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HEADER HYDROLASE 21-NOV-18 6I8W
TITLE CRYSTAL STRUCTURE OF A MEMBRANE PHOSPHOLIPASE A, A NOVEL BACTERIAL
TITLE 2 VIRULENCE FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ESTERASE,LIPASE,LIPASE 3,PUTATIVE LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: FME:N-FORMYLMETHIONINE, C-TERMINAL HIS-TAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: LIP3, AOY09_04297, C8257_11100, DN070_25360, NCTC13719_02038,
SOURCE 5 PAMH19_2121;
SOURCE 6 EXPRESSION_SYSTEM: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 208964
KEYWDS LIPASE, MEMBRANE PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GRANZIN,R.BATRA-SAFFERLING
REVDAT 3 29-JUL-20 6I8W 1 COMPND REMARK HETNAM SITE
REVDAT 2 10-JUN-20 6I8W 1 JRNL
REVDAT 1 27-NOV-19 6I8W 0
JRNL AUTH F.BLEFFERT,J.GRANZIN,M.CALISKAN,S.N.SCHOTT-VERDUGO,L.RAHME,
JRNL AUTH 2 M.SIEBERS,B.THIELE,P.DOERMANN,H.GOHLKE,R.BATRA-SAFFERLING,
JRNL AUTH 3 F.KOVACIC,K.-E.JAEGER
JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHTS INTO PHOSPHOLIPASE
JRNL TITL 2 A-MEDIATED MEMBRANE PHOSPHOLIPID DEGRADATION ASSOCIATED WITH
JRNL TITL 3 BACTERIAL VIRULENCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 47.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 65084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3298
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 47.3438 - 5.7657 0.99 2777 140 0.1738 0.1784
REMARK 3 2 5.7657 - 4.5776 1.00 2652 143 0.1439 0.1858
REMARK 3 3 4.5776 - 3.9993 1.00 2634 129 0.1327 0.1468
REMARK 3 4 3.9993 - 3.6338 1.00 2600 132 0.1491 0.1695
REMARK 3 5 3.6338 - 3.3734 1.00 2589 147 0.1597 0.1508
REMARK 3 6 3.3734 - 3.1746 1.00 2584 146 0.1687 0.1752
REMARK 3 7 3.1746 - 3.0156 1.00 2588 131 0.1829 0.2145
REMARK 3 8 3.0156 - 2.8844 1.00 2578 124 0.1777 0.2104
REMARK 3 9 2.8844 - 2.7733 1.00 2578 137 0.1728 0.2119
REMARK 3 10 2.7733 - 2.6776 1.00 2554 126 0.1734 0.1970
REMARK 3 11 2.6776 - 2.5939 1.00 2554 145 0.1650 0.1879
REMARK 3 12 2.5939 - 2.5198 1.00 2571 132 0.1643 0.1931
REMARK 3 13 2.5198 - 2.4535 1.00 2547 148 0.1588 0.1916
REMARK 3 14 2.4535 - 2.3936 1.00 2536 147 0.1636 0.1998
REMARK 3 15 2.3936 - 2.3392 1.00 2560 133 0.1606 0.1957
REMARK 3 16 2.3392 - 2.2894 1.00 2567 126 0.1591 0.2015
REMARK 3 17 2.2894 - 2.2436 1.00 2532 155 0.1610 0.1783
REMARK 3 18 2.2436 - 2.2013 1.00 2542 125 0.1687 0.2261
REMARK 3 19 2.2013 - 2.1620 1.00 2529 140 0.1815 0.2074
REMARK 3 20 2.1620 - 2.1253 1.00 2535 132 0.1967 0.2512
REMARK 3 21 2.1253 - 2.0910 1.00 2527 144 0.2009 0.2411
REMARK 3 22 2.0910 - 2.0589 1.00 2542 142 0.2142 0.2914
REMARK 3 23 2.0589 - 2.0286 1.00 2559 134 0.2216 0.2571
REMARK 3 24 2.0286 - 2.0000 1.00 2551 140 0.2410 0.2672
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.20
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.008 5067
REMARK 3 ANGLE : 1.069 6892
REMARK 3 CHIRALITY : 0.047 786
REMARK 3 PLANARITY : 0.006 904
REMARK 3 DIHEDRAL : 14.404 1914
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.4359 38.4985 11.9893
REMARK 3 T TENSOR
REMARK 3 T11: 0.9217 T22: 0.9527
REMARK 3 T33: 1.2703 T12: -0.3696
REMARK 3 T13: -0.0049 T23: -0.1194
REMARK 3 L TENSOR
