HEADER PROTEIN BINDING 18-MAY-15 4ZUY
TITLE STRUCTURE OF TSI6 FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TSI6;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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: PA0092;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS 4-HELIX BUNDLE, BACTERIAL TYPE VI SECRETION IMMUNITY PROTEIN, TSE6
KEYWDS 2 IMMUNITY PROTEIN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.WHITNEY,S.SAWAI,H.ROBINSON,J.D.MOUGOUS
REVDAT 4 11-DEC-19 4ZUY 1 REMARK
REVDAT 3 24-APR-19 4ZUY 1 REMARK
REVDAT 2 20-SEP-17 4ZUY 1 REMARK
REVDAT 1 11-NOV-15 4ZUY 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. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 18765
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1869
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 47.9800 - 4.5889 1.00 1410 158 0.1811 0.2115
REMARK 3 2 4.5889 - 3.6427 0.98 1327 148 0.1631 0.1925
REMARK 3 3 3.6427 - 3.1824 0.99 1317 144 0.2005 0.2443
REMARK 3 4 3.1824 - 2.8914 1.00 1329 150 0.2212 0.2899
REMARK 3 5 2.8914 - 2.6842 1.00 1317 142 0.2083 0.2762
REMARK 3 6 2.6842 - 2.5260 1.00 1309 144 0.1992 0.3004
REMARK 3 7 2.5260 - 2.3995 1.00 1288 145 0.1976 0.2358
REMARK 3 8 2.3995 - 2.2950 0.99 1290 145 0.2001 0.2590
REMARK 3 9 2.2950 - 2.2067 0.99 1297 138 0.2006 0.2314
REMARK 3 10 2.2067 - 2.1305 0.98 1287 150 0.2026 0.2424
REMARK 3 11 2.1305 - 2.0639 0.98 1263 136 0.2060 0.2627
REMARK 3 12 2.0639 - 2.0049 0.98 1295 141 0.2186 0.2659
REMARK 3 13 2.0049 - 1.9521 0.91 1167 128 0.2477 0.2662
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290
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 : 0.007 1472
REMARK 3 ANGLE : 0.933 1991
REMARK 3 CHIRALITY : 0.038 233
REMARK 3 PLANARITY : 0.004 253
REMARK 3 DIHEDRAL : 14.241 565
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7942 -13.4023 13.6926
REMARK 3 T TENSOR
REMARK 3 T11: 0.4574 T22: 0.4285
REMARK 3 T33: 0.3159 T12: -0.0088
REMARK 3 T13: 0.1042 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 1.7651 L22: 4.9425
REMARK 3 L33: 4.5316 L12: 0.0158
REMARK 3 L13: 0.5235 L23: -1.9805
REMARK 3 S TENSOR
REMARK 3 S11: 0.1949 S12: -0.6533 S13: 0.1426
REMARK 3 S21: 0.6243 S22: -0.0920 S23: 0.5776
REMARK 3 S31: -0.2869 S32: -0.5104 S33: -0.0839
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6650 -16.5745 11.6180
REMARK 3 T TENSOR
REMARK 3 T11: 0.3915 T22: 0.4931
REMARK 3 T33: 0.5002 T12: 0.0585
REMARK 3 T13: -0.0421 T23: 0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 3.8992 L22: 3.1032
REMARK 3 L33: 4.2259 L12: 1.3044
REMARK 3 L13: -1.0417 L23: -1.0655
REMARK 3 S TENSOR
REMARK 3 S11: -0.5065 S12: -0.5241 S13: 0.0103
REMARK 3 S21: -0.1002 S22: -0.0825 S23: -0.8465
REMARK 3 S31: 0.3099 S32: 0.0147 S33: 0.5674
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4930 -3.4823 2.0746
REMARK 3 T TENSOR
REMARK 3 T11: 0.9637 T22: 0.6213
REMARK 3 T33: 0.5493 T12: -0.2122
REMARK 3 T13: -0.0110 T23: 0.1158
REMARK 3 L TENSOR
REMARK 3 L11: 8.8904 L22: 2.8402
REMARK 3 L33: 5.1035 L12: -3.3964
REMARK 3 L13: 3.1120 L23: -0.5472
REMARK 3 S TENSOR
REMARK 3 S11: -0.0718 S12: -1.0882 S13: 0.6009
REMARK 3 S21: -0.6085 S22: -0.1369 S23: -1.3209
REMARK 3 S31: -0.6290 S32: -0.5102 S33: -0.1773
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 55 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3662 -15.9877 0.0144
REMARK 3 T TENSOR
REMARK 3 T11: 0.2989 T22: 0.5798
REMARK 3 T33: 0.3433 T12: -0.0022
REMARK 3 T13: -0.0066 T23: -0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 9.5612 L22: 2.0217
