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HEADER HYDROLASE 09-APR-19 6RB3
TITLE STRUCTURAL BASIS FOR RECOGNITION AND RING-CLEAVAGE OF THE PSEUDOMONAS
TITLE 2 QUINOLONE SIGNAL (PQS) BY AQDC VARIANT IN COMPLEX WITH ITS SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIOXYGENASE (1H-3-HYDROXY-4-OXOQUINALDINE 2,4-
COMPND 3 DIOXYGENASE);
COMPND 4 CHAIN: E, A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM ABSCESSUS;
SOURCE 3 ORGANISM_TAXID: 36809;
SOURCE 4 GENE: MAB_0303;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DIOXYGENASE; ALPHA/BETA HYDROLASE FOLD, CATALYTIC TRIAD, QUORUM
KEYWDS 2 SENSING, PSEUDOMONAS QUINOLONE SIGNAL, PSEUDOMONAS AERUGINOSA,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WULLICH,S.KOBUS,S.H.SMITS,S.FETZNER
REVDAT 1 03-JUL-19 6RB3 0
JRNL AUTH S.C.WULLICH,S.KOBUS,M.WIENHOLD,U.HENNECKE,S.H.J.SMITS,
JRNL AUTH 2 S.FETZNER
JRNL TITL STRUCTURAL BASIS FOR RECOGNITION AND RING-CLEAVAGE OF THE
JRNL TITL 2 PSEUDOMONAS QUINOLONE SIGNAL (PQS) BY AQDC, A MYCOBACTERIAL
JRNL TITL 3 DIOXYGENASE OF THE ALPHA / BETA-HYDROLASE FOLD FAMILY.
JRNL REF J.STRUCT.BIOL. 2019
JRNL REFN ESSN 1095-8657
JRNL PMID 31228546
JRNL DOI 10.1016/J.JSB.2019.06.006
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 40828
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2078
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 47.5446 - 5.6694 1.00 2778 183 0.2015 0.2331
REMARK 3 2 5.6694 - 4.5011 1.00 2649 154 0.1598 0.2065
REMARK 3 3 4.5011 - 3.9324 1.00 2639 127 0.1653 0.2166
REMARK 3 4 3.9324 - 3.5730 1.00 2590 144 0.1807 0.2170
REMARK 3 5 3.5730 - 3.3170 1.00 2584 136 0.2086 0.2903
REMARK 3 6 3.3170 - 3.1215 1.00 2564 146 0.2145 0.2563
REMARK 3 7 3.1215 - 2.9652 1.00 2589 123 0.2093 0.2543
REMARK 3 8 2.9652 - 2.8361 1.00 2539 142 0.1996 0.2458
REMARK 3 9 2.8361 - 2.7269 1.00 2558 150 0.2170 0.2726
REMARK 3 10 2.7269 - 2.6328 1.00 2536 136 0.2167 0.2709
REMARK 3 11 2.6328 - 2.5505 1.00 2549 135 0.2144 0.2908
REMARK 3 12 2.5505 - 2.4776 1.00 2549 117 0.2202 0.2925
REMARK 3 13 2.4776 - 2.4124 1.00 2554 129 0.2049 0.2800
REMARK 3 14 2.4124 - 2.3535 1.00 2523 137 0.2098 0.2617
REMARK 3 15 2.3535 - 2.3000 1.00 2549 119 0.2157 0.2702
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.800
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.33
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 6RB3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101674.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-18
