO SER LEU LYS ALA ALA ALA PRO MET ALA PRO
SEQRES 13 A 265 TRP SER SER SER THR ASN PHE SER SER VAL THR VAL PRO
SEQRES 14 A 265 THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO
SEQRES 15 A 265 VAL ASN SER HIS ALA LEU PRO ILE TYR ASN SER MET SER
SEQRES 16 A 265 ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER
SEQRES 17 A 265 HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU
SEQRES 18 A 265 ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET
SEQRES 19 A 265 ASP ASN ASP THR ARG TYR SER GLN PHE ALA CYS GLU ASN
SEQRES 20 A 265 PRO ASN SER THR ALA VAL SER ASP PHE ARG THR ALA ASN
SEQRES 21 A 265 CYS SER LEU GLU ASP
SEQRES 1 C 265 GLY GLY SER HIS MET ARG GLY PRO ASN PRO THR ALA ALA
SEQRES 2 C 265 SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER
SEQRES 3 C 265 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 C 265 VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA
SEQRES 5 C 265 ILE ALA ILE VAL PRO GLY TYR THR ALA THR GLN SER SER
SEQRES 6 C 265 ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 C 265 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 C 265 PRO SER SER ARG SER ASP GLN GLN MET ALA ALA LEU ASP
SEQRES 9 C 265 GLN LEU ALA SER LEU ASN ASN ASP SER SER SER PRO ILE
SEQRES 10 C 265 TYR GLY LYS VAL ASP THR SER ARG MET GLY VAL MET GLY
SEQRES 11 C 265 TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA
SEQRES 12 C 265 ASN ASN PRO SER LEU LYS ALA ALA ALA PRO MET ALA PRO
SEQRES 13 C 265 TRP SER SER SER THR ASN PHE SER SER VAL THR VAL PRO
SEQRES 14 C 265 THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO
SEQRES 15 C 265 VAL ASN SER HIS ALA LEU PRO ILE TYR ASN SER MET SER
SEQRES 16 C 265 ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER
SEQRES 17 C 265 HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU
SEQRES 18 C 265 ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET
SEQRES 19 C 265 ASP ASN ASP THR ARG TYR SER GLN PHE ALA CYS GLU ASN
SEQRES 20 C 265 PRO ASN SER THR ALA VAL SER ASP PHE ARG THR ALA ASN
SEQRES 21 C 265 CYS SER LEU GLU ASP
SEQRES 1 E 265 GLY GLY SER HIS MET ARG GLY PRO ASN PRO THR ALA ALA
SEQRES 2 E 265 SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER
SEQRES 3 E 265 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 E 265 VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA
SEQRES 5 E 265 ILE ALA ILE VAL PRO GLY TYR THR ALA THR GLN SER SER
SEQRES 6 E 265 ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 E 265 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 E 265 PRO SER SER ARG SER ASP GLN GLN MET ALA ALA LEU ASP
SEQRES 9 E 265 GLN LEU ALA SER LEU ASN ASN ASP SER SER SER PRO ILE
SEQRES 10 E 265 TYR GLY LYS VAL ASP THR SER ARG MET GLY VAL MET GLY
SEQRES 11 E 265 TRP SER MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA
SEQRES 12 E 265 ASN ASN PRO SER LEU LYS ALA ALA ALA PRO MET ALA PRO
SEQRES 13 E 265 TRP SER SER SER THR ASN PHE SER SER VAL THR VAL PRO
SEQRES 14 E 265 THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO
SEQRES 15 E 265 VAL ASN SER HIS ALA LEU PRO ILE TYR ASN SER MET SER
SEQRES 16 E 265 ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER
SEQRES 17 E 265 HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU
SEQRES 18 E 265 ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET
SEQRES 19 E 265 ASP ASN ASP THR ARG TYR SER GLN PHE ALA CYS GLU ASN
SEQRES 20 E 265 PRO ASN SER THR ALA VAL SER ASP PHE ARG THR ALA ASN
SEQRES 21 E 265 CYS SER LEU GLU ASP
HET CA A 301 1
HET CA C 301 1
HETNAM CA CALCIUM ION
FORMUL 4 CA 2(CA 2+)