REMARK 3 L11: 4.3437 L22: 1.8875
REMARK 3 L33: 7.5132 L12: 2.1782
REMARK 3 L13: -0.4565 L23: -1.3233
REMARK 3 S TENSOR
REMARK 3 S11: 0.3162 S12: -0.6284 S13: 1.8362
REMARK 3 S21: 0.2078 S22: 0.1453 S23: -0.4678
REMARK 3 S31: -0.9295 S32: 2.0465 S33: -0.4707
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.3587 22.8505 -1.1034
REMARK 3 T TENSOR
REMARK 3 T11: 0.3944 T22: 0.3131
REMARK 3 T33: 0.3537 T12: -0.0108
REMARK 3 T13: -0.0093 T23: 0.1649
REMARK 3 L TENSOR
REMARK 3 L11: 1.6301 L22: 1.8720
REMARK 3 L33: 1.9623 L12: -0.5828
REMARK 3 L13: -0.1443 L23: -1.2341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0391 S12: 0.3787 S13: 0.2315
REMARK 3 S21: -0.1372 S22: -0.2545 S23: -0.4322
REMARK 3 S31: -0.1747 S32: 0.3248 S33: 0.2613
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0905 27.0606 -0.9302
REMARK 3 T TENSOR
REMARK 3 T11: 0.3416 T22: 0.2437
REMARK 3 T33: 0.3210 T12: 0.0114
REMARK 3 T13: -0.0063 T23: 0.1213
REMARK 3 L TENSOR
REMARK 3 L11: 2.1159 L22: 2.6173
REMARK 3 L33: 2.8367 L12: 1.0394
REMARK 3 L13: -0.7326 L23: -0.5894
REMARK 3 S TENSOR
REMARK 3 S11: -0.0447 S12: 0.3563 S13: 0.4554
REMARK 3 S21: -0.0341 S22: 0.0073 S23: 0.0929
REMARK 3 S31: -0.2502 S32: -0.1082 S33: 0.0407
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3149 28.9932 4.9707
REMARK 3 T TENSOR
REMARK 3 T11: 0.2896 T22: 0.2329
REMARK 3 T33: 0.4450 T12: 0.0002
REMARK 3 T13: 0.0660 T23: 0.0883
REMARK 3 L TENSOR
REMARK 3 L11: 3.3722 L22: 5.8023
REMARK 3 L33: 3.6835 L12: -0.2335
REMARK 3 L13: 0.5134 L23: 1.9940
REMARK 3 S TENSOR
REMARK 3 S11: 0.0460 S12: 0.0231 S13: 0.6246
REMARK 3 S21: 0.2288 S22: -0.1418 S23: 0.8700
REMARK 3 S31: -0.1709 S32: -0.4392 S33: 0.0438
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 172 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.5276 35.6845 19.4903
REMARK 3 T TENSOR
REMARK 3 T11: 0.8620 T22: 0.3650
REMARK 3 T33: 0.4690 T12: -0.1788
REMARK 3 T13: 0.0203 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 3.0668 L22: 3.2946
REMARK 3 L33: 2.0403 L12: -1.1160
REMARK 3 L13: 0.6400 L23: 0.0837
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: -0.2572 S13: 0.4913
REMARK 3 S21: 0.8152 S22: -0.0995 S23: -0.1770
REMARK 3 S31: -0.7771 S32: 0.2307 S33: 0.0951
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 234 )
REMARK 3 ORIGIN FOR THE GROUP (A): 71.7484 38.5745 9.9212
REMARK 3 T TENSOR
REMARK 3 T11: 0.6324 T22: 0.3389
REMARK 3 T33: 0.5516 T12: -0.1167
REMARK 3 T13: -0.0146 T23: 0.0978
REMARK 3 L TENSOR
REMARK 3 L11: 3.0371 L22: 5.8290
REMARK 3 L33: 4.3952 L12: -3.8164
REMARK 3 L13: 2.3359 L23: -1.9962
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: -0.3598 S13: 0.9972
REMARK 3 S21: 0.1746 S22: -0.1722 S23: -0.6093
REMARK 3 S31: -0.7122 S32: 0.3535 S33: 0.1967
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 235 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.1457 26.7629 10.7793
REMARK 3 T TENSOR
REMARK 3 T11: 0.4041 T22: 0.2337
REMARK 3 T33: 0.4434 T12: 0.0310
REMARK 3 T13: 0.1247 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 2.3011 L22: 3.3587
REMARK 3 L33: 1.2997 L12: 1.5060
REMARK 3 L13: -0.5168 L23: -0.5145
REMARK 3 S TENSOR
REMARK 3 S11: 0.1948 S12: 0.0895 S13: 0.6983
