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HEADER HYDROLASE 05-APR-19 6RA3
TITLE STRUCTURAL BASIS FOR RECOGNITION AND RING-CLEAVAGE OF THE PSEUDOMONAS
TITLE 2 QUINOLONE SIGNAL (PQS) BY AQDC IN COMPLEX WITH ITS PRODUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIOXYGENASE (1H-3-HYDROXY-4-OXOQUINALDINE 2,4-
COMPND 3 DIOXYGENASE);
COMPND 4 CHAIN: A, F, E;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTEROIDES ABSCESSUS SUBSP. ABSCESSUS;
SOURCE 3 ORGANISM_TAXID: 1185650;
SOURCE 4 GENE: SAMEA2070698_02780, SAMEA2161603_04096, SAMEA2275805_05965;
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 6RA3 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. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 60826
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 3007
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 4.8100 - 5.5152 1.00 3018 154 0.1851 0.2164
REMARK 3 2 5.5152 - 4.3786 1.00 2853 148 0.1440 0.1783
REMARK 3 3 4.3786 - 3.8253 1.00 2797 156 0.1574 0.2351
REMARK 3 4 3.8253 - 3.4757 1.00 2813 131 0.1689 0.2113
REMARK 3 5 3.4757 - 3.2266 1.00 2736 169 0.1883 0.2386
REMARK 3 6 3.2266 - 3.0364 1.00 2762 155 0.1908 0.2336
REMARK 3 7 3.0364 - 2.8844 1.00 2763 140 0.1963 0.2371
REMARK 3 8 2.8844 - 2.7588 1.00 2717 149 0.1952 0.2567
REMARK 3 9 2.7588 - 2.6526 1.00 2741 146 0.2062 0.2747
REMARK 3 10 2.6526 - 2.5611 1.00 2738 136 0.2023 0.2684
REMARK 3 11 2.5611 - 2.4810 1.00 2737 149 0.2022 0.2492
REMARK 3 12 2.4810 - 2.4101 1.00 2718 129 0.2075 0.2713
REMARK 3 13 2.4101 - 2.3467 1.00 2729 132 0.2040 0.2558
REMARK 3 14 2.3467 - 2.2894 1.00 2722 128 0.2125 0.2575
REMARK 3 15 2.2894 - 2.2374 1.00 2725 138 0.2199 0.3048
REMARK 3 16 2.2374 - 2.1898 1.00 2717 147 0.2219 0.3210
REMARK 3 17 2.1898 - 2.1460 1.00 2705 142 0.2340 0.2620
REMARK 3 18 2.1460 - 2.1055 1.00 2721 139 0.2350 0.3114
REMARK 3 19 2.1055 - 2.0679 1.00 2727 134 0.2335 0.3228
REMARK 3 20 2.0679 - 2.0328 1.00 2700 138 0.2548 0.3220
REMARK 3 21 2.0328 - 2.0000 1.00 2680 147 0.2659 0.3494
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.95
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 : 0.011 6397
REMARK 3 ANGLE : 1.066 8711
REMARK 3 CHIRALITY : 0.060 913
REMARK 3 PLANARITY : 0.008 1159
REMARK 3 DIHEDRAL : 12.547 3703
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 6RA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101680.
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 : 2
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-W
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60826
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.086
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : 0.09956
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.68580
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: 2WJ3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.10 TO 0.15 M MAGNESIUM CHLORIDE, 0.1
REMARK 280 M SODIUM CHLORIDE, 0.1 M MES PH 6.5 AND 30 TO 40 % PEG 400 AT
REMARK 280 12C., VAPOR DIFFUSION, HANGING 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 94.80800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.08650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.08650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 142.21200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.08650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.08650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.40400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.08650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.08650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 142.21200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.08650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.08650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 47.40400
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 94.80800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, 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 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 371 LIES ON A SPECIAL POSITION.
