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HEADER HYDROLASE 11-MAR-21 7EC8
TITLE POLYETHYLENE TEREPHTHALATE HYDROLYZING LIPASE PET2 MUTANT - F105R-
TITLE 2 E110K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPIAF5-2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: LIPIAF5-2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET27B
KEYWDS POLYETHYLENE TEREPHTHALATE HYDROLASE, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NAKAMURA
REVDAT 1 07-JUL-21 7EC8 0
JRNL AUTH A.NAKAMURA
JRNL TITL POSITIVE CHARGE INTRODUCTION ON THE SURFACE OF
JRNL TITL 2 THERMOSTABILIZED PET HYDROLASE FACILITATES PET BINDING AND
JRNL TITL 3 DEGRADATION.
JRNL REF ACS CATALYSIS 2021
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.1C01204
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 111776
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5588
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 33.4000 - 4.1800 1.00 3803 200 0.1502 0.1641
REMARK 3 2 4.1800 - 3.3200 1.00 3672 193 0.1369 0.1689
REMARK 3 3 3.3200 - 2.9000 1.00 3612 190 0.1539 0.1764
REMARK 3 4 2.9000 - 2.6400 1.00 3624 191 0.1570 0.1752
REMARK 3 5 2.6400 - 2.4500 1.00 3588 189 0.1553 0.1858
REMARK 3 6 2.4500 - 2.3000 1.00 3570 188 0.1492 0.1636
REMARK 3 7 2.3000 - 2.1900 1.00 3586 188 0.1576 0.1907
REMARK 3 8 2.1900 - 2.0900 1.00 3562 188 0.1606 0.1862
REMARK 3 9 2.0900 - 2.0100 1.00 3550 187 0.1609 0.1963
REMARK 3 10 2.0100 - 1.9400 1.00 3584 188 0.1591 0.2022
REMARK 3 11 1.9400 - 1.8800 1.00 3523 186 0.1631 0.2089
REMARK 3 12 1.8800 - 1.8300 1.00 3563 187 0.1670 0.2182
REMARK 3 13 1.8300 - 1.7800 1.00 3513 184 0.1672 0.1926
REMARK 3 14 1.7800 - 1.7400 1.00 3572 188 0.1734 0.2117
REMARK 3 15 1.7400 - 1.7000 1.00 3519 186 0.1708 0.1886
REMARK 3 16 1.7000 - 1.6600 1.00 3515 185 0.1789 0.2297
REMARK 3 17 1.6600 - 1.6300 1.00 3546 187 0.1871 0.2070
REMARK 3 18 1.6300 - 1.6000 1.00 3538 185 0.1835 0.2232
REMARK 3 19 1.6000 - 1.5700 1.00 3498 184 0.1930 0.2075
REMARK 3 20 1.5700 - 1.5400 1.00 3524 186 0.1961 0.2388
REMARK 3 21 1.5400 - 1.5200 1.00 3493 183 0.1910 0.2315
REMARK 3 22 1.5200 - 1.4900 0.99 3501 185 0.2010 0.2379
REMARK 3 23 1.4900 - 1.4700 0.99 3494 184 0.2084 0.2264
REMARK 3 24 1.4700 - 1.4500 1.00 3497 184 0.2157 0.2227
REMARK 3 25 1.4500 - 1.4300 0.99 3510 185 0.2321 0.2492
REMARK 3 26 1.4300 - 1.4100 0.99 3480 183 0.2528 0.3009
REMARK 3 27 1.4100 - 1.4000 0.99 3483 183 0.2746 0.3303
REMARK 3 28 1.4000 - 1.3800 0.99 3488 184 0.2907 0.3220
REMARK 3 29 1.3800 - 1.3600 0.99 3477 183 0.3109 0.3131
REMARK 3 30 1.3600 - 1.3500 0.94 3303 174 0.4043 0.4227
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) : 0.169
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.361
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.56
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 : 0.012 4371
REMARK 3 ANGLE : 1.121 5962
REMARK 3 CHIRALITY : 0.094 627
REMARK 3 PLANARITY : 0.008 787
REMARK 3 DIHEDRAL : 21.615 1573
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 7EC8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAR-21.