REMARK 3 S21: 0.5032 S22: -0.1022 S23: 0.6973
REMARK 3 S31: -0.3784 S32: -0.2340 S33: -0.0927
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5978 11.7793 6.6377
REMARK 3 T TENSOR
REMARK 3 T11: 0.4040 T22: 0.2947
REMARK 3 T33: 0.3579 T12: -0.0293
REMARK 3 T13: 0.0600 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 2.4956 L22: 2.2570
REMARK 3 L33: 8.5445 L12: -1.8894
REMARK 3 L13: 3.4552 L23: -0.9575
REMARK 3 S TENSOR
REMARK 3 S11: 0.2302 S12: 0.1329 S13: -0.5182
REMARK 3 S21: 0.1399 S22: -0.1609 S23: 0.3740
REMARK 3 S31: 0.6341 S32: -0.3250 S33: -0.1120
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 97.9057 30.3156 5.8969
REMARK 3 T TENSOR
REMARK 3 T11: 0.6294 T22: 0.5195
REMARK 3 T33: 0.8006 T12: -0.1557
REMARK 3 T13: 0.0445 T23: 0.1393
REMARK 3 L TENSOR
REMARK 3 L11: 4.3209 L22: 6.0737
REMARK 3 L33: 0.1672 L12: 5.2474
REMARK 3 L13: -1.1194 L23: -1.3276
REMARK 3 S TENSOR
REMARK 3 S11: 0.4361 S12: 0.1774 S13: -0.5389
REMARK 3 S21: 0.5568 S22: -0.1441 S23: -1.5693
REMARK 3 S31: -0.2204 S32: 0.2786 S33: -0.1390
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 93.2940 -2.0457 21.3392
REMARK 3 T TENSOR
REMARK 3 T11: 0.3201 T22: 0.2711
REMARK 3 T33: 0.2923 T12: -0.0398
REMARK 3 T13: -0.1151 T23: 0.0808
REMARK 3 L TENSOR
REMARK 3 L11: 3.1780 L22: 2.0848
REMARK 3 L33: 3.7494 L12: 0.7353
REMARK 3 L13: 1.4265 L23: 0.9889
REMARK 3 S TENSOR
REMARK 3 S11: -0.1129 S12: 0.2281 S13: 0.0430
REMARK 3 S21: 0.0094 S22: 0.1218 S23: -0.2540
REMARK 3 S31: -0.0898 S32: 0.3953 S33: -0.0103
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 6I8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200013014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : SILICON (111) CHANNEL-CUT
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65113
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.6000
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) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MRBUMP
REMARK 200 STARTING MODEL: 2VF2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRISODIUM CITRATE, 10% (W/V) PEG
REMARK 280 4000, 10% (W/V) ISOPROPANOL, PH 5.6, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 292.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-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 66.93550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 66.93550
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.17900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 66.93550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.08950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 66.93550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 159.26850
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 66.93550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 159.26850
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.93550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 53.08950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 66.93550
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 66.93550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 106.17900
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 66.93550
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 66.93550
