HEADER PROTEIN BINDING 18-MAY-15 4ZV0
TITLE STRUCTURE OF TSE6 IN COMPLEX WITH TSI6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBACTERIAL EFFECTOR SECRETED PROTEIN (TYPE VI SECRETION
COMPND 3 SYSTEM);
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TSE6-BINDING/TSE6 IMMUNITY PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 /
SOURCE 3 PAO1 / 1C / PRS 101 / LMG 12228);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 6 GENE: PA0093;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 /
SOURCE 12 PAO1 / 1C / PRS 101 / LMG 12228);
SOURCE 13 ORGANISM_TAXID: 208964;
SOURCE 14 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 15 GENE: PA0092;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS
KEYWDS T6SS EFFECTOR-IMMUNITY PAIR, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.WHITNEY,S.SAWAI,C.RALSTON,J.D.MOUGOUS
REVDAT 4 11-DEC-19 4ZV0 1 REMARK
REVDAT 3 24-APR-19 4ZV0 1 REMARK
REVDAT 2 20-SEP-17 4ZV0 1 REMARK
REVDAT 1 11-NOV-15 4ZV0 0
JRNL AUTH J.C.WHITNEY,D.QUENTIN,S.SAWAI,M.LEROUX,B.N.HARDING,
JRNL AUTH 2 H.E.LEDVINA,B.Q.TRAN,H.ROBINSON,Y.A.GOO,D.R.GOODLETT,
JRNL AUTH 3 S.RAUNSER,J.D.MOUGOUS
JRNL TITL AN INTERBACTERIAL NAD(P)(+) GLYCOHYDROLASE TOXIN REQUIRES
JRNL TITL 2 ELONGATION FACTOR TU FOR DELIVERY TO TARGET CELLS.
JRNL REF CELL V. 163 607 2015
JRNL REFN ISSN 1097-4172
JRNL PMID 26456113
JRNL DOI 10.1016/J.CELL.2015.09.027
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 64549
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2022
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 37.2741 - 3.3754 1.00 4540 147 0.1486 0.1612
REMARK 3 2 3.3754 - 2.6794 1.00 4480 149 0.1527 0.1572
REMARK 3 3 2.6794 - 2.3408 1.00 4492 146 0.1402 0.1803
REMARK 3 4 2.3408 - 2.1268 1.00 4482 145 0.1336 0.1383
REMARK 3 5 2.1268 - 1.9743 1.00 4446 140 0.1318 0.1367
REMARK 3 6 1.9743 - 1.8579 1.00 4482 144 0.1337 0.1651
REMARK 3 7 1.8579 - 1.7649 1.00 4445 147 0.1400 0.1846
REMARK 3 8 1.7649 - 1.6881 1.00 4470 142 0.1415 0.1635
REMARK 3 9 1.6881 - 1.6231 1.00 4456 143 0.1421 0.1637
REMARK 3 10 1.6231 - 1.5671 1.00 4456 143 0.1538 0.1945
REMARK 3 11 1.5671 - 1.5181 1.00 4439 147 0.1555 0.1651
REMARK 3 12 1.5181 - 1.4747 1.00 4443 146 0.1669 0.1939
REMARK 3 13 1.4747 - 1.4359 1.00 4453 140 0.1807 0.1858
REMARK 3 14 1.4359 - 1.4008 1.00 4443 143 0.1992 0.2245
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.022 1885
REMARK 3 ANGLE : 1.713 2561
REMARK 3 CHIRALITY : 0.103 279
REMARK 3 PLANARITY : 0.010 339
REMARK 3 DIHEDRAL : 13.567 712
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 282 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8959 35.1727 55.7475
REMARK 3 T TENSOR
REMARK 3 T11: 0.0905 T22: 0.1315
REMARK 3 T33: 0.1016 T12: 0.0534
REMARK 3 T13: -0.0113 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.3154 L22: 6.2154
REMARK 3 L33: 4.3369 L12: 0.3656
REMARK 3 L13: -0.3269 L23: -3.7412
REMARK 3 S TENSOR
REMARK 3 S11: -0.1428 S12: -0.1464 S13: 0.1121
REMARK 3 S21: 0.4426 S22: 0.1960 S23: 0.1567
REMARK 3 S31: -0.2710 S32: -0.1404 S33: -0.0691