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R CDTE 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40828
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.535
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04034
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18910
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 6RA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M TRI
REMARK 280 SODIUM CITRATE PH 5.6 AND 30% PEG 4000, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 95.06900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.32200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.32200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 142.60350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.32200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.32200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.53450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.32200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.32200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 142.60350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.32200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.32200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 47.53450
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 95.06900
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 3
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 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 546 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 525 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 ARG E 270
REMARK 465 ILE E 271
REMARK 465 ARG A 270
REMARK 465 ILE A 271
REMARK 465 ARG B 270
REMARK 465 ILE B 271
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 MET E 3 CG SD CE
REMARK 470 MET A 3 CG SD CE
REMARK 470 MET B 3 CG SD CE
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 HE ARG B 187 O HOH B 403 1.46
REMARK 500 HE21 GLN A 13 O HOH A 413 1.49
REMARK 500 O VAL A 154 H TRP A 157 1.52
REMARK 500 H GLN A 155 O HOH A 403 1.53
REMARK 500 HE ARG B 241 OE2 GLU B 261 1.58
REMARK 500 O HOH B 517 O HOH B 519 1.81
REMARK 500 N MET B 3 O HOH B 401 1.88
REMARK 500 O ALA E 269 O HOH E 401 1.95
REMARK 500 O HOH B 407 O HOH B 537 1.96
REMARK 500 NH2 ARG A 145 O HOH A 401 1.97
REMARK 500 O HOH E 495 O HOH E 508 1.97
REMARK 500 O HOH A 483 O HOH A 518 2.00
REMARK 500 NH2 ARG B 234 O HOH B 402 2.01
REMARK 500 O HOH E 475 O HOH E 528 2.01
REMARK 500 O HOH A 464 O HOH A 511 2.01
REMARK 500 OD2 ASP A 151 O HOH A 402 2.02