REMARK 3 L33: 3.9692 L12: -1.4488
REMARK 3 L13: 1.7001 L23: 4.0818
REMARK 3 S TENSOR
REMARK 3 S11: -0.2172 S12: 0.8941 S13: -1.1147
REMARK 3 S21: 0.3409 S22: -0.0976 S23: -1.3352
REMARK 3 S31: 0.1493 S32: 1.0870 S33: 0.1287
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3927 -18.2889 4.1370
REMARK 3 T TENSOR
REMARK 3 T11: 0.2796 T22: 0.3185
REMARK 3 T33: 0.3481 T12: 0.0367
REMARK 3 T13: 0.0656 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 3.3531 L22: 4.1592
REMARK 3 L33: 6.5359 L12: 1.1084
REMARK 3 L13: 0.9445 L23: 0.9194
REMARK 3 S TENSOR
REMARK 3 S11: -0.2398 S12: -0.2146 S13: -0.2914
REMARK 3 S21: 0.0512 S22: 0.3199 S23: 0.3383
REMARK 3 S31: 0.2668 S32: -0.4292 S33: -0.0090
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1499 7.0034 0.0664
REMARK 3 T TENSOR
REMARK 3 T11: 0.5311 T22: 0.3803
REMARK 3 T33: 0.6333 T12: -0.0912
REMARK 3 T13: 0.0378 T23: -0.1098
REMARK 3 L TENSOR
REMARK 3 L11: 4.7331 L22: 7.4103
REMARK 3 L33: 0.5735 L12: -5.9794
REMARK 3 L13: -0.6638 L23: 0.8137
REMARK 3 S TENSOR
REMARK 3 S11: -0.0631 S12: 0.6602 S13: -0.1614
REMARK 3 S21: -0.1419 S22: -0.5169 S23: 0.9000
REMARK 3 S31: 0.5891 S32: -0.7312 S33: -0.5145
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7197 -20.0403 -15.9940
REMARK 3 T TENSOR
REMARK 3 T11: 0.3779 T22: 0.3896
REMARK 3 T33: 0.3659 T12: -0.0292
REMARK 3 T13: -0.0013 T23: -0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 2.8942 L22: 2.6344
REMARK 3 L33: 0.7677 L12: 0.4103
REMARK 3 L13: -0.3204 L23: -0.2319
REMARK 3 S TENSOR
REMARK 3 S11: -0.1267 S12: 0.3062 S13: 0.1170
REMARK 3 S21: -0.2564 S22: 0.0601 S23: 0.1630
REMARK 3 S31: -0.0968 S32: -0.0906 S33: 0.0928
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1167 -32.6585 -4.8256
REMARK 3 T TENSOR
REMARK 3 T11: 0.3885 T22: 0.4459
REMARK 3 T33: 0.7218 T12: -0.0593
REMARK 3 T13: -0.0376 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 2.1343 L22: 0.6411
REMARK 3 L33: 2.0014 L12: 0.3113
REMARK 3 L13: 1.2013 L23: -0.6681
REMARK 3 S TENSOR
REMARK 3 S11: 0.2309 S12: -0.9246 S13: 0.2743
REMARK 3 S21: 0.8658 S22: 0.1612 S23: 0.3366
REMARK 3 S31: -0.6564 S32: -0.0017 S33: 0.1532
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 51 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1460 -16.4939 -7.5662
REMARK 3 T TENSOR
REMARK 3 T11: 0.2850 T22: 0.2696
REMARK 3 T33: 0.2817 T12: -0.0267
REMARK 3 T13: 0.0015 T23: -0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 4.6272 L22: 7.9030
REMARK 3 L33: 4.8356 L12: -1.6622
REMARK 3 L13: 2.1193 L23: -0.4214
REMARK 3 S TENSOR
REMARK 3 S11: -0.0993 S12: 0.1345 S13: -0.1729
REMARK 3 S21: -0.0223 S22: 0.1114 S23: 0.1500
REMARK 3 S31: -0.2757 S32: 0.1048 S33: -0.0661
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 4ZUY 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_1000209956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-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 : NSLS
REMARK 200 BEAMLINE : X29A
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 : 19003
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 47.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 15.00
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.68700
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: SHELXDE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE:HCL PH 8.0, 2.5 M
REMARK 280 NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.54900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.54900
