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HEADER HYDROLASE 18-MAY-22 7XTV
TITLE THE STRUCTURE OF MHET-BOUND TFCUT S130A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: GB:PZN61876.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_COMMON: THERMOMONOSPORA FUSCA;
SOURCE 4 ORGANISM_TAXID: 2021;
SOURCE 5 GENE: CUT-2.KW3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PET HYDROLASE, PBAT HYDROLASE, ENZYME ENGINEERING, CUTINASE,
KEYWDS 2 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 7XTV 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. 2.31 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) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 100354
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.750
REMARK 3 FREE R VALUE TEST SET COUNT : 3764
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 42.0000 - 6.9200 0.98 3552 139 0.1632 0.2031
REMARK 3 2 6.9200 - 5.5000 0.99 3594 138 0.1833 0.2157
REMARK 3 3 5.5000 - 4.8000 0.99 3557 152 0.1510 0.1487
REMARK 3 4 4.8000 - 4.3600 0.99 3636 127 0.1207 0.1651
REMARK 3 5 4.3600 - 4.0500 0.99 3603 133 0.1289 0.1404
REMARK 3 6 4.0500 - 3.8100 0.99 3536 144 0.1313 0.1694
REMARK 3 7 3.8100 - 3.6200 0.99 3612 143 0.1453 0.1794
REMARK 3 8 3.6200 - 3.4700 0.99 3585 135 0.1619 0.2227
REMARK 3 9 3.4600 - 3.3300 0.99 3612 141 0.1634 0.2367
REMARK 3 10 3.3300 - 3.2200 0.98 3557 138 0.1687 0.2425
REMARK 3 11 3.2200 - 3.1200 0.99 3583 147 0.1825 0.2509
REMARK 3 12 3.1200 - 3.0300 0.97 3518 125 0.1904 0.2112
REMARK 3 13 3.0300 - 2.9500 0.99 3527 138 0.1898 0.2710
REMARK 3 14 2.9500 - 2.8800 0.99 3659 137 0.1829 0.2637
REMARK 3 15 2.8800 - 2.8100 1.00 3622 141 0.1816 0.2935
REMARK 3 16 2.8100 - 2.7500 1.00 3578 142 0.1848 0.2254
REMARK 3 17 2.7500 - 2.7000 1.00 3615 144 0.1833 0.2905
REMARK 3 18 2.7000 - 2.6400 1.00 3670 146 0.2005 0.2719
REMARK 3 19 2.6400 - 2.6000 0.93 3349 123 0.1975 0.2920
REMARK 3 20 2.6000 - 2.5500 0.98 3484 141 0.1914 0.2396
REMARK 3 21 2.5500 - 2.5100 0.99 3652 146 0.1744 0.2341
REMARK 3 22 2.5100 - 2.4700 0.99 3546 135 0.1855 0.2539
REMARK 3 23 2.4700 - 2.4400 1.00 3691 148 0.1839 0.2427
REMARK 3 24 2.4400 - 2.4000 1.00 3553 140 0.1731 0.2809
REMARK 3 25 2.4000 - 2.3700 1.00 3628 146 0.1808 0.2474
REMARK 3 26 2.3700 - 2.3400 1.00 3599 134 0.1701 0.2228
REMARK 3 27 2.3400 - 2.3100 0.94 3472 141 0.1850 0.2514
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.30
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 7XTV 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_1300028972.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
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 : 100354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310
REMARK 200 RESOLUTION RANGE LOW (A) : 45.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.06920
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.01
REMARK 200 R MERGE FOR SHELL (I) : 0.16010
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.660
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: 5ZOA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% V/V PEG200; 0.8 M LITHIUM SULFATE;
REMARK 280 0.1 M SODIUM ACETATE PH4.0, EVAPORATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.54867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 165.09733
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 165.09733
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 82.54867
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 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 350
REMARK 350 BIOMOLECULE: 3
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 511 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 514 LIES ON A SPECIAL POSITION.