REMARK 500 OE1 GLN A 155 O HOH A 403 2.02
REMARK 500 NH2 ARG A 150 O HOH A 404 2.02
REMARK 500 O HOH B 536 O HOH B 552 2.03
REMARK 500 O PHE E 238 NH1 ARG A 131 2.08
REMARK 500 N GLN A 155 O HOH A 403 2.09
REMARK 500 O HOH A 494 O HOH A 514 2.10
REMARK 500 NH1 ARG A 150 O HOH A 404 2.10
REMARK 500 O HOH E 467 O HOH E 512 2.11
REMARK 500 O HOH E 480 O HOH E 507 2.12
REMARK 500 O ARG A 131 O HOH A 405 2.18
REMARK 500 OG SER E 98 O18 JWW E 301 2.19
REMARK 500 NH2 ARG A 131 O HOH A 406 2.19
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 E 21 89.86 -154.06
REMARK 500 ASP E 36 -159.61 -125.55
REMARK 500 ASP E 90 -108.92 -77.81
REMARK 500 SER E 98 -126.48 50.10
REMARK 500 ASP E 123 70.17 43.00
REMARK 500 ALA E 159 -143.46 49.94
REMARK 500 HIS E 218 -74.09 -89.70
REMARK 500 PRO E 219 130.07 -36.97
REMARK 500 ASP A 36 -161.11 -124.28
REMARK 500 ASP A 90 -114.34 -88.90
REMARK 500 SER A 98 -126.18 43.21
REMARK 500 ASP A 123 82.77 31.79
REMARK 500 ARG A 131 -8.75 -58.35
REMARK 500 VAL A 154 -78.96 -21.11
REMARK 500 ALA A 159 -121.51 78.94
REMARK 500 SER A 174 28.18 -151.06
REMARK 500 HIS A 218 -63.26 -92.44
REMARK 500 ASP B 36 -158.19 -127.70
REMARK 500 ASP B 90 -108.74 -84.69
REMARK 500 SER B 98 -126.07 43.22
REMARK 500 ALA B 159 -131.36 51.91
REMARK 500 HIS B 218 -60.77 -98.68
REMARK 500 ILE B 221 150.45 -49.39
REMARK 500 PHE B 249 62.43 -118.31
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 SER E 217 HIS E 218 -146.08
REMARK 500 SER A 217 HIS A 218 -145.29
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 561 DISTANCE = 5.84 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JWW E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JWW A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JWW B 301
DBREF 6RB3 E 3 271 UNP B1MFK2 B1MFK2_MYCA9 1 269
DBREF 6RB3 A 3 271 UNP B1MFK2 B1MFK2_MYCA9 1 269
DBREF 6RB3 B 3 271 UNP B1MFK2 B1MFK2_MYCA9 1 269
SEQADV 6RB3 SER E 98 UNP B1MFK2 ALA 96 ENGINEERED MUTATION
SEQADV 6RB3 ALA E 248 UNP B1MFK2 HIS 246 ENGINEERED MUTATION
SEQADV 6RB3 SER A 98 UNP B1MFK2 ALA 96 ENGINEERED MUTATION
SEQADV 6RB3 ALA A 248 UNP B1MFK2 HIS 246 ENGINEERED MUTATION
SEQADV 6RB3 SER B 98 UNP B1MFK2 ALA 96 ENGINEERED MUTATION
SEQADV 6RB3 ALA B 248 UNP B1MFK2 HIS 246 ENGINEERED MUTATION
SEQRES 1 E 269 MET ILE THR THR LYS THR VAL ASN GLY VAL GLN ILE ALA
SEQRES 2 E 269 PHE ASP ASP GLN GLY HIS GLU PRO GLY PRO VAL PHE VAL
SEQRES 3 E 269 THR LEU SER GLY TRP ALA HIS ASP LEU ARG ALA TYR ASP
SEQRES 4 E 269 GLY MET LEU PRO TYR LEU ARG ALA ALA GLN ARG THR VAL