REMARK 375 HOH F 494 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 A 270
REMARK 465 ILE A 271
REMARK 465 MET F 3
REMARK 465 ALA F 269
REMARK 465 ARG F 270
REMARK 465 ILE F 271
REMARK 465 ARG E 270
REMARK 465 ILE E 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 A 3 CG SD CE
REMARK 470 LYS A 220 CG CD CE NZ
REMARK 470 HIS F 218 CG ND1 CD2 CE1 NE2
REMARK 470 PRO F 219 CG CD
REMARK 470 LYS F 220 CG CD CE NZ
REMARK 470 ILE F 221 CG1 CG2 CD1
REMARK 470 GLU F 223 CG CD OE1 OE2
REMARK 470 MET E 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 OD1 ASP A 229 HH TYR A 240 1.36
REMARK 500 HE21 GLN F 13 O HOH F 306 1.46
REMARK 500 HG SER A 239 O HOH A 302 1.47
REMARK 500 HH TYR E 172 O HOH E 405 1.48
REMARK 500 O PRO F 219 HH22 ARG F 242 1.49
REMARK 500 HH TYR A 46 O HOH A 304 1.51
REMARK 500 HH TYR F 46 O HOH F 307 1.56
REMARK 500 HE21 GLN A 51 O HOH A 309 1.59
REMARK 500 O HOH F 488 O HOH F 517 1.84
REMARK 500 O HOH A 444 O HOH A 447 1.88
REMARK 500 O LEU F 111 O HOH F 301 1.90
REMARK 500 N ILE F 4 O HOH F 302 1.92
REMARK 500 O GLY F 268 O HOH F 303 1.92
REMARK 500 OE2 GLU E 223 O HOH E 401 1.92
REMARK 500 O ALA E 269 O HOH E 402 1.97
REMARK 500 O HOH F 497 O HOH F 521 1.98
REMARK 500 O2 JWH E 301 O HOH E 403 1.99
REMARK 500 O HOH A 398 O HOH A 453 1.99
REMARK 500 O HIS A 218 N LYS A 220 2.00
REMARK 500 O HOH E 533 O HOH E 586 2.03
REMARK 500 OD1 ASP E 90 O HOH E 404 2.04
REMARK 500 O HOH F 407 O HOH F 467 2.05
REMARK 500 O HOH E 574 O HOH E 618 2.06
REMARK 500 O HOH E 426 O HOH E 450 2.08
REMARK 500 O HOH F 386 O HOH F 490 2.10
REMARK 500 OD1 ASP F 229 O HOH F 304 2.13
REMARK 500 O HOH F 349 O HOH F 427 2.13
REMARK 500 OE2 GLU A 132 O HOH A 301 2.15
REMARK 500 OD1 ASP A 229 OH TYR A 240 2.16
REMARK 500 O HOH F 373 O HOH F 504 2.17
REMARK 500 O HOH F 347 O HOH F 461 2.18
REMARK 500 OH TYR E 172 O HOH E 405 2.18
REMARK 500 O ALA E 159 O HOH E 406 2.19
REMARK 500 O HOH E 592 O HOH E 608 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 F 464 O HOH F 478 8555 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO F 219 N - CA - CB ANGL. DEV. = 7.7 DEGREES
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 ASP A 36 -159.78 -124.37
REMARK 500 ASP A 90 -101.99 -87.32
REMARK 500 ALA A 98 -121.09 33.60
REMARK 500 HIS A 218 -70.99 -98.41
REMARK 500 PRO A 219 -42.48 -10.30
REMARK 500 LYS A 220 -111.07 -160.73
REMARK 500 ILE A 221 -69.00 -150.62
REMARK 500 ARG A 241 107.19 -165.45
REMARK 500 HIS A 248 0.30 -69.78
REMARK 500 HIS F 21 -3.78 -144.31
REMARK 500 ASP F 36 -156.45 -126.20
REMARK 500 ASP F 90 -109.13 -101.70
REMARK 500 ALA F 98 -122.01 39.40
REMARK 500 ASP F 123 73.43 40.76
REMARK 500 GLU F 208 73.21 -154.73
REMARK 500 PRO F 219 64.21 62.33
REMARK 500 ILE F 221 -166.99 -115.75
REMARK 500 ASP E 36 -159.60 -127.76