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 301 THROUGH 373 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7595 32.6760 37.8521
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.1123
REMARK 3 T33: 0.1062 T12: 0.0508
REMARK 3 T13: 0.0026 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.8768 L22: 0.6380
REMARK 3 L33: 1.2083 L12: -0.1657
REMARK 3 L13: 0.3546 L23: -0.7413
REMARK 3 S TENSOR
REMARK 3 S11: 0.0359 S12: 0.0908 S13: -0.0258
REMARK 3 S21: -0.0885 S22: -0.0725 S23: -0.0585
REMARK 3 S31: 0.2041 S32: 0.2656 S33: 0.0015
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 374 THROUGH 390 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8235 34.8066 37.2050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0905 T22: 0.2643
REMARK 3 T33: 0.1499 T12: 0.0216
REMARK 3 T13: 0.0121 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 0.6843 L22: 0.4943
REMARK 3 L33: 2.2004 L12: -0.5602
REMARK 3 L13: -0.1097 L23: -0.1367
REMARK 3 S TENSOR
REMARK 3 S11: 0.0535 S12: 0.1766 S13: 0.1130
REMARK 3 S21: -0.0308 S22: -0.1113 S23: -0.1836
REMARK 3 S31: -0.1065 S32: 0.6238 S33: 0.0424
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 391 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3736 23.2013 43.7197
REMARK 3 T TENSOR
REMARK 3 T11: 0.3206 T22: 0.2752
REMARK 3 T33: 0.4108 T12: 0.0011
REMARK 3 T13: -0.0182 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 3.5451 L22: 1.6228
REMARK 3 L33: 0.4979 L12: -2.3055
REMARK 3 L13: -0.9785 L23: 0.6002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0572 S12: 0.6758 S13: -1.5591
REMARK 3 S21: 0.1416 S22: -0.1057 S23: 0.7015
REMARK 3 S31: 0.4633 S32: -0.2436 S33: -0.0333
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 427 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2473 36.5947 35.0809
REMARK 3 T TENSOR
REMARK 3 T11: 0.0702 T22: 0.1978
REMARK 3 T33: 0.1181 T12: 0.0420
REMARK 3 T13: -0.0014 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 1.2045 L22: 1.8137
REMARK 3 L33: 2.5467 L12: 0.1865
REMARK 3 L13: -1.3285 L23: -1.4026
REMARK 3 S TENSOR
REMARK 3 S11: 0.0931 S12: 0.2943 S13: 0.0051
REMARK 3 S21: -0.1965 S22: -0.1672 S23: -0.1910
REMARK 3 S31: 0.1475 S32: 0.2547 S33: 0.0538
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6994 41.9596 38.9628
REMARK 3 T TENSOR
REMARK 3 T11: 0.0721 T22: 0.1142
REMARK 3 T33: 0.1315 T12: 0.0103
REMARK 3 T13: -0.0056 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.9910 L22: 1.1396
REMARK 3 L33: 4.6409 L12: -0.1382
REMARK 3 L13: -0.7012 L23: 1.1368
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: 0.0540 S13: 0.1224
REMARK 3 S21: -0.0093 S22: 0.0113 S23: 0.1278
REMARK 3 S31: -0.2085 S32: -0.1921 S33: -0.0206
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 21 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2058 32.6354 41.5639
REMARK 3 T TENSOR
REMARK 3 T11: 0.0561 T22: 0.0994
REMARK 3 T33: 0.0922 T12: -0.0133
REMARK 3 T13: -0.0115 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.4633 L22: 0.6388