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 D 681 O HOH D 690 2.02
REMARK 500 O HOH B 632 O HOH B 648 2.06
REMARK 500 O HOH A 629 O HOH A 658 2.08
REMARK 500 O HOH C 631 O HOH C 657 2.12
REMARK 500 ND1 HIS C 248 O HOH C 501 2.17
REMARK 500 O HOH C 716 O HOH C 719 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 89 169.03 176.71
REMARK 500 THR A 101 -4.98 75.12
REMARK 500 ALA A 170 -119.01 52.92
REMARK 500 THR A 193 60.72 26.81
REMARK 500 HIS A 224 -80.47 -125.57
REMARK 500 ASN B 89 165.86 175.55
REMARK 500 THR B 101 -3.12 71.78
REMARK 500 ALA B 170 -119.21 57.05
REMARK 500 THR B 193 62.09 28.03
REMARK 500 HIS B 224 -80.57 -126.23
REMARK 500 ASN C 89 177.58 174.44
REMARK 500 ALA C 170 -117.53 66.50
REMARK 500 THR C 193 57.08 32.94
REMARK 500 HIS C 224 -79.54 -127.89
REMARK 500 PHE C 289 9.97 57.73
REMARK 500 THR D 101 -2.43 67.23
REMARK 500 ALA D 170 -121.08 65.54
REMARK 500 PRO D 184 -7.52 -59.73
REMARK 500 THR D 193 59.37 29.96
REMARK 500 HIS D 224 -80.02 -124.66
REMARK 500 PHE D 289 11.05 57.73
REMARK 500 THR D 298 30.48 -98.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG D 285 ASP D 286 -137.75
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 728 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH C 722 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH C 723 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH D 706 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH D 707 DISTANCE = 6.62 ANGSTROMS
DBREF 7XTV A 41 301 PDB 7XTV 7XTV 41 301
DBREF 7XTV B 41 301 PDB 7XTV 7XTV 41 301
DBREF 7XTV C 41 301 PDB 7XTV 7XTV 41 301
DBREF 7XTV D 41 301 PDB 7XTV 7XTV 41 301
SEQRES 1 A 261 MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 A 261 LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER GLU
SEQRES 3 A 261 GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 A 261 GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY
SEQRES 5 A 261 ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA
SEQRES 6 A 261 SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY
SEQRES 7 A 261 PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP
SEQRES 8 A 261 GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU
SEQRES 9 A 261 ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 A 261 ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS ALA
SEQRES 11 A 261 MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN ARG
SEQRES 12 A 261 PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 A 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 A 261 ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA
SEQRES 15 A 261 THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 A 261 ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS
SEQRES 17 A 261 PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR
SEQRES 18 A 261 SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 A 261 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 A 261 LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO
SEQRES 21 A 261 PHE
SEQRES 1 B 261 MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 B 261 LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER GLU
SEQRES 3 B 261 GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 B 261 GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY
SEQRES 5 B 261 ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA
SEQRES 6 B 261 SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY
SEQRES 7 B 261 PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP
SEQRES 8 B 261 GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU
SEQRES 9 B 261 ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 B 261 ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS ALA
SEQRES 11 B 261 MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN ARG
SEQRES 12 B 261 PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 B 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 B 261 ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA
SEQRES 15 B 261 THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 B 261 ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS
SEQRES 17 B 261 PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR
SEQRES 18 B 261 SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 B 261 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 B 261 LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO
SEQRES 21 B 261 PHE
SEQRES 1 C 261 MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 C 261 LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER GLU
SEQRES 3 C 261 GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 C 261 GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY
SEQRES 5 C 261 ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA
SEQRES 6 C 261 SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY
SEQRES 7 C 261 PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP
SEQRES 8 C 261 GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU
SEQRES 9 C 261 ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 C 261 ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS ALA
SEQRES 11 C 261 MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN ARG
SEQRES 12 C 261 PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 C 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 C 261 ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA
SEQRES 15 C 261 THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 C 261 ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS
SEQRES 17 C 261 PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR
SEQRES 18 C 261 SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 C 261 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 C 261 LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO
SEQRES 21 C 261 PHE
SEQRES 1 D 261 MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 D 261 LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER GLU
SEQRES 3 D 261 GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 D 261 GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY
SEQRES 5 D 261 ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA
SEQRES 6 D 261 SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY
SEQRES 7 D 261 PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP
SEQRES 8 D 261 GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU
SEQRES 9 D 261 ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 D 261 ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS ALA
SEQRES 11 D 261 MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN ARG
SEQRES 12 D 261 PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 D 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 D 261 ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA
SEQRES 15 D 261 THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 D 261 ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS
SEQRES 17 D 261 PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR
SEQRES 18 D 261 SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 D 261 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 D 261 LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO
SEQRES 21 D 261 PHE
HET C9C A 401 15
HET PEG A 402 7
HET GOL A 403 6
HET C9C B 401 15
HET ACT B 402 4
HET PEG B 403 7
HET PEG B 404 7
HET SO4 C 401 5
HET SO4 C 402 5
HET ACT C 403 4
HET PEG C 404 7
HET PEG C 405 7
HET SO4 D 401 5
HET SO4 D 402 5
HET ACT D 403 4
HET PEG D 404 7
HETNAM C9C 4-(2-HYDROXYETHYLOXYCARBONYL)BENZOIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETSYN C9C MONOHYDROXYETHYL TEREPHTHALATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 C9C 2(C10 H10 O5)
FORMUL 6 PEG 6(C4 H10 O3)
FORMUL 7 GOL C3 H8 O3
FORMUL 9 ACT 3(C2 H3 O2 1-)
FORMUL 12 SO4 4(O4 S 2-)
FORMUL 21 HOH *867(H2 O)
HELIX 1 AA1 THR A 51 ALA A 57 1 7
HELIX 2 AA2 THR A 103 SER A 106 5 4
HELIX 3 AA3 ILE A 107 SER A 116 1 10
HELIX 4 AA4 GLN A 132 ARG A 150 1 19
HELIX 5 AA5 SER A 152 SER A 157 1 6
HELIX 6 AA6 ALA A 170 ARG A 183 1 14
HELIX 7 AA7 HIS A 224 LEU A 232 1 9
HELIX 8 AA8 PHE A 249 ILE A 253 5 5
HELIX 9 AA9 ASN A 255 ASP A 271 1 17
HELIX 10 AB1 ASP A 273 ARG A 275 5 3
HELIX 11 AB2 TYR A 276 CYS A 281 1 6
HELIX 12 AB3 THR B 51 ALA B 57 1 7
HELIX 13 AB4 THR B 103 SER B 106 5 4