REMARK 500 ASP E 90 -107.21 -88.08
REMARK 500 ALA E 98 -122.77 43.41
REMARK 500 ILE E 125 109.69 -52.06
REMARK 500 ALA E 159 -130.26 49.61
REMARK 500 HIS E 218 -61.41 -98.53
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 HIS A 218 PRO A 219 -147.88
REMARK 500 HIS F 218 PRO F 219 -135.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JWH E 301
DBREF1 6RA3 A 3 271 UNP A0A1M8M580_9MYCO
DBREF2 6RA3 A A0A1M8M580 1 269
DBREF1 6RA3 F 3 271 UNP A0A1M8M580_9MYCO
DBREF2 6RA3 F A0A1M8M580 1 269
DBREF1 6RA3 E 3 271 UNP A0A1M8M580_9MYCO
DBREF2 6RA3 E A0A1M8M580 1 269
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 ALA 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 HIS 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 F 269 MET ILE THR THR LYS THR VAL ASN GLY VAL GLN ILE ALA
SEQRES 2 F 269 PHE ASP ASP GLN GLY HIS GLU PRO GLY PRO VAL PHE VAL
SEQRES 3 F 269 THR LEU SER GLY TRP ALA HIS ASP LEU ARG ALA TYR ASP
SEQRES 4 F 269 GLY MET LEU PRO TYR LEU ARG ALA ALA GLN ARG THR VAL
SEQRES 5 F 269 ARG VAL CYS TRP ARG GLY HIS GLY PRO ASP ARG ASN LEU
SEQRES 6 F 269 VAL GLY ASP PHE GLY ILE ASP GLU MET ALA ALA ASP THR
SEQRES 7 F 269 ILE GLY LEU LEU ASP ALA LEU GLU VAL ASP SER PHE VAL
SEQRES 8 F 269 PRO ILE ALA HIS ALA HIS GLY GLY TRP ALA ALA LEU GLU
SEQRES 9 F 269 ILE ALA ASP ARG LEU GLY ALA GLN ARG VAL PRO ALA VAL
SEQRES 10 F 269 MET ILE LEU ASP LEU ILE MET THR PRO ALA PRO ARG GLU
SEQRES 11 F 269 PHE VAL ALA ALA LEU HIS GLY ILE GLN ASP PRO GLU ARG
SEQRES 12 F 269 TRP LYS GLU GLY ARG ASP GLY LEU VAL GLN SER TRP LEU
SEQRES 13 F 269 ALA GLY THR THR ASN GLN ALA VAL LEU ASP HIS VAL ARG
SEQRES 14 F 269 TYR ASP SER GLY GLY HIS GLY PHE ASP MET TRP ALA ARG
SEQRES 15 F 269 ALA GLY ARG VAL ILE ASP GLU ALA TYR ARG THR TRP GLY
SEQRES 16 F 269 SER PRO MET ARG ARG MET GLU ALA LEU ALA GLU PRO CYS
SEQRES 17 F 269 ALA ILE ARG HIS VAL PHE SER HIS PRO LYS ILE GLY GLU
SEQRES 18 F 269 TYR ASP ALA LEU HIS ASP ASP PHE ALA ALA ARG HIS PRO
SEQRES 19 F 269 TRP PHE SER TYR ARG ARG LEU GLY GLY GLU THR HIS PHE
SEQRES 20 F 269 PRO GLY ILE GLU LEU PRO GLN GLN VAL ALA ALA GLU ALA
SEQRES 21 F 269 ILE ASP LEU LEU ALA GLY ALA ARG ILE
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 ALA 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 HIS 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
HET JWH E 301 39
HETNAM JWH 2-(OCTANOYLAMINO)BENZOIC ACID
FORMUL 4 JWH C15 H21 N O3
FORMUL 5 HOH *602(H2 O)
HELIX 1 AA1 ASP A 36 ASP A 41 5 6
HELIX 2 AA2 MET A 43 GLN A 51 1 9
HELIX 3 AA3 GLY A 72 LEU A 87 1 16
HELIX 4 AA4 GLY A 100 GLY A 112 1 13
HELIX 5 AA5 PRO A 130 ILE A 140 1 11
HELIX 6 AA6 ARG A 145 ALA A 159 1 15
HELIX 7 AA7 ASN A 163 ASP A 173 1 11
HELIX 8 AA8 GLY A 178 GLY A 197 1 20
HELIX 9 AA9 SER A 198 ALA A 205 1 8
HELIX 10 AB1 GLY A 222 HIS A 235 1 14