SEQRES 5 E 269 ARG VAL CYS TRP ARG GLY HIS GLY PRO ASP ARG ASN LEU
SEQRES 6 E 269 VAL GLY ASP PHE GLY ILE ASP GLU MET ALA ALA ASP THR
SEQRES 7 E 269 ILE GLY LEU LEU ASP ALA LEU GLU VAL ASP SER PHE VAL
SEQRES 8 E 269 PRO ILE ALA HIS SER HIS GLY GLY TRP ALA ALA LEU GLU
SEQRES 9 E 269 ILE ALA ASP ARG LEU GLY ALA GLN ARG VAL PRO ALA VAL
SEQRES 10 E 269 MET ILE LEU ASP LEU ILE MET THR PRO ALA PRO ARG GLU
SEQRES 11 E 269 PHE VAL ALA ALA LEU HIS GLY ILE GLN ASP PRO GLU ARG
SEQRES 12 E 269 TRP LYS GLU GLY ARG ASP GLY LEU VAL GLN SER TRP LEU
SEQRES 13 E 269 ALA GLY THR THR ASN GLN ALA VAL LEU ASP HIS VAL ARG
SEQRES 14 E 269 TYR ASP SER GLY GLY HIS GLY PHE ASP MET TRP ALA ARG
SEQRES 15 E 269 ALA GLY ARG VAL ILE ASP GLU ALA TYR ARG THR TRP GLY
SEQRES 16 E 269 SER PRO MET ARG ARG MET GLU ALA LEU ALA GLU PRO CYS
SEQRES 17 E 269 ALA ILE ARG HIS VAL PHE SER HIS PRO LYS ILE GLY GLU
SEQRES 18 E 269 TYR ASP ALA LEU HIS ASP ASP PHE ALA ALA ARG HIS PRO
SEQRES 19 E 269 TRP PHE SER TYR ARG ARG LEU GLY GLY GLU THR ALA PHE
SEQRES 20 E 269 PRO GLY ILE GLU LEU PRO GLN GLN VAL ALA ALA GLU ALA
SEQRES 21 E 269 ILE ASP LEU LEU ALA GLY ALA ARG ILE
SEQRES 1 A 269 MET ILE THR THR LYS THR VAL ASN GLY VAL GLN ILE ALA
SEQRES 2 A 269 PHE ASP ASP GLN GLY HIS GLU PRO GLY PRO VAL PHE VAL
SEQRES 3 A 269 THR LEU SER GLY TRP ALA HIS ASP LEU ARG ALA TYR ASP
SEQRES 4 A 269 GLY MET LEU PRO TYR LEU ARG ALA ALA GLN ARG THR VAL
SEQRES 5 A 269 ARG VAL CYS TRP ARG GLY HIS GLY PRO ASP ARG ASN LEU
SEQRES 6 A 269 VAL GLY ASP PHE GLY ILE ASP GLU MET ALA ALA ASP THR
SEQRES 7 A 269 ILE GLY LEU LEU ASP ALA LEU GLU VAL ASP SER PHE VAL
SEQRES 8 A 269 PRO ILE ALA HIS SER HIS GLY GLY TRP ALA ALA LEU GLU
SEQRES 9 A 269 ILE ALA ASP ARG LEU GLY ALA GLN ARG VAL PRO ALA VAL
SEQRES 10 A 269 MET ILE LEU ASP LEU ILE MET THR PRO ALA PRO ARG GLU
SEQRES 11 A 269 PHE VAL ALA ALA LEU HIS GLY ILE GLN ASP PRO GLU ARG
SEQRES 12 A 269 TRP LYS GLU GLY ARG ASP GLY LEU VAL GLN SER TRP LEU
SEQRES 13 A 269 ALA GLY THR THR ASN GLN ALA VAL LEU ASP HIS VAL ARG
SEQRES 14 A 269 TYR ASP SER GLY GLY HIS GLY PHE ASP MET TRP ALA ARG
SEQRES 15 A 269 ALA GLY ARG VAL ILE ASP GLU ALA TYR ARG THR TRP GLY
SEQRES 16 A 269 SER PRO MET ARG ARG MET GLU ALA LEU ALA GLU PRO CYS
SEQRES 17 A 269 ALA ILE ARG HIS VAL PHE SER HIS PRO LYS ILE GLY GLU
SEQRES 18 A 269 TYR ASP ALA LEU HIS ASP ASP PHE ALA ALA ARG HIS PRO
SEQRES 19 A 269 TRP PHE SER TYR ARG ARG LEU GLY GLY GLU THR ALA PHE
SEQRES 20 A 269 PRO GLY ILE GLU LEU PRO GLN GLN VAL ALA ALA GLU ALA
SEQRES 21 A 269 ILE ASP LEU LEU ALA GLY ALA ARG ILE