REMARK 100 THE DEPOSITION ID IS D_1300021141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AICHISR
REMARK 200 BEAMLINE : BL2S1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 111811
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 33.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 13.60
REMARK 200 R MERGE FOR SHELL (I) : 1.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM SULFATE IN 100 MM TRIS
REMARK 280 -HCL PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 35.52500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.05500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.05500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.52500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.24500
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
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 ALA A 28
REMARK 465 ASN A 29
REMARK 465 PRO A 30
REMARK 465 PRO A 31
REMARK 465 GLY A 32
REMARK 465 GLY A 33
REMARK 465 ASP A 34
REMARK 465 PRO A 35
REMARK 465 ASP A 36
REMARK 465 PRO A 37
REMARK 465 GLY A 38
REMARK 465 CYS A 39
REMARK 465 GLN A 40
REMARK 465 THR A 41
REMARK 465 ASP A 42
REMARK 465 CYS A 43
REMARK 465 ASN A 44
REMARK 465 ASN A 310
REMARK 465 LEU A 311
REMARK 465 TYR A 312
REMARK 465 PHE A 313
REMARK 465 GLN A 314
REMARK 465 GLY A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 ALA B 28
REMARK 465 ASN B 29
REMARK 465 PRO B 30
REMARK 465 PRO B 31
REMARK 465 GLY B 32
REMARK 465 GLY B 33
REMARK 465 ASP B 34
REMARK 465 PRO B 35
REMARK 465 ASP B 36
REMARK 465 PRO B 37
REMARK 465 GLY B 38
REMARK 465 CYS B 39
REMARK 465 GLN B 40
REMARK 465 THR B 41
REMARK 465 ASP B 42
REMARK 465 CYS B 43
REMARK 465 ASN B 44
REMARK 465 ASN B 310
REMARK 465 LEU B 311
REMARK 465 TYR B 312
REMARK 465 PHE B 313
REMARK 465 GLN B 314
REMARK 465 GLY B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
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 507 O HOH A 540 2.01
REMARK 500 O HOH A 521 O HOH A 677 2.03
REMARK 500 O HOH A 591 O HOH A 755 2.06
REMARK 500 O HOH A 808 O HOH A 823 2.06
REMARK 500 NH2 ARG A 139 OD1 ASP A 187 2.07
REMARK 500 O HOH A 650 O HOH A 657 2.07
REMARK 500 O HOH B 525 O HOH B 554 2.11
REMARK 500 O HOH A 583 O HOH A 798 2.13
REMARK 500 O HOH B 641 O HOH B 747 2.14
REMARK 500 O HOH B 641 O HOH B 783 2.15
REMARK 500 O HOH A 792 O HOH B 571 2.16
REMARK 500 O HOH A 626 O HOH A 726 2.16
REMARK 500 O HOH A 708 O HOH A 774 2.16
REMARK 500 O HOH A 503 O HOH A 773 2.16
REMARK 500 OE1 GLU A 57 O HOH A 501 2.16
REMARK 500 O HOH A 521 O HOH A 819 2.18
REMARK 500 O HOH A 516 O HOH A 794 2.18
REMARK 500 OD1 ASN B 129 O HOH B 501 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 837 O HOH B 801 4465 2.14
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 175 -123.15 61.84