REMARK 3 L33: 6.7592 L12: -0.2162
REMARK 3 L13: -2.9977 L23: 0.3715
REMARK 3 S TENSOR
REMARK 3 S11: -0.0526 S12: -0.0018 S13: -0.0626
REMARK 3 S21: 0.0518 S22: 0.0119 S23: 0.0513
REMARK 3 S31: 0.2027 S32: -0.1568 S33: 0.0539
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3135 30.0152 54.8058
REMARK 3 T TENSOR
REMARK 3 T11: 0.1777 T22: 0.1833
REMARK 3 T33: 0.1822 T12: 0.0231
REMARK 3 T13: 0.0219 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 5.3018 L22: 1.9556
REMARK 3 L33: 3.5140 L12: 0.1846
REMARK 3 L13: -2.3147 L23: -1.4391
REMARK 3 S TENSOR
REMARK 3 S11: -0.3092 S12: -0.8371 S13: -0.7251
REMARK 3 S21: 0.4371 S22: 0.0282 S23: 0.0895
REMARK 3 S31: 0.2007 S32: 0.5693 S33: 0.1942
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 56 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4339 39.3910 43.0303
REMARK 3 T TENSOR
REMARK 3 T11: 0.0439 T22: 0.0543
REMARK 3 T33: 0.0736 T12: 0.0165
REMARK 3 T13: -0.0079 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.1349 L22: 0.9224
REMARK 3 L33: 2.4633 L12: 0.0619
REMARK 3 L13: -0.6023 L23: -0.1270
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: -0.0071 S13: 0.0116
REMARK 3 S21: 0.0714 S22: 0.0198 S23: -0.0348
REMARK 3 S31: -0.0065 S32: 0.0555 S33: -0.0224
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8187 44.3756 56.6951
REMARK 3 T TENSOR
REMARK 3 T11: 0.2853 T22: 0.1712
REMARK 3 T33: 0.1648 T12: 0.0208
REMARK 3 T13: -0.0117 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 3.9080 L22: 7.2298
REMARK 3 L33: 7.8593 L12: 0.8097
REMARK 3 L13: 0.4827 L23: -6.4621
REMARK 3 S TENSOR
REMARK 3 S11: 0.1272 S12: -0.2902 S13: 0.4724
REMARK 3 S21: 0.6620 S22: -0.3095 S23: -0.0656
REMARK 3 S31: -0.7581 S32: 0.2211 S33: 0.1256
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 4ZV0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69121
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 15.20
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.61700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350, 0.2M AMMONIUM
REMARK 280 IODIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.83867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.91933
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.87900
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 13.95967
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.79833
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MSE A 268
REMARK 465 GLY A 269
REMARK 465 SER A 270
REMARK 465 SER A 271
REMARK 465 HIS A 272
REMARK 465 HIS A 273
REMARK 465 HIS A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
REMARK 465 SER A 278
REMARK 465 GLN A 279
REMARK 465 ASP A 280
REMARK 465 PRO A 281
REMARK 465 VAL A 400
REMARK 465 LYS A 401
REMARK 465 GLY A 402
REMARK 465 GLN A 403
REMARK 465 SER A 404
REMARK 465 TYR A 405
REMARK 465 PRO A 406
REMARK 465 ALA A 407
REMARK 465 LYS A 408
REMARK 465 GLU A 428
REMARK 465 GLY A 429
REMARK 465 SER A 430
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 GLU A 291 CD OE1 OE2
