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HEADER HYDROLASE 18-MAY-22 7XTR
TITLE THE APO STRUCTURE OF THE ENGINEERED TFCUT
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 PETASE, CUTINASE, ENZYME ENGINEERING, PBAT DEGRADATION, 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 7XTR 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 3 NUMBER OF REFLECTIONS : 38580
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.180
REMARK 3 FREE R VALUE TEST SET COUNT : 3542
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 32.6800 - 6.4200 0.91 1444 157 0.1639 0.1771
REMARK 3 2 6.4200 - 5.1000 0.92 1438 155 0.1788 0.2061
REMARK 3 3 5.1000 - 4.4600 0.91 1454 150 0.1440 0.1762
REMARK 3 4 4.4600 - 4.0500 0.90 1429 148 0.1372 0.1564
REMARK 3 5 4.0500 - 3.7600 0.90 1400 147 0.1460 0.1729
REMARK 3 6 3.7600 - 3.5400 0.89 1409 142 0.1596 0.1957
REMARK 3 7 3.5400 - 3.3600 0.91 1481 145 0.1741 0.2431
REMARK 3 8 3.3600 - 3.2200 0.93 1458 137 0.1702 0.2198
REMARK 3 9 3.2200 - 3.0900 0.92 1501 142 0.1851 0.2718
REMARK 3 10 3.0900 - 2.9900 0.93 1420 150 0.1822 0.2444
REMARK 3 11 2.9900 - 2.8900 0.92 1497 139 0.1883 0.3289
REMARK 3 12 2.8900 - 2.8100 0.93 1468 158 0.2050 0.2810
REMARK 3 13 2.8100 - 2.7400 0.91 1455 159 0.1904 0.2535
REMARK 3 14 2.7400 - 2.6700 0.93 1490 140 0.1855 0.2478
REMARK 3 15 2.6700 - 2.6100 0.89 1362 131 0.1959 0.3046
REMARK 3 16 2.6100 - 2.5500 0.86 1431 139 0.1894 0.3209
REMARK 3 17 2.5500 - 2.5000 0.86 1364 143 0.2000 0.2951
REMARK 3 18 2.5000 - 2.4500 0.86 1312 144 0.1811 0.2586
REMARK 3 19 2.4500 - 2.4100 0.84 1408 133 0.1894 0.2752
REMARK 3 20 2.4100 - 2.3700 0.86 1318 117 0.1646 0.2953
REMARK 3 21 2.3700 - 2.3300 0.80 1237 143 0.1648 0.2408
REMARK 3 22 2.3300 - 2.3000 0.80 1307 125 0.1717 0.2535
REMARK 3 23 2.3000 - 2.2600 0.82 1281 136 0.1859 0.2725
REMARK 3 24 2.2600 - 2.2300 0.84 1321 131 0.1766 0.3233
REMARK 3 25 2.2300 - 2.2000 0.85 1353 131 0.1724 0.2938
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) : 22.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.29
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 7XTR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300028968.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 : CMOS
REMARK 200 DETECTOR MANUFACTURER : BRUKER PHOTON 100
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38580
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 37.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.09900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
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: 4CG2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3350, 0.2 M SODIUM NITRATE,
REMARK 280 0.1 M BIS-TRIS PROPANE 8.5, PH 8.5, EVAPORATION, TEMPERATURE 273K
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 20.98050
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 LEU A 288
REMARK 465 PHE A 289
REMARK 465 ARG B 285
REMARK 465 GLY B 287
REMARK 465 LEU B 288
REMARK 465 PHE B 289
REMARK 465 GLY B 290
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 639 O HOH A 665 2.13
REMARK 500 OG SER B 170 O HOH B 501 2.13
REMARK 500 O HOH A 609 O HOH A 632 2.14
REMARK 500 O2 SO4 A 401 O1 GOL A 402 2.17
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 NH1 ARG B 86 NH2 ARG B 150 2545 1.55
REMARK 500 O HOH A 524 O HOH B 608 2546 2.05
REMARK 500 O HOH A 579 O HOH A 619 2546 2.12
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 SER A 170 -115.44 62.78
REMARK 500 THR A 193 58.04 30.99
REMARK 500 SER A 224 -70.04 -124.17
REMARK 500 ASP A 286 -149.44 -109.64
REMARK 500 THR A 298 32.14 -97.04
REMARK 500 THR B 101 13.30 59.49
REMARK 500 SER B 170 -114.98 51.16
REMARK 500 THR B 193 56.06 32.33
REMARK 500 SER B 224 -76.53 -133.17
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 ILE A 124 ASP A 125 149.70
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 677 DISTANCE = 6.23 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 LI A 404 LI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 214 OD2
REMARK 620 2 ASP A 244 OD1 86.1
REMARK 620 3 ASN B 230 O 58.2 29.9
REMARK 620 4 LEU B 232 O 60.6 27.2 2.8
REMARK 620 N 1 2 3
DBREF 7XTR A 41 301 PDB 7XTR 7XTR 41 301
DBREF 7XTR B 41 301 PDB 7XTR 7XTR 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 SER
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 SER ALA LYS PRO ILE 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 SER
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 SER ALA LYS PRO ILE 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
HET SO4 A 401 5
HET GOL A 402 6
HET GOL A 403 6
HET LI A 404 1
HET SO4 B 401 5
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM LI LITHIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 LI LI 1+
FORMUL 8 HOH *338(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 SER 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 SER 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 MET A 167 N ALA A 95
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 VAL A 292 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 VAL B 120
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 294 N GLU B 242
SSBOND 1 CYS A 281 CYS A 299 1555 1555 2.06
SSBOND 2 CYS B 281 CYS B 299 1555 1555 2.03
LINK OD2 ASP A 214 LI LI A 404 1555 1555 2.23
LINK OD1 ASP A 244 LI LI A 404 1555 1555 2.32
LINK LI LI A 404 O ASN B 230 1455 1555 2.21
LINK LI LI A 404 O LEU B 232 1455 1555 2.39
CISPEP 1 CYS A 281 PRO A 282 0 1.11
CISPEP 2 CYS A 299 PRO A 300 0 13.05
CISPEP 3 CYS B 281 PRO B 282 0 11.18
CISPEP 4 CYS B 299 PRO B 300 0 -6.19
CRYST1 65.689 41.961 80.767 90.00 92.61 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 0.015223 0.000000 0.000694 0.00000
SCALE2 0.000000 0.023832 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012394 0.00000
TER 1970 PHE A 301
TER 3921 PHE B 301
MASTER 322 0 5 22 18 0 0 6 4280 2 29 42
END |