FORMUL 6 HOH *443(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 THR A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 ASN A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 HIS A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASN A 264 1 19
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
HELIX 10 AB1 THR C 39 ALA C 45 1 7
HELIX 11 AB2 THR C 90 LYS C 95 5 6
HELIX 12 AB3 TRP C 96 SER C 103 1 8
HELIX 13 AB4 GLN C 119 ASN C 139 1 21
HELIX 14 AB5 SER C 160 ASN C 173 1 14
HELIX 15 AB6 HIS C 214 MET C 222 1 9
HELIX 16 AB7 ASN C 246 ASN C 264 1 19
HELIX 17 AB8 ASP C 265 ARG C 267 5 3
HELIX 18 AB9 TYR C 268 GLU C 274 1 7
HELIX 19 AC1 THR E 39 ALA E 45 1 7
HELIX 20 AC2 THR E 90 LYS E 95 5 6
HELIX 21 AC3 TRP E 96 SER E 103 1 8
HELIX 22 AC4 GLN E 119 ASN E 138 1 20
HELIX 23 AC5 SER E 160 ASN E 173 1 14
HELIX 24 AC6 HIS E 214 MET E 222 1 9
HELIX 25 AC7 ASN E 246 ASP E 263 1 18
HELIX 26 AC8 ASP E 265 ARG E 267 5 3
HELIX 27 AC9 TYR E 268 GLU E 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 PHE A 106 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 83 O ILE A 109
SHEET 5 AA1 6 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 MET A 182 1 O MET 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
SHEET 1 AA3 6 VAL C 52 THR C 56 0
SHEET 2 AA3 6 ALA C 65 PRO C 71 -1 O VAL C 68 N PHE C 55
SHEET 3 AA3 6 VAL C 107 ASP C 112 -1 O VAL C 108 N TYR C 69
SHEET 4 AA3 6 VAL C 78 VAL C 84 1 N ILE C 83 O ILE C 109
SHEET 5 AA3 6 VAL C 149 TRP C 159 1 O ASP C 150 N VAL C 78
SHEET 6 AA3 6 ALA C 178 MET C 182 1 O MET C 182 N GLY C 158
SHEET 1 AA4 3 THR C 198 CYS C 203 0
SHEET 2 AA4 3 LYS C 227 ILE C 232 1 O GLN C 228 N ILE C 200
SHEET 3 AA4 3 VAL C 281 ALA C 287 -1 O ARG C 285 N PHE C 229
SHEET 1 AA5 6 VAL E 52 THR E 56 0
SHEET 2 AA5 6 ALA E 65 PRO E 71 -1 O VAL E 68 N PHE E 55
SHEET 3 AA5 6 PHE E 106 ASP E 112 -1 O VAL E 108 N TYR E 69
SHEET 4 AA5 6 VAL E 78 VAL E 84 1 N ILE E 81 O ILE E 109
SHEET 5 AA5 6 VAL E 149 TRP E 159 1 O ASP E 150 N VAL E 78
SHEET 6 AA5 6 ALA E 178 MET E 182 1 O MET E 182 N GLY E 158
SHEET 1 AA6 3 THR E 198 CYS E 203 0
SHEET 2 AA6 3 LYS E 227 ILE E 232 1 O GLN E 228 N ILE E 200
SHEET 3 AA6 3 VAL E 281 ALA E 287 -1 O ARG E 285 N PHE E 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.05
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.04
SSBOND 3 CYS C 203 CYS C 239 1555 1555 2.06
SSBOND 4 CYS C 273 CYS C 289 1555 1555 2.04
SSBOND 5 CYS E 203 CYS E 239 1555 1555 2.04
SSBOND 6 CYS E 273 CYS E 289 1555 1555 2.05
LINK OE1 GLU A 204 CA CA A 301 1555 1555 2.48
LINK OE2 GLU A 204 CA CA A 301 1555 1555 2.65
LINK OE1 GLU A 204 CA CA A 301 1555 2656 2.51
LINK OE2 GLU A 204 CA CA A 301 1555 2656 2.65
LINK OD1 ASN A 233 CA CA A 301 1555 1555 2.32
LINK OD1 ASN A 233 CA CA A 301 1555 2656 2.34
LINK CA CA A 301 O HOH A 540 1555 1555 2.47
LINK CA CA A 301 O HOH A 540 1555 2656 2.46
LINK OE1 GLU C 204 CA CA C 301 1555 1555 2.48
LINK OE2 GLU C 204 CA CA C 301 1555 1555 2.59
LINK OD1 ASN C 233 CA CA C 301 1555 1555 2.40
LINK CA CA C 301 O HOH C 503 1555 1555 2.42
LINK CA CA C 301 OE1 GLU E 204 1554 1555 2.51
LINK CA CA C 301 OE2 GLU E 204 1554 1555 2.54
LINK CA CA C 301 OD1 ASN E 233 1554 1555 2.30
LINK CA CA C 301 O HOH E 374 1555 1556 2.29
CRYST1 136.586 159.173 45.043 90.00 90.07 90.00 C 1 2 1 12
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 0.007321 0.000000 0.000009 0.00000
SCALE2 0.000000 0.006282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022201 0.00000
TER 3830 SER A 290
TER 7587 SER C 290
TER 11400 SER E 290
MASTER 346 0 2 27 27 0 0 6 6192 3 23 63
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