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 106.17900
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 66.93550
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 159.26850
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 66.93550
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 53.08950
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 66.93550
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 53.08950
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 66.93550
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 159.26850
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 66.93550
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 66.93550
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 106.17900
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 GLN A 311
REMARK 465 VAL A 312
REMARK 465 ALA A 313
REMARK 465 GLY A 314
REMARK 465 ARG A 315
REMARK 465 GLY 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 HIS A 322
REMARK 465 GLN B 311
REMARK 465 VAL B 312
REMARK 465 ALA B 313
REMARK 465 GLY B 314
REMARK 465 ARG B 315
REMARK 465 GLY 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 465 HIS B 322
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 LYS A 2 CG CD CE NZ
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 130 CZ NH1 NH2
REMARK 470 ARG A 169 NE CZ NH1 NH2
REMARK 470 LYS A 194 CD CE NZ
REMARK 470 GLU A 247 CG CD OE1 OE2
REMARK 470 ARG A 308 CZ NH1 NH2
REMARK 470 ARG B 3 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 LYS B 61 CD CE NZ
REMARK 470 ARG B 88 CZ NH1 NH2
REMARK 470 GLN B 106 CG CD OE1 NE2
REMARK 470 GLN B 107 CG CD OE1 NE2
REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 130 NE CZ NH1 NH2
REMARK 470 LYS B 170 CD CE NZ
REMARK 470 GLU B 175 CD OE1 OE2
REMARK 470 LYS B 194 CD CE NZ
REMARK 470 ARG B 212 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 217 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 OD2 ASP A 101 O HOH A 501 2.06
REMARK 500 O ILE B 246 O HOH B 601 2.07
REMARK 500 O2 CO2 A 406 O HOH A 502 2.13
REMARK 500 O VAL B 185 O HOH B 602 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 SER A 137 -120.68 56.77
REMARK 500 SER A 137 -118.47 53.29
REMARK 500 SER B 137 -120.58 56.73
REMARK 500 SER B 137 -119.18 54.45
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6I8W A 1 315 UNP Q9KJG6 Q9KJG6_PSEAI 1 315
DBREF 6I8W B 1 315 UNP Q9KJG6 Q9KJG6_PSEAI 1 315
SEQADV 6I8W GLY A 316 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS A 317 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS A 318 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS A 319 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS A 320 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS A 321 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS A 322 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W GLY B 316 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS B 317 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS B 318 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS B 319 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS B 320 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS B 321 UNP Q9KJG6 EXPRESSION TAG
