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HEADER HYDROLASE 18-MAY-22 7XTT
TITLE THE STRUCTURE OF ENGINEERED TFCUT S130A IN COMPLEX WITH MHET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
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 7XTT 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. 1.82 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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 75313
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 3782
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 32.6200 - 5.4500 0.96 2623 136 0.1577 0.1683
REMARK 3 2 5.4500 - 4.3300 1.00 2716 140 0.1260 0.1448
REMARK 3 3 4.3300 - 3.7800 1.00 2700 136 0.1121 0.1302
REMARK 3 4 3.7800 - 3.4400 1.00 2728 146 0.1282 0.1440
REMARK 3 5 3.4400 - 3.1900 1.00 2734 154 0.1349 0.1557
REMARK 3 6 3.1900 - 3.0000 1.00 2643 140 0.1396 0.1684
REMARK 3 7 3.0000 - 2.8500 1.00 2811 132 0.1463 0.1993
REMARK 3 8 2.8500 - 2.7300 1.00 2732 142 0.1401 0.1965
REMARK 3 9 2.7300 - 2.6200 1.00 2674 150 0.1396 0.1716
REMARK 3 10 2.6200 - 2.5300 1.00 2716 132 0.1392 0.1790
REMARK 3 11 2.5300 - 2.4500 1.00 2716 145 0.1379 0.1921
REMARK 3 12 2.4500 - 2.3800 1.00 2765 147 0.1398 0.1731
REMARK 3 13 2.3800 - 2.3200 0.99 2679 138 0.1305 0.1694
REMARK 3 14 2.3200 - 2.2700 0.99 2738 144 0.1316 0.1916
REMARK 3 15 2.2700 - 2.2100 0.98 2639 131 0.1342 0.1735
REMARK 3 16 2.2100 - 2.1700 0.97 2629 138 0.1325 0.1800
REMARK 3 17 2.1700 - 2.1200 0.97 2690 147 0.1326 0.2026
REMARK 3 18 2.1200 - 2.0800 0.97 2629 121 0.1349 0.1847
REMARK 3 19 2.0800 - 2.0500 0.96 2636 156 0.1331 0.1625
REMARK 3 20 2.0500 - 2.0100 0.96 2596 135 0.1295 0.1720
REMARK 3 21 2.0100 - 1.9800 0.95 2561 141 0.1393 0.1948
REMARK 3 22 1.9800 - 1.9500 0.95 2619 159 0.1394 0.1908
REMARK 3 23 1.9500 - 1.9200 0.94 2533 137 0.1477 0.2077
REMARK 3 24 1.9200 - 1.8900 0.93 2505 135 0.1476 0.2001
REMARK 3 25 1.8900 - 1.8700 0.93 2565 138 0.1548 0.2076
REMARK 3 26 1.8700 - 1.8400 0.93 2510 143 0.1483 0.2055
REMARK 3 27 1.8400 - 1.8200 0.91 2444 119 0.1602 0.2262
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.28
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 7XTT 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_1300028970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-DEC-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : 75313
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 32.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.03370
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 38.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.21
REMARK 200 R MERGE FOR SHELL (I) : 0.10470
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 8.950
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 (%): 37.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/V PEG8000; 0.2 M AMMONIUM
REMARK 280 SULFATE; 0.1 M SODIUM CACODYLATE 6.5, PH 6.5, EVAPORATION,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 20.95150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 GLY B 40
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 GLN A 278 CG CD OE1 NE2
REMARK 470 ARG B 285 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 B 715 O HOH B 731 2.05
REMARK 500 O HOH A 620 O HOH A 760 2.07
REMARK 500 O HOH B 556 O HOH B 708 2.11
REMARK 500 O HOH A 536 O HOH A 620 2.11
REMARK 500 O HOH A 757 O HOH A 815 2.12
REMARK 500 O HOH A 504 O HOH A 772 2.15
REMARK 500 O HOH A 503 O HOH A 530 2.15
REMARK 500 O ARG B 285 O HOH B 501 2.15
REMARK 500 O HOH B 745 O HOH B 751 2.16
REMARK 500 O HOH B 683 O HOH B 785 2.18
REMARK 500 O HOH A 604 O HOH A 759 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 B 785 O HOH B 826 2555 2.06
REMARK 500 O HOH A 752 O HOH B 806 2546 2.15
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 ALA A 170 -119.93 65.74
REMARK 500 THR A 193 58.99 32.21
REMARK 500 SER A 224 -77.71 -119.26
REMARK 500 ASN B 89 173.09 177.77
REMARK 500 THR B 101 -5.45 75.71
REMARK 500 ALA B 170 -114.18 63.28
REMARK 500 THR B 193 58.91 30.89
REMARK 500 SER B 224 -80.24 -118.87
REMARK 500 PRO B 284 48.64 -74.88
REMARK 500 GLU B 291 -59.81 -131.88
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 849 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A 850 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A 851 DISTANCE = 7.45 ANGSTROMS
REMARK 525 HOH B 830 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B 831 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B 832 DISTANCE = 6.25 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 NA B 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 214 OD2
REMARK 620 2 ASP A 244 OD1 86.5
REMARK 620 3 GLU A 293 OE1 111.6 84.7
REMARK 620 4 ASN B 230 O 59.9 28.8 85.7
REMARK 620 5 LEU B 232 O 62.3 26.0 85.9 2.8
REMARK 620 6 HOH B 562 O 60.5 27.1 88.1 3.0 2.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 64 O
REMARK 620 2 ARG B 150 O 31.5
REMARK 620 3 ALA B 151 O 24.0 7.9
REMARK 620 4 HOH B 622 O 24.6 7.4 0.6
REMARK 620 5 HOH B 634 O 32.8 8.3 10.2 9.6
REMARK 620 6 HOH B 659 O 24.9 13.0 7.9 7.8 8.9
REMARK 620 N 1 2 3 4 5
DBREF 7XTT A 40 301 PDB 7XTT 7XTT 40 301
DBREF 7XTT B 40 301 PDB 7XTT 7XTT 40 301