SEQRES 1 B 269 MET ILE THR THR LYS THR VAL ASN GLY VAL GLN ILE ALA
SEQRES 2 B 269 PHE ASP ASP GLN GLY HIS GLU PRO GLY PRO VAL PHE VAL
SEQRES 3 B 269 THR LEU SER GLY TRP ALA HIS ASP LEU ARG ALA TYR ASP
SEQRES 4 B 269 GLY MET LEU PRO TYR LEU ARG ALA ALA GLN ARG THR VAL
SEQRES 5 B 269 ARG VAL CYS TRP ARG GLY HIS GLY PRO ASP ARG ASN LEU
SEQRES 6 B 269 VAL GLY ASP PHE GLY ILE ASP GLU MET ALA ALA ASP THR
SEQRES 7 B 269 ILE GLY LEU LEU ASP ALA LEU GLU VAL ASP SER PHE VAL
SEQRES 8 B 269 PRO ILE ALA HIS SER HIS GLY GLY TRP ALA ALA LEU GLU
SEQRES 9 B 269 ILE ALA ASP ARG LEU GLY ALA GLN ARG VAL PRO ALA VAL
SEQRES 10 B 269 MET ILE LEU ASP LEU ILE MET THR PRO ALA PRO ARG GLU
SEQRES 11 B 269 PHE VAL ALA ALA LEU HIS GLY ILE GLN ASP PRO GLU ARG
SEQRES 12 B 269 TRP LYS GLU GLY ARG ASP GLY LEU VAL GLN SER TRP LEU
SEQRES 13 B 269 ALA GLY THR THR ASN GLN ALA VAL LEU ASP HIS VAL ARG
SEQRES 14 B 269 TYR ASP SER GLY GLY HIS GLY PHE ASP MET TRP ALA ARG
SEQRES 15 B 269 ALA GLY ARG VAL ILE ASP GLU ALA TYR ARG THR TRP GLY
SEQRES 16 B 269 SER PRO MET ARG ARG MET GLU ALA LEU ALA GLU PRO CYS
SEQRES 17 B 269 ALA ILE ARG HIS VAL PHE SER HIS PRO LYS ILE GLY GLU
SEQRES 18 B 269 TYR ASP ALA LEU HIS ASP ASP PHE ALA ALA ARG HIS PRO
SEQRES 19 B 269 TRP PHE SER TYR ARG ARG LEU GLY GLY GLU THR ALA PHE
SEQRES 20 B 269 PRO GLY ILE GLU LEU PRO GLN GLN VAL ALA ALA GLU ALA
SEQRES 21 B 269 ILE ASP LEU LEU ALA GLY ALA ARG ILE
HET JWW E 301 39
HET JWW A 301 39
HET JWW B 301 39
HETNAM JWW 2-HEPTYLQUINOLINE-3,4-DIOL
FORMUL 4 JWW 3(C16 H21 N O2)
FORMUL 7 HOH *448(H2 O)
HELIX 1 AA1 ASP E 36 ASP E 41 5 6
HELIX 2 AA2 MET E 43 GLN E 51 1 9
HELIX 3 AA3 GLY E 72 GLU E 88 1 17
HELIX 4 AA4 HIS E 99 VAL E 116 1 18
HELIX 5 AA5 PRO E 130 ILE E 140 1 11
HELIX 6 AA6 ARG E 145 ALA E 159 1 15
HELIX 7 AA7 ASN E 163 ASP E 173 1 11
HELIX 8 AA8 GLY E 178 GLY E 197 1 20
HELIX 9 AA9 SER E 198 ALA E 205 1 8
HELIX 10 AB1 GLY E 222 HIS E 235 1 14
HELIX 11 AB2 PHE E 249 LEU E 254 1 6
HELIX 12 AB3 LEU E 254 GLY E 268 1 15
HELIX 13 AB4 ASP A 36 ASP A 41 5 6
HELIX 14 AB5 MET A 43 GLN A 51 1 9
HELIX 15 AB6 GLY A 72 LEU A 87 1 16
HELIX 16 AB7 HIS A 99 GLY A 112 1 14
HELIX 17 AB8 PRO A 130 ILE A 140 1 11
HELIX 18 AB9 ARG A 145 ALA A 159 1 15
HELIX 19 AC1 ASN A 163 ASP A 173 1 11
HELIX 20 AC2 GLY A 178 GLY A 197 1 20
HELIX 21 AC3 SER A 198 ALA A 205 1 8
HELIX 22 AC4 GLY A 222 HIS A 235 1 14
HELIX 23 AC5 PHE A 249 LEU A 254 1 6
HELIX 24 AC6 LEU A 254 ALA A 269 1 16
HELIX 25 AC7 ASP B 36 ASP B 41 5 6
HELIX 26 AC8 MET B 43 GLN B 51 1 9