REMARK 470 GLU B 25 CG CD OE1 OE2
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 HZ3 LYS A 295 O HOH A 602 1.37
REMARK 500 HH11 ARG B 44 O HOH B 201 1.59
REMARK 500 O PRO A 393 O HOH A 601 1.87
REMARK 500 O HOH A 710 O HOH A 813 1.88
REMARK 500 O HOH B 206 O HOH B 309 1.92
REMARK 500 O HOH B 231 O HOH B 306 1.93
REMARK 500 O HOH A 669 O HOH A 795 1.94
REMARK 500 O HOH A 755 O HOH B 288 1.96
REMARK 500 O HOH B 283 O HOH B 314 1.97
REMARK 500 O HOH A 699 O HOH A 733 2.00
REMARK 500 O HOH B 294 O HOH B 301 2.03
REMARK 500 O HOH B 201 O HOH B 304 2.04
REMARK 500 O HOH A 679 O HOH A 776 2.07
REMARK 500 O HOH B 299 O HOH B 311 2.08
REMARK 500 O HOH A 612 O HOH A 658 2.13
REMARK 500 O HOH B 317 O HOH B 325 2.14
REMARK 500 O HOH B 219 O HOH B 282 2.14
REMARK 500 NH1 ARG B 44 O HOH B 201 2.14
REMARK 500 O HOH B 317 O HOH B 337 2.15
REMARK 500 O HOH B 331 O HOH B 334 2.16
REMARK 500 O HOH A 614 O HOH A 700 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 744 O HOH A 764 4665 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 287 CG ARG A 287 CD 0.191
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 ARG A 287 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG A 287 NE - CZ - NH1 ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG A 287 NE - CZ - NH2 ANGL. DEV. = -6.8 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 B 68 72.01 -151.76
REMARK 500 ASP B 92 55.35 -96.69
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 825 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 341 DISTANCE = 6.19 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 105
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZUY RELATED DB: PDB
REMARK 900 RELATED ID: 4ZV4 RELATED DB: PDB
DBREF 4ZV0 A 282 430 UNP Q9I739 Q9I739_PSEAE 282 430
DBREF 4ZV0 B 2 94 UNP Q9I740 Q9I740_PSEAE 2 94
SEQADV 4ZV0 MSE A 268 UNP Q9I739 INITIATING METHIONINE
SEQADV 4ZV0 GLY A 269 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 SER A 270 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 SER A 271 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 HIS A 272 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 HIS A 273 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 HIS A 274 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 HIS A 275 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 HIS A 276 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 HIS A 277 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 SER A 278 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 GLN A 279 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 ASP A 280 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 PRO A 281 UNP Q9I739 EXPRESSION TAG
SEQADV 4ZV0 MSE B 1 UNP Q9I740 INITIATING METHIONINE
SEQRES 1 A 163 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 163 PRO HIS ASP ILE ASN TYR ARG GLY ASN ARG GLU THR ALA
SEQRES 3 A 163 ALA LYS PHE PHE LYS SER LYS ASP ILE ASP PRO ALA ASP
SEQRES 4 A 163 ALA GLU SER TYR MSE ASN GLY LEU ASP PHE ASN HIS PRO