SEQADV 6I8W HIS B 322 UNP Q9KJG6 EXPRESSION TAG
SEQRES 1 A 322 FME LYS ARG PHE LEU LEU GLY LEU VAL LEU LEU LEU ALA
SEQRES 2 A 322 VAL ALA ALA GLY VAL LEU TYR PHE VAL PRO ALA THR LEU
SEQRES 3 A 322 LEU ALA SER VAL ARG THR VAL GLU ARG GLY LEU ALA GLY
SEQRES 4 A 322 LEU SER GLU HIS SER VAL GLN VAL ASP ASN LEU GLU ILE
SEQRES 5 A 322 ALA TYR LEU GLU GLY GLY SER GLU LYS ASN PRO THR LEU
SEQRES 6 A 322 LEU LEU ILE HIS GLY PHE GLY ALA ASP LYS ASP ASN TRP
SEQRES 7 A 322 LEU ARG PHE ALA ARG PRO LEU THR GLU ARG TYR HIS VAL
SEQRES 8 A 322 VAL ALA LEU ASP LEU PRO GLY PHE GLY ASP SER SER LYS
SEQRES 9 A 322 PRO GLN GLN ALA SER TYR ASP VAL GLY THR GLN ALA GLU
SEQRES 10 A 322 ARG VAL ALA ASN PHE ALA ALA ALA ILE GLY VAL ARG ARG
SEQRES 11 A 322 LEU HIS LEU ALA GLY ASN SER MET GLY GLY HIS ILE ALA
SEQRES 12 A 322 ALA LEU TYR ALA ALA ARG HIS PRO GLU GLN VAL LEU SER
SEQRES 13 A 322 LEU ALA LEU ILE ASP ASN ALA GLY VAL MET PRO ALA ARG
SEQRES 14 A 322 LYS SER GLU LEU PHE GLU ASP LEU GLU ARG GLY GLU ASN
SEQRES 15 A 322 PRO LEU VAL VAL ARG GLN PRO GLU ASP PHE GLN LYS LEU
SEQRES 16 A 322 LEU ASP PHE VAL PHE VAL GLN GLN PRO PRO LEU PRO ALA
SEQRES 17 A 322 PRO LEU LYS ARG TYR LEU GLY GLU ARG ALA VAL ALA ALA
SEQRES 18 A 322 SER ALA PHE ASN ALA GLN ILE PHE GLU GLN LEU ARG GLN
SEQRES 19 A 322 ARG TYR ILE PRO LEU GLU PRO GLU LEU PRO LYS ILE GLU
SEQRES 20 A 322 ALA PRO THR LEU LEU LEU TRP GLY ASP ARG ASP ARG VAL
SEQRES 21 A 322 LEU ASP VAL SER SER ILE GLU VAL MET ARG PRO LEU LEU
SEQRES 22 A 322 LYS ARG PRO SER VAL VAL ILE MET GLU ASN CYS GLY HIS
SEQRES 23 A 322 VAL PRO MET VAL GLU ARG PRO GLU GLU THR ALA GLN HIS
SEQRES 24 A 322 TYR GLN ALA PHE LEU ASP GLY VAL ARG ASN ALA GLN VAL
SEQRES 25 A 322 ALA GLY ARG GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 322 FME LYS ARG PHE LEU LEU GLY LEU VAL LEU LEU LEU ALA
SEQRES 2 B 322 VAL ALA ALA GLY VAL LEU TYR PHE VAL PRO ALA THR LEU
SEQRES 3 B 322 LEU ALA SER VAL ARG THR VAL GLU ARG GLY LEU ALA GLY
SEQRES 4 B 322 LEU SER GLU HIS SER VAL GLN VAL ASP ASN LEU GLU ILE
SEQRES 5 B 322 ALA TYR LEU GLU GLY GLY SER GLU LYS ASN PRO THR LEU
SEQRES 6 B 322 LEU LEU ILE HIS GLY PHE GLY ALA ASP LYS ASP ASN TRP
SEQRES 7 B 322 LEU ARG PHE ALA ARG PRO LEU THR GLU ARG TYR HIS VAL
SEQRES 8 B 322 VAL ALA LEU ASP LEU PRO GLY PHE GLY ASP SER SER LYS
SEQRES 9 B 322 PRO GLN GLN ALA SER TYR ASP VAL GLY THR GLN ALA GLU
SEQRES 10 B 322 ARG VAL ALA ASN PHE ALA ALA ALA ILE GLY VAL ARG ARG
SEQRES 11 B 322 LEU HIS LEU ALA GLY ASN SER MET GLY GLY HIS ILE ALA
SEQRES 12 B 322 ALA LEU TYR ALA ALA ARG HIS PRO GLU GLN VAL LEU SER
SEQRES 13 B 322 LEU ALA LEU ILE ASP ASN ALA GLY VAL MET PRO ALA ARG
SEQRES 14 B 322 LYS SER GLU LEU PHE GLU ASP LEU GLU ARG GLY GLU ASN
SEQRES 15 B 322 PRO LEU VAL VAL ARG GLN PRO GLU ASP PHE GLN LYS LEU
SEQRES 16 B 322 LEU ASP PHE VAL PHE VAL GLN GLN PRO PRO LEU PRO ALA
SEQRES 17 B 322 PRO LEU LYS ARG TYR LEU GLY GLU ARG ALA VAL ALA ALA
SEQRES 18 B 322 SER ALA PHE ASN ALA GLN ILE PHE GLU GLN LEU ARG GLN
SEQRES 19 B 322 ARG TYR ILE PRO LEU GLU PRO GLU LEU PRO LYS ILE GLU
SEQRES 20 B 322 ALA PRO THR LEU LEU LEU TRP GLY ASP ARG ASP ARG VAL
SEQRES 21 B 322 LEU ASP VAL SER SER ILE GLU VAL MET ARG PRO LEU LEU