SEQRES 1 A 262 GLY MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP
SEQRES 2 A 262 ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER
SEQRES 3 A 262 GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY
SEQRES 4 A 262 GLY GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR
SEQRES 5 A 262 GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU
SEQRES 6 A 262 ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS
SEQRES 7 A 262 GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU
SEQRES 8 A 262 ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA
SEQRES 9 A 262 LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG
SEQRES 10 A 262 SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS
SEQRES 11 A 262 ALA MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN
SEQRES 12 A 262 ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP
SEQRES 13 A 262 HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR
SEQRES 14 A 262 LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 262 ALA THR SER ALA LYS PRO ILE TYR ASN SER LEU PRO SER
SEQRES 16 A 262 SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR
SEQRES 17 A 262 HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS
SEQRES 18 A 262 TYR SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP
SEQRES 19 A 262 THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP
SEQRES 20 A 262 GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS
SEQRES 21 A 262 PRO PHE
SEQRES 1 B 262 GLY MET ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP
SEQRES 2 B 262 ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL SER
SEQRES 3 B 262 GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY
SEQRES 4 B 262 GLY GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR
SEQRES 5 B 262 GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU
SEQRES 6 B 262 ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS
SEQRES 7 B 262 GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU
SEQRES 8 B 262 ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA
SEQRES 9 B 262 LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG
SEQRES 10 B 262 SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS
SEQRES 11 B 262 ALA MET GLY GLY GLY GLY SER LEU ARG LEU ALA SER GLN
SEQRES 12 B 262 ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP
SEQRES 13 B 262 HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR
SEQRES 14 B 262 LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL
SEQRES 15 B 262 ALA THR SER ALA LYS PRO ILE TYR ASN SER LEU PRO SER
SEQRES 16 B 262 SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR
SEQRES 17 B 262 HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS
SEQRES 18 B 262 TYR SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP
SEQRES 19 B 262 THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP
SEQRES 20 B 262 GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS
SEQRES 21 B 262 PRO PHE
HET EDO A 401 4
HET C9C B 401 15
HET EDO B 402 4
HET EDO B 403 4
HET SO4 B 404 5
HET NA B 405 1
HET NA B 406 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM C9C 4-(2-HYDROXYETHYLOXYCARBONYL)BENZOIC ACID
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN C9C MONOHYDROXYETHYL TEREPHTHALATE
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 4 C9C C10 H10 O5
FORMUL 7 SO4 O4 S 2-
FORMUL 8 NA 2(NA 1+)
FORMUL 10 HOH *683(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 SER 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 SER 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
SHEET 1 AA1 6 VAL A 64 VAL A 69 0
SHEET 2 AA1 6 GLY A 80 PRO A 85 -1 O ILE A 82 N GLU A 67
SHEET 3 AA1 6 VAL A 120 ILE A 124 -1 O VAL A 121 N TYR A 83
SHEET 4 AA1 6 TYR A 91 SER A 97 1 N VAL A 94 O VAL A 120
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 ARG A 296 N TYR A 240
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 VAL B 120 ILE B 124 -1 O VAL B 121 N TYR B 83
SHEET 4 AA3 6 TYR B 91 SER B 97 1 N VAL B 94 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 VAL B 292 SER B 297 -1 O GLU B 293 N GLU B 242
SSBOND 1 CYS A 281 CYS A 299 1555 1555 2.04
SSBOND 2 CYS B 281 CYS B 299 1555 1555 2.06
LINK OD2 ASP A 214 NA NA B 406 1555 1655 2.31
LINK OD1 ASP A 244 NA NA B 406 1555 1655 2.25
LINK OE1 GLU A 293 NA NA B 406 1555 1655 2.27
LINK O VAL B 64 NA NA B 405 1555 2545 2.35
LINK O ARG B 150 NA NA B 405 1555 1555 2.45
LINK O ALA B 151 NA NA B 405 1555 1555 2.43
LINK O ASN B 230 NA NA B 406 1555 1555 2.31
LINK O LEU B 232 NA NA B 406 1555 1555 2.37
LINK NA NA B 405 O HOH B 622 1555 1555 2.39
LINK NA NA B 405 O HOH B 634 1555 2555 2.45
LINK NA NA B 405 O HOH B 659 1555 1555 2.36
LINK NA NA B 406 O HOH B 562 1555 1555 2.48
CISPEP 1 CYS A 281 PRO A 282 0 3.49
CISPEP 2 CYS A 299 PRO A 300 0 9.48
CISPEP 3 CYS B 281 PRO B 282 0 -0.09
CISPEP 4 CYS B 299 PRO B 300 0 8.24
CRYST1 65.838 41.903 80.868 90.00 92.11 90.00 P 1 21 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 0.015189 0.000000 0.000559 0.00000
SCALE2 0.000000 0.023865 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012374 0.00000
TER 2009 PHE A 301
TER 4012 PHE B 301
MASTER 340 0 7 22 18 0 0 6 4685 2 45 42
END |