HELIX 27 AC9 GLY B 72 LEU B 87 1 16
HELIX 28 AD1 HIS B 99 VAL B 116 1 18
HELIX 29 AD2 PRO B 130 ILE B 140 1 11
HELIX 30 AD3 ARG B 145 ALA B 159 1 15
HELIX 31 AD4 ASN B 163 TYR B 172 1 10
HELIX 32 AD5 GLY B 178 GLY B 197 1 20
HELIX 33 AD6 SER B 198 ALA B 205 1 8
HELIX 34 AD7 GLY B 222 HIS B 235 1 14
HELIX 35 AD8 PHE B 249 LEU B 254 1 6
HELIX 36 AD9 LEU B 254 ALA B 269 1 16
SHEET 1 AA1 8 THR E 5 VAL E 9 0
SHEET 2 AA1 8 VAL E 12 GLN E 19 -1 O ILE E 14 N LYS E 7
SHEET 3 AA1 8 THR E 53 VAL E 56 -1 O THR E 53 N GLN E 19
SHEET 4 AA1 8 VAL E 26 LEU E 30 1 N PHE E 27 O VAL E 54
SHEET 5 AA1 8 PHE E 92 HIS E 97 1 O VAL E 93 N VAL E 26
SHEET 6 AA1 8 ALA E 118 LEU E 122 1 O MET E 120 N PRO E 94
SHEET 7 AA1 8 ALA E 211 PHE E 216 1 O ARG E 213 N ILE E 121
SHEET 8 AA1 8 PHE E 238 ARG E 242 1 O SER E 239 N HIS E 214
SHEET 1 AA2 8 THR A 5 VAL A 9 0
SHEET 2 AA2 8 VAL A 12 GLN A 19 -1 O VAL A 12 N VAL A 9
SHEET 3 AA2 8 THR A 53 VAL A 56 -1 O THR A 53 N GLN A 19
SHEET 4 AA2 8 VAL A 26 LEU A 30 1 N PHE A 27 O VAL A 54
SHEET 5 AA2 8 PHE A 92 HIS A 97 1 O ILE A 95 N VAL A 28
SHEET 6 AA2 8 ALA A 118 LEU A 122 1 O LEU A 122 N ALA A 96
SHEET 7 AA2 8 ALA A 211 PHE A 216 1 O ARG A 213 N ILE A 121
SHEET 8 AA2 8 PHE A 238 ARG A 242 1 O SER A 239 N ILE A 212
SHEET 1 AA3 8 THR B 5 VAL B 9 0
SHEET 2 AA3 8 VAL B 12 GLN B 19 -1 O ILE B 14 N LYS B 7
SHEET 3 AA3 8 THR B 53 VAL B 56 -1 O THR B 53 N GLN B 19
SHEET 4 AA3 8 VAL B 26 LEU B 30 1 N PHE B 27 O VAL B 54
SHEET 5 AA3 8 PHE B 92 HIS B 97 1 O ILE B 95 N LEU B 30
SHEET 6 AA3 8 ALA B 118 LEU B 122 1 O MET B 120 N PRO B 94
SHEET 7 AA3 8 ALA B 211 PHE B 216 1 O ARG B 213 N ILE B 121
SHEET 8 AA3 8 PHE B 238 ARG B 242 1 O SER B 239 N ILE B 212
SITE 1 AC1 14 GLY E 32 TRP E 33 HIS E 35 HIS E 97
SITE 2 AC1 14 SER E 98 HIS E 99 PHE E 133 ILE E 140
SITE 3 AC1 14 LEU E 153 TRP E 157 SER E 174 TRP E 182
SITE 4 AC1 14 HOH E 423 HOH E 498
SITE 1 AC2 12 GLY A 32 TRP A 33 HIS A 35 HIS A 97
SITE 2 AC2 12 SER A 98 HIS A 99 PHE A 133 LEU A 153
SITE 3 AC2 12 TRP A 157 SER A 174 HOH A 409 HOH A 410
SITE 1 AC3 11 GLY B 32 TRP B 33 HIS B 35 HIS B 97
SITE 2 AC3 11 SER B 98 HIS B 99 PHE B 133 TRP B 157
SITE 3 AC3 11 ALA B 185 ILE B 189 HOH B 474
CRYST1 96.644 96.644 190.138 90.00 90.00 90.00 P 43 21 2 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 0.010347 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005259 0.00000
TER 4059 ALA E 269
TER 8118 ALA A 269
TER 12177 ALA B 269
MASTER 380 0 3 36 24 0 10 6 6727 3 117 63
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