REMARK 500 HIS A 229 -90.58 -128.18
REMARK 500 SER B 175 -129.36 65.78
REMARK 500 HIS B 229 -87.23 -126.24
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 848 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A 849 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A 850 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 805 DISTANCE = 6.75 ANGSTROMS
DBREF 7EC8 A 28 308 UNP C3RYL0 C3RYL0_9BACT 28 308
DBREF 7EC8 B 28 308 UNP C3RYL0 C3RYL0_9BACT 28 308
SEQADV 7EC8 ARG A 105 UNP C3RYL0 PHE 105 ENGINEERED MUTATION
SEQADV 7EC8 LYS A 110 UNP C3RYL0 GLU 110 ENGINEERED MUTATION
SEQADV 7EC8 GLU A 309 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 ASN A 310 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 LEU A 311 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 TYR A 312 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 PHE A 313 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 GLN A 314 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 GLY A 315 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS A 316 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS A 317 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS A 318 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS A 319 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS A 320 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS A 321 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 ARG B 105 UNP C3RYL0 PHE 105 ENGINEERED MUTATION
SEQADV 7EC8 LYS B 110 UNP C3RYL0 GLU 110 ENGINEERED MUTATION
SEQADV 7EC8 GLU B 309 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 ASN B 310 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 LEU B 311 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 TYR B 312 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 PHE B 313 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 GLN B 314 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 GLY B 315 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS B 316 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS B 317 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS B 318 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS B 319 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS B 320 UNP C3RYL0 EXPRESSION TAG
SEQADV 7EC8 HIS B 321 UNP C3RYL0 EXPRESSION TAG
SEQRES 1 A 294 ALA ASN PRO PRO GLY GLY ASP PRO ASP PRO GLY CYS GLN
SEQRES 2 A 294 THR ASP CYS ASN TYR GLN ARG GLY PRO ASP PRO THR ASP
SEQRES 3 A 294 ALA TYR LEU GLU ALA ALA SER GLY PRO TYR THR VAL SER
SEQRES 4 A 294 THR ILE ARG VAL SER SER LEU VAL PRO GLY PHE GLY GLY
SEQRES 5 A 294 GLY THR ILE HIS TYR PRO THR ASN ALA GLY GLY GLY LYS
SEQRES 6 A 294 MET ALA GLY ILE VAL VAL ILE PRO GLY TYR LEU SER ARG
SEQRES 7 A 294 GLU SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER
SEQRES 8 A 294 HIS GLY PHE VAL VAL MET THR ILE ASP THR ASN THR ILE
SEQRES 9 A 294 TYR ASP GLN PRO SER GLN ARG ARG ASP GLN ILE GLU ALA
SEQRES 10 A 294 ALA LEU GLN TYR LEU VAL ASN GLN SER ASN SER SER SER
SEQRES 11 A 294 SER PRO ILE SER GLY MET VAL ASP SER SER ARG LEU ALA
SEQRES 12 A 294 ALA VAL GLY TRP SER MET GLY GLY GLY GLY THR LEU GLN
SEQRES 13 A 294 LEU ALA ALA ASP GLY GLY ILE LYS ALA ALA ILE ALA LEU
SEQRES 14 A 294 ALA PRO TRP ASN SER SER ILE ASN ASP PHE ASN ARG ILE
SEQRES 15 A 294 GLN VAL PRO THR LEU ILE PHE ALA CYS GLN LEU ASP ALA
SEQRES 16 A 294 ILE ALA PRO VAL ALA LEU HIS ALA SER PRO PHE TYR ASN
SEQRES 17 A 294 ARG ILE PRO ASN THR THR PRO LYS ALA PHE PHE GLU MET
SEQRES 18 A 294 THR GLY GLY ASP HIS TRP CYS ALA ASN GLY GLY ASN ILE
SEQRES 19 A 294 TYR SER ALA LEU LEU GLY LYS TYR GLY VAL SER TRP MET
SEQRES 20 A 294 LYS LEU HIS LEU ASP GLN ASP THR ARG TYR ALA PRO PHE
SEQRES 21 A 294 LEU CYS GLY PRO ASN HIS ALA ALA GLN THR LEU ILE SER
SEQRES 22 A 294 GLU TYR ARG GLY ASN CYS PRO TYR GLU ASN LEU TYR PHE
SEQRES 23 A 294 GLN GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 294 ALA ASN PRO PRO GLY GLY ASP PRO ASP PRO GLY CYS GLN
SEQRES 2 B 294 THR ASP CYS ASN TYR GLN ARG GLY PRO ASP PRO THR ASP
SEQRES 3 B 294 ALA TYR LEU GLU ALA ALA SER GLY PRO TYR THR VAL SER
SEQRES 4 B 294 THR ILE ARG VAL SER SER LEU VAL PRO GLY PHE GLY GLY
SEQRES 5 B 294 GLY THR ILE HIS TYR PRO THR ASN ALA GLY GLY GLY LYS
SEQRES 6 B 294 MET ALA GLY ILE VAL VAL ILE PRO GLY TYR LEU SER ARG
SEQRES 7 B 294 GLU SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER
SEQRES 8 B 294 HIS GLY PHE VAL VAL MET THR ILE ASP THR ASN THR ILE
SEQRES 9 B 294 TYR ASP GLN PRO SER GLN ARG ARG ASP GLN ILE GLU ALA
SEQRES 10 B 294 ALA LEU GLN TYR LEU VAL ASN GLN SER ASN SER SER SER
SEQRES 11 B 294 SER PRO ILE SER GLY MET VAL ASP SER SER ARG LEU ALA
SEQRES 12 B 294 ALA VAL GLY TRP SER MET GLY GLY GLY GLY THR LEU GLN
SEQRES 13 B 294 LEU ALA ALA ASP GLY GLY ILE LYS ALA ALA ILE ALA LEU
SEQRES 14 B 294 ALA PRO TRP ASN SER SER ILE ASN ASP PHE ASN ARG ILE
SEQRES 15 B 294 GLN VAL PRO THR LEU ILE PHE ALA CYS GLN LEU ASP ALA
SEQRES 16 B 294 ILE ALA PRO VAL ALA LEU HIS ALA SER PRO PHE TYR ASN
SEQRES 17 B 294 ARG ILE PRO ASN THR THR PRO LYS ALA PHE PHE GLU MET
SEQRES 18 B 294 THR GLY GLY ASP HIS TRP CYS ALA ASN GLY GLY ASN ILE
SEQRES 19 B 294 TYR SER ALA LEU LEU GLY LYS TYR GLY VAL SER TRP MET
SEQRES 20 B 294 LYS LEU HIS LEU ASP GLN ASP THR ARG TYR ALA PRO PHE
SEQRES 21 B 294 LEU CYS GLY PRO ASN HIS ALA ALA GLN THR LEU ILE SER
SEQRES 22 B 294 GLU TYR ARG GLY ASN CYS PRO TYR GLU ASN LEU TYR PHE
SEQRES 23 B 294 GLN GLY HIS HIS HIS HIS HIS HIS
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET SO4 A 406 5
HET EDO B 401 4
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HET EDO B 405 4