HELIX 14 AB5 ILE B 107 SER B 116 1 10
HELIX 15 AB6 GLN B 132 ARG B 150 1 19
HELIX 16 AB7 SER B 152 SER B 157 1 6
HELIX 17 AB8 ALA B 170 ARG B 183 1 14
HELIX 18 AB9 HIS B 224 LEU B 232 1 9
HELIX 19 AC1 PHE B 249 ILE B 253 5 5
HELIX 20 AC2 ASN B 255 ASP B 271 1 17
HELIX 21 AC3 ASP B 273 ARG B 275 5 3
HELIX 22 AC4 TYR B 276 CYS B 281 1 6
HELIX 23 AC5 THR C 51 ALA C 57 1 7
HELIX 24 AC6 THR C 103 SER C 106 5 4
HELIX 25 AC7 ILE C 107 SER C 116 1 10
HELIX 26 AC8 GLN C 132 ARG C 150 1 19
HELIX 27 AC9 SER C 152 SER C 157 1 6
HELIX 28 AD1 ALA C 170 ARG C 183 1 14
HELIX 29 AD2 HIS C 224 LEU C 232 1 9
HELIX 30 AD3 PHE C 249 ILE C 253 5 5
HELIX 31 AD4 ASN C 255 ASP C 271 1 17
HELIX 32 AD5 ASP C 273 ARG C 275 5 3
HELIX 33 AD6 TYR C 276 CYS C 281 1 6
HELIX 34 AD7 GLY C 287 GLY C 290 5 4
HELIX 35 AD8 THR D 51 ALA D 57 1 7
HELIX 36 AD9 THR D 103 SER D 106 5 4
HELIX 37 AE1 ILE D 107 SER D 116 1 10
HELIX 38 AE2 GLN D 132 ARG D 150 1 19
HELIX 39 AE3 SER D 152 SER D 157 1 6
HELIX 40 AE4 ALA D 170 ARG D 183 1 14
HELIX 41 AE5 HIS D 224 LEU D 232 1 9
HELIX 42 AE6 PHE D 249 ILE D 253 5 5
HELIX 43 AE7 ASN D 255 ASP D 271 1 17
HELIX 44 AE8 ASP D 273 ARG D 275 5 3
HELIX 45 AE9 TYR D 276 CYS D 281 1 6
HELIX 46 AF1 GLY D 287 GLY D 290 5 4
SHEET 1 AA1 6 VAL A 64 VAL A 69 0
SHEET 2 AA1 6 GLY A 80 PRO A 85 -1 O GLY A 80 N VAL A 69
SHEET 3 AA1 6 PHE A 119 ILE A 124 -1 O VAL A 121 N TYR A 83
SHEET 4 AA1 6 TYR A 91 SER A 97 1 N ILE A 96 O ILE A 122
SHEET 5 AA1 6 ILE A 159 HIS A 169 1 O ASP A 160 N TYR A 91
SHEET 6 AA1 6 ALA A 188 LEU A 192 1 O LEU A 192 N GLY A 168
SHEET 1 AA2 3 THR A 208 ALA A 213 0
SHEET 2 AA2 3 LYS A 238 LEU A 243 1 O LEU A 243 N GLY A 212
SHEET 3 AA2 3 GLU A 294 SER A 297 -1 O GLU A 294 N GLU A 242
SHEET 1 AA3 6 VAL B 64 VAL B 69 0
SHEET 2 AA3 6 GLY B 80 PRO B 85 -1 O GLY B 80 N VAL B 69
SHEET 3 AA3 6 PHE B 119 ILE B 124 -1 O VAL B 121 N TYR B 83
SHEET 4 AA3 6 TYR B 91 SER B 97 1 N ILE B 96 O ILE B 122
SHEET 5 AA3 6 ILE B 159 HIS B 169 1 O ASP B 160 N TYR B 91
SHEET 6 AA3 6 ALA B 188 LEU B 192 1 O LEU B 192 N GLY B 168
SHEET 1 AA4 3 THR B 208 ALA B 213 0
SHEET 2 AA4 3 LYS B 238 LEU B 243 1 O LEU B 243 N GLY B 212
SHEET 3 AA4 3 GLU B 294 SER B 297 -1 O GLU B 294 N GLU B 242
SHEET 1 AA5 6 VAL C 64 VAL C 69 0
SHEET 2 AA5 6 GLY C 80 PRO C 85 -1 O ILE C 82 N GLU C 67
SHEET 3 AA5 6 VAL C 120 ILE C 124 -1 O VAL C 121 N TYR C 83
SHEET 4 AA5 6 TYR C 91 SER C 97 1 N VAL C 94 O VAL C 120
SHEET 5 AA5 6 ILE C 159 HIS C 169 1 O ASP C 160 N TYR C 91
SHEET 6 AA5 6 ALA C 188 LEU C 192 1 O LEU C 192 N GLY C 168
SHEET 1 AA6 3 THR C 208 ALA C 213 0
SHEET 2 AA6 3 LYS C 238 LEU C 243 1 O LEU C 243 N GLY C 212
SHEET 3 AA6 3 VAL C 292 SER C 297 -1 O ARG C 296 N TYR C 240
SHEET 1 AA7 6 VAL D 64 VAL D 69 0
SHEET 2 AA7 6 GLY D 80 PRO D 85 -1 O ILE D 82 N GLU D 67
SHEET 3 AA7 6 VAL D 120 ILE D 124 -1 O VAL D 121 N TYR D 83
SHEET 4 AA7 6 TYR D 91 SER D 97 1 N VAL D 94 O VAL D 120
SHEET 5 AA7 6 ILE D 159 HIS D 169 1 O ASP D 160 N TYR D 91
SHEET 6 AA7 6 ALA D 188 LEU D 192 1 O LEU D 192 N GLY D 168
SHEET 1 AA8 3 THR D 208 ALA D 213 0
SHEET 2 AA8 3 LYS D 238 LEU D 243 1 O LEU D 243 N GLY D 212
SHEET 3 AA8 3 VAL D 292 SER D 297 -1 O ARG D 296 N TYR D 240
SSBOND 1 CYS A 281 CYS A 299 1555 1555 2.03
SSBOND 2 CYS B 281 CYS B 299 1555 1555 2.05
SSBOND 3 CYS C 281 CYS C 299 1555 1555 2.08
SSBOND 4 CYS D 281 CYS D 299 1555 1555 2.10
CISPEP 1 CYS A 281 PRO A 282 0 1.15
CISPEP 2 CYS A 299 PRO A 300 0 -4.04
CISPEP 3 CYS B 281 PRO B 282 0 1.89
CISPEP 4 CYS B 299 PRO B 300 0 -6.57
CISPEP 5 CYS C 281 PRO C 282 0 0.80
CISPEP 6 CYS C 299 PRO C 300 0 -0.56
CISPEP 7 CYS D 281 PRO D 282 0 3.57
CISPEP 8 ASP D 286 GLY D 287 0 -7.02
CISPEP 9 CYS D 299 PRO D 300 0 -0.61
CRYST1 91.489 91.489 247.646 90.00 90.00 120.00 P 31 2 1 24
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 0.010930 0.006311 0.000000 0.00000
SCALE2 0.000000 0.012621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004038 0.00000
TER 1995 PHE A 301
TER 3990 PHE B 301
TER 5985 PHE C 301
TER 7980 PHE D 301
MASTER 334 0 16 46 36 0 0 6 8953 4 118 84
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