SEQRES 5 A 163 VAL ARG VAL GLU THR LEU ALA PRO GLY LYS ASN LEU TRP
SEQRES 6 A 163 GLN TYR GLN SER PRO GLY ALA PRO GLN GLY ASN TRP TYR
SEQRES 7 A 163 THR LEU SER PRO ARG VAL GLN PRO THR GLU LEU GLY ILE
SEQRES 8 A 163 ASN PRO MSE GLY THR ASN ARG ALA ALA ASN THR ILE GLU
SEQRES 9 A 163 PRO LYS VAL LEU ASN SER TYR ARG THR THR GLN LYS VAL
SEQRES 10 A 163 GLU VAL LEU ARG SER THR ALA ALA PRO THR ASP ASP PHE
SEQRES 11 A 163 TRP SER VAL LYS GLY GLN SER TYR PRO ALA LYS GLY GLY
SEQRES 12 A 163 ALA GLN GLN LEU PHE SER ASN GLU LYS GLY SER PHE GLY
SEQRES 13 A 163 LEU LEU PRO ARG GLU GLY SER
SEQRES 1 B 94 MSE THR PRO ILE GLU TYR ILE ASP ARG ALA LEU ALA LEU
SEQRES 2 B 94 VAL VAL ASP ARG LEU ALA ARG TYR PRO GLY TYR GLU VAL
SEQRES 3 B 94 LEU LEU SER ALA GLU LYS GLN LEU GLN TYR ILE ARG SER
SEQRES 4 B 94 VAL LEU LEU ASP ARG SER LEU ASP ARG SER ALA LEU HIS
SEQRES 5 B 94 ARG LEU THR LEU GLY SER ILE ALA VAL LYS GLU PHE ASP
SEQRES 6 B 94 GLU THR ASP PRO GLU LEU SER ARG ALA LEU LYS ASP ALA
SEQRES 7 B 94 TYR TYR VAL GLY ILE ARG THR GLY ARG GLY LEU LYS VAL
SEQRES 8 B 94 ASP LEU PRO
MODRES 4ZV0 MSE A 311 MET MODIFIED RESIDUE
MODRES 4ZV0 MSE A 361 MET MODIFIED RESIDUE
HET MSE A 311 9
HET MSE A 361 17
HET MSE B 1 19
HET IOD A 501 1
HET IOD A 502 1
HET IOD A 503 1
HET IOD A 504 1
HET IOD A 505 1
HET IOD B 101 1
HET IOD B 102 1
HET IOD B 103 1
HET IOD B 104 1
HET IOD B 105 1
HETNAM MSE SELENOMETHIONINE
HETNAM IOD IODIDE ION
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 3 IOD 10(I 1-)
FORMUL 13 HOH *366(H2 O)
HELIX 1 AA1 ASP A 283 LYS A 300 1 18
HELIX 2 AA2 ASP A 303 GLY A 313 1 11
HELIX 3 AA3 PRO A 353 GLY A 357 5 5
HELIX 4 AA4 GLU A 418 GLY A 420 5 3
HELIX 5 AA5 THR B 2 TYR B 21 1 20
HELIX 6 AA6 TYR B 24 ASP B 43 1 20
HELIX 7 AA7 ARG B 48 LEU B 54 5 7
HELIX 8 AA8 THR B 55 PHE B 64 1 10
HELIX 9 AA9 ASP B 68 ARG B 87 1 20
SHEET 1 AA1 4 ARG A 321 LEU A 325 0
SHEET 2 AA1 4 VAL A 384 THR A 390 -1 O ARG A 388 N ARG A 321
SHEET 3 AA1 4 GLN A 412 PHE A 415 -1 O GLN A 413 N SER A 389
SHEET 4 AA1 4 TRP A 344 TYR A 345 -1 N TYR A 345 O LEU A 414
SHEET 1 AA2 3 ASN A 330 GLN A 335 0
SHEET 2 AA2 3 VAL A 374 THR A 380 -1 O VAL A 374 N GLN A 335
SHEET 3 AA2 3 PHE A 422 LEU A 424 -1 O GLY A 423 N ARG A 379
SHEET 1 AA3 2 MSE A 361 ASN A 364 0
SHEET 2 AA3 2 THR A 369 PRO A 372 -1 O GLU A 371 N GLY A 362
LINK C TYR A 310 N MSE A 311 1555 1555 1.31
LINK C MSE A 311 N ASN A 312 1555 1555 1.32
LINK C PRO A 360 N MSE A 361 1555 1555 1.33
LINK C MSE A 361 N GLY A 362 1555 1555 1.34
LINK C MSE B 1 N THR B 2 1555 1555 1.33
SITE 1 AC1 2 ASN A 289 GLN B 35
SITE 1 AC2 1 HOH A 820
SITE 1 AC3 2 GLN A 412 HOH B 276
SITE 1 AC4 1 ARG B 20
SITE 1 AC5 3 GLY A 410 HOH A 776 HOH B 271
SITE 1 AC6 3 HOH A 655 GLU B 25 HOH B 320
SITE 1 AC7 2 LYS B 76 HOH B 247
CRYST1 83.209 83.209 83.758 90.00 90.00 120.00 P 65 6
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 0.012018 0.006939 0.000000 0.00000
SCALE2 0.000000 0.013877 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011939 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