HELIX 11 AB2 PHE A 249 LEU A 254 1 6
HELIX 12 AB3 LEU A 254 ALA A 269 1 16
HELIX 13 AB4 ASP F 36 ASP F 41 5 6
HELIX 14 AB5 MET F 43 GLN F 51 1 9
HELIX 15 AB6 GLY F 72 LEU F 87 1 16
HELIX 16 AB7 HIS F 99 VAL F 116 1 18
HELIX 17 AB8 PRO F 130 ILE F 140 1 11
HELIX 18 AB9 ARG F 145 ALA F 159 1 15
HELIX 19 AC1 ASN F 163 ASP F 173 1 11
HELIX 20 AC2 GLY F 178 GLY F 197 1 20
HELIX 21 AC3 SER F 198 ALA F 205 1 8
HELIX 22 AC4 GLY F 222 HIS F 235 1 14
HELIX 23 AC5 PHE F 249 LEU F 254 1 6
HELIX 24 AC6 LEU F 254 GLY F 268 1 15
HELIX 25 AC7 ASP E 36 ASP E 41 5 6
HELIX 26 AC8 MET E 43 GLN E 51 1 9
HELIX 27 AC9 GLY E 72 GLU E 88 1 17
HELIX 28 AD1 HIS E 99 VAL E 116 1 18
HELIX 29 AD2 PRO E 130 ILE E 140 1 11
HELIX 30 AD3 ARG E 145 ALA E 159 1 15
HELIX 31 AD4 ASN E 163 ASP E 173 1 11
HELIX 32 AD5 GLY E 178 GLY E 197 1 20
HELIX 33 AD6 SER E 198 ALA E 205 1 8
HELIX 34 AD7 GLY E 222 HIS E 235 1 14
HELIX 35 AD8 PHE E 249 LEU E 254 1 6
HELIX 36 AD9 LEU E 254 ALA E 269 1 16
SHEET 1 AA1 8 THR A 5 VAL A 9 0
SHEET 2 AA1 8 VAL A 12 GLN A 19 -1 O ILE A 14 N LYS A 7
SHEET 3 AA1 8 THR A 53 VAL A 56 -1 O THR A 53 N GLN A 19
SHEET 4 AA1 8 VAL A 26 LEU A 30 1 N PHE A 27 O VAL A 54
SHEET 5 AA1 8 PHE A 92 HIS A 97 1 O ILE A 95 N VAL A 28
SHEET 6 AA1 8 ALA A 118 LEU A 122 1 O MET A 120 N PRO A 94
SHEET 7 AA1 8 ALA A 211 PHE A 216 1 O VAL A 215 N ILE A 121
SHEET 8 AA1 8 PHE A 238 ARG A 242 1 O SER A 239 N ILE A 212
SHEET 1 AA2 8 THR F 5 VAL F 9 0
SHEET 2 AA2 8 VAL F 12 GLN F 19 -1 O ILE F 14 N LYS F 7
SHEET 3 AA2 8 THR F 53 VAL F 56 -1 O THR F 53 N GLN F 19
SHEET 4 AA2 8 VAL F 26 LEU F 30 1 N PHE F 27 O VAL F 54
SHEET 5 AA2 8 PHE F 92 HIS F 97 1 O ILE F 95 N VAL F 28
SHEET 6 AA2 8 ALA F 118 LEU F 122 1 O MET F 120 N PRO F 94
SHEET 7 AA2 8 ALA F 211 PHE F 216 1 O ARG F 213 N ILE F 121
SHEET 8 AA2 8 PHE F 238 ARG F 242 1 O SER F 239 N ILE F 212
SHEET 1 AA3 8 THR E 5 VAL E 9 0
SHEET 2 AA3 8 VAL E 12 GLN E 19 -1 O ILE E 14 N LYS E 7
SHEET 3 AA3 8 THR E 53 VAL E 56 -1 O THR E 53 N GLN E 19
SHEET 4 AA3 8 VAL E 26 LEU E 30 1 N PHE E 27 O VAL E 54
SHEET 5 AA3 8 PHE E 92 HIS E 97 1 O VAL E 93 N VAL E 26
SHEET 6 AA3 8 ALA E 118 LEU E 122 1 O MET E 120 N ALA E 96
SHEET 7 AA3 8 ALA E 211 PHE E 216 1 O ARG E 213 N ILE E 121
SHEET 8 AA3 8 PHE E 238 ARG E 242 1 O ARG E 241 N HIS E 214
CISPEP 1 ILE A 221 GLY A 222 0 4.75
SITE 1 AC1 14 TRP E 33 HIS E 35 HIS E 97 ALA E 98
SITE 2 AC1 14 HIS E 99 PHE E 133 TRP E 157 VAL E 170
SITE 3 AC1 14 TRP E 182 ILE E 189 HIS E 248 PHE E 249
SITE 4 AC1 14 HOH E 403 HOH E 568
CRYST1 96.173 96.173 189.616 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 0.010398 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005274 0.00000
TER 4057 ALA A 269
TER 8064 GLY F 268
TER 12135 ALA E 269
MASTER 406 0 1 36 24 0 4 6 6823 3 39 63
END |