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 27.25550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.47800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.25550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.47800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.54900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.25550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.47800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.54900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.25550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.47800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 HIS A 97
REMARK 465 HIS A 98
REMARK 465 HIS A 99
REMARK 465 HIS A 100
REMARK 465 HIS A 101
REMARK 465 HIS A 102
REMARK 465 ARG B 87
REMARK 465 GLY B 88
REMARK 465 LEU B 89
REMARK 465 LYS B 90
REMARK 465 VAL B 91
REMARK 465 ASP B 92
REMARK 465 LEU B 93
REMARK 465 PRO B 94
REMARK 465 LEU B 95
REMARK 465 GLU B 96
REMARK 465 HIS B 97
REMARK 465 HIS B 98
REMARK 465 HIS B 99
REMARK 465 HIS B 100
REMARK 465 HIS B 101
REMARK 465 HIS B 102
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 66 CG CD OE1 OE2
REMARK 470 LYS B 32 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 341 O HOH B 345 1.86
REMARK 500 O HOH A 327 O HOH A 346 1.94
REMARK 500 O GLU A 96 O HOH A 301 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 TYR A 24 105.75 -56.18
REMARK 500 LEU A 95 -10.53 72.88
REMARK 500 ASP B 68 72.91 -150.15
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 CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZV0 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZV4 RELATED DB: PDB
DBREF 4ZUY A 1 94 UNP Q9I740 Q9I740_PSEAE 1 94
DBREF 4ZUY B 1 94 UNP Q9I740 Q9I740_PSEAE 1 94
SEQADV 4ZUY MSE A 37 UNP Q9I740 ILE 37 ENGINEERED MUTATION
SEQADV 4ZUY LEU A 95 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY GLU A 96 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS A 97 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS A 98 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS A 99 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS A 100 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS A 101 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS A 102 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY MSE B 37 UNP Q9I740 ILE 37 ENGINEERED MUTATION
SEQADV 4ZUY LEU B 95 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY GLU B 96 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS B 97 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS B 98 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS B 99 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS B 100 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS B 101 UNP Q9I740 EXPRESSION TAG
SEQADV 4ZUY HIS B 102 UNP Q9I740 EXPRESSION TAG
SEQRES 1 A 102 MSE THR PRO ILE GLU TYR ILE ASP ARG ALA LEU ALA LEU
SEQRES 2 A 102 VAL VAL ASP ARG LEU ALA ARG TYR PRO GLY TYR GLU VAL
SEQRES 3 A 102 LEU LEU SER ALA GLU LYS GLN LEU GLN TYR MSE ARG SER
SEQRES 4 A 102 VAL LEU LEU ASP ARG SER LEU ASP ARG SER ALA LEU HIS
SEQRES 5 A 102 ARG LEU THR LEU GLY SER ILE ALA VAL LYS GLU PHE ASP
SEQRES 6 A 102 GLU THR ASP PRO GLU LEU SER ARG ALA LEU LYS ASP ALA
SEQRES 7 A 102 TYR TYR VAL GLY ILE ARG THR GLY ARG GLY LEU LYS VAL
SEQRES 8 A 102 ASP LEU PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 102 MSE THR PRO ILE GLU TYR ILE ASP ARG ALA LEU ALA LEU
SEQRES 2 B 102 VAL VAL ASP ARG LEU ALA ARG TYR PRO GLY TYR GLU VAL
SEQRES 3 B 102 LEU LEU SER ALA GLU LYS GLN LEU GLN TYR MSE ARG SER
SEQRES 4 B 102 VAL LEU LEU ASP ARG SER LEU ASP ARG SER ALA LEU HIS
SEQRES 5 B 102 ARG LEU THR LEU GLY SER ILE ALA VAL