HET EDO B 406 8
HET EDO B 407 4
HET EDO B 408 8
HET EDO B 409 4
HET SO4 B 410 5
HET SO4 B 411 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 14(C2 H6 O2)
FORMUL 8 SO4 3(O4 S 2-)
FORMUL 20 HOH *655(H2 O)
HELIX 1 AA1 THR A 52 ALA A 58 1 7
HELIX 2 AA2 ARG A 105 LYS A 110 5 6
HELIX 3 AA3 TRP A 111 SER A 118 1 8
HELIX 4 AA4 GLN A 134 SER A 155 1 22
HELIX 5 AA5 SER A 175 GLY A 188 1 14
HELIX 6 AA6 ASP A 205 ILE A 209 5 5
HELIX 7 AA7 HIS A 229 ILE A 237 1 9
HELIX 8 AA8 TRP A 254 GLY A 258 5 5
HELIX 9 AA9 TYR A 262 GLN A 280 1 19
HELIX 10 AB1 ASP A 281 ARG A 283 5 3
HELIX 11 AB2 TYR A 284 CYS A 289 1 6
HELIX 12 AB3 ASN A 292 GLN A 296 5 5
HELIX 13 AB4 THR B 52 ALA B 58 1 7
HELIX 14 AB5 ARG B 105 LYS B 110 5 6
HELIX 15 AB6 TRP B 111 SER B 118 1 8
HELIX 16 AB7 GLN B 134 SER B 155 1 22
HELIX 17 AB8 SER B 175 GLY B 188 1 14
HELIX 18 AB9 ASP B 205 ILE B 209 5 5
HELIX 19 AC1 HIS B 229 ILE B 237 1 9
HELIX 20 AC2 TRP B 254 GLY B 258 5 5
HELIX 21 AC3 TYR B 262 ASP B 279 1 18
HELIX 22 AC4 ASP B 281 LEU B 288 5 8
HELIX 23 AC5 ASN B 292 GLN B 296 5 5
SHEET 1 AA1 9 VAL A 65 VAL A 70 0
SHEET 2 AA1 9 GLY A 80 PRO A 85 -1 O GLY A 80 N VAL A 70
SHEET 3 AA1 9 VAL A 122 ILE A 126 -1 O VAL A 123 N HIS A 83
SHEET 4 AA1 9 MET A 93 ILE A 99 1 N ILE A 96 O MET A 124
SHEET 5 AA1 9 VAL A 164 TRP A 174 1 O ASP A 165 N MET A 93
SHEET 6 AA1 9 ALA A 192 LEU A 196 1 O LEU A 196 N GLY A 173
SHEET 7 AA1 9 THR A 213 CYS A 218 1 O PHE A 216 N ALA A 195
SHEET 8 AA1 9 LYS A 243 MET A 248 1 O ALA A 244 N ILE A 215
SHEET 9 AA1 9 ILE A 299 GLY A 304 -1 O GLU A 301 N GLU A 247
SHEET 1 AA2 9 VAL B 65 VAL B 70 0
SHEET 2 AA2 9 GLY B 80 PRO B 85 -1 O GLY B 80 N VAL B 70
SHEET 3 AA2 9 VAL B 122 ILE B 126 -1 O VAL B 123 N HIS B 83
SHEET 4 AA2 9 MET B 93 ILE B 99 1 N ILE B 96 O MET B 124
SHEET 5 AA2 9 VAL B 164 TRP B 174 1 O ASP B 165 N MET B 93
SHEET 6 AA2 9 ALA B 192 LEU B 196 1 O LEU B 196 N GLY B 173
SHEET 7 AA2 9 THR B 213 CYS B 218 1 O PHE B 216 N ALA B 195
SHEET 8 AA2 9 LYS B 243 MET B 248 1 O ALA B 244 N ILE B 215
SHEET 9 AA2 9 ILE B 299 GLY B 304 -1 O GLU B 301 N GLU B 247
SSBOND 1 CYS A 218 CYS A 255 1555 1555 2.02
SSBOND 2 CYS A 289 CYS A 306 1555 1555 2.06
SSBOND 3 CYS B 218 CYS B 255 1555 1555 2.06
SSBOND 4 CYS B 289 CYS B 306 1555 1555 2.07
CISPEP 1 PRO A 100 GLY A 101 0 -2.01
CISPEP 2 CYS A 306 PRO A 307 0 -5.44
CISPEP 3 CYS B 306 PRO B 307 0 -3.27
CRYST1 71.050 72.490 98.110 90.00 90.00 90.00 P 21 21 21 8
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 0.014075 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013795 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010193 0.00000
TER 2127 GLU A 309
TER 4176 GLU B 309
MASTER 371 0 17 23 18 0 0 6 4728 2 87 46
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