SEQRES 22 B 322 LYS ARG PRO SER VAL VAL ILE MET GLU ASN CYS GLY HIS
SEQRES 23 B 322 VAL PRO MET VAL GLU ARG PRO GLU GLU THR ALA GLN HIS
SEQRES 24 B 322 TYR GLN ALA PHE LEU ASP GLY VAL ARG ASN ALA GLN VAL
SEQRES 25 B 322 ALA GLY ARG GLY HIS HIS HIS HIS HIS HIS
MODRES 6I8W FME A 1 MET MODIFIED RESIDUE
MODRES 6I8W FME B 1 MET MODIFIED RESIDUE
HET FME A 1 10
HET FME B 1 17
HET MYR A 401 16
HET BOG A 402 20
HET IPA A 403 4
HET CO2 A 404 3
HET CO2 A 405 3
HET CO2 A 406 3
HET 11A B 501 13
HET BOG B 502 20
HET IPA B 503 4
HET IPA B 504 4
HET CO2 B 505 3
HET CO2 B 506 3
HETNAM FME N-FORMYLMETHIONINE
HETNAM MYR MYRISTIC ACID
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM CO2 CARBON DIOXIDE
HETNAM 11A UNDECANOIC ACID
HETSYN IPA 2-PROPANOL
FORMUL 1 FME 2(C6 H11 N O3 S)
FORMUL 3 MYR C14 H28 O2
FORMUL 4 BOG 2(C14 H28 O6)
FORMUL 5 IPA 3(C3 H8 O)
FORMUL 6 CO2 5(C O2)
FORMUL 9 11A C11 H22 O2
FORMUL 15 HOH *233(H2 O)
HELIX 1 AA1 FME A 1 TYR A 20 1 20
HELIX 2 AA2 TYR A 20 GLY A 39 1 20
HELIX 3 AA3 ASP A 74 ASN A 77 5 4
HELIX 4 AA4 TRP A 78 ARG A 83 1 6
HELIX 5 AA5 ASP A 111 ILE A 126 1 16
HELIX 6 AA6 SER A 137 HIS A 150 1 14
HELIX 7 AA7 SER A 171 GLU A 178 1 8
HELIX 8 AA8 GLU A 190 PHE A 200 1 11
HELIX 9 AA9 PRO A 207 ARG A 235 1 29
HELIX 10 AB1 GLU A 242 ILE A 246 5 5
HELIX 11 AB2 SER A 264 ARG A 270 1 7
HELIX 12 AB3 PRO A 271 LEU A 273 5 3
HELIX 13 AB4 VAL A 287 ARG A 292 1 6
HELIX 14 AB5 ARG A 292 ASN A 309 1 18
HELIX 15 AB6 LYS B 2 ALA B 38 1 37
HELIX 16 AB7 ASP B 74 ASN B 77 5 4
HELIX 17 AB8 TRP B 78 ARG B 83 1 6
HELIX 18 AB9 ASP B 111 ILE B 126 1 16
HELIX 19 AC1 SER B 137 HIS B 150 1 14
HELIX 20 AC2 SER B 171 GLU B 178 1 8
HELIX 21 AC3 GLU B 190 PHE B 200 1 11
HELIX 22 AC4 PRO B 207 ARG B 235 1 29
HELIX 23 AC5 GLU B 242 ILE B 246 5 5
HELIX 24 AC6 SER B 264 ARG B 270 1 7
HELIX 25 AC7 PRO B 271 LEU B 273 5 3
HELIX 26 AC8 VAL B 287 ARG B 292 1 6
HELIX 27 AC9 ARG B 292 ASN B 309 1 18
SHEET 1 AA1 8 SER A 41 VAL A 47 0
SHEET 2 AA1 8 LEU A 50 GLY A 57 -1 O TYR A 54 N HIS A 43
SHEET 3 AA1 8 HIS A 90 LEU A 94 -1 O ALA A 93 N LEU A 55
SHEET 4 AA1 8 THR A 64 ILE A 68 1 N LEU A 67 O VAL A 92
SHEET 5 AA1 8 LEU A 131 ASN A 136 1 O HIS A 132 N LEU A 66
SHEET 6 AA1 8 VAL A 154 ILE A 160 1 O ILE A 160 N GLY A 135
SHEET 7 AA1 8 THR A 250 GLY A 255 1 O LEU A 251 N LEU A 159
SHEET 8 AA1 8 PRO A 276 MET A 281 1 O MET A 281 N TRP A 254
SHEET 1 AA2 8 SER B 41 VAL B 47 0
SHEET 2 AA2 8 LEU B 50 GLY B 57 -1 O LEU B 50 N VAL B 47
SHEET 3 AA2 8 HIS B 90 LEU B 94 -1 O ALA B 93 N LEU B 55
SHEET 4 AA2 8 THR B 64 ILE B 68 1 N LEU B 67 O VAL B 92
SHEET 5 AA2 8 LEU B 131 ASN B 136 1 O HIS B 132 N LEU B 66
SHEET 6 AA2 8 VAL B 154 ILE B 160 1 O ILE B 160 N GLY B 135
SHEET 7 AA2 8 THR B 250 GLY B 255 1 O LEU B 251 N LEU B 159
SHEET 8 AA2 8 PRO B 276 MET B 281 1 O MET B 281 N TRP B 254
LINK C FME A 1 N LYS A 2 1555 1555 1.33
LINK C FME B 1 N LYS B 2 1555 1555 1.33
CRYST1 133.871 133.871 212.358 90.00 90.00 90.00 I 41 2 2 32
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 0.007470 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004709 0.00000
TER 2442 ALA A 310
TER 4860 ALA B 310
MASTER 508 0 14 27 16 0 0 6 5092 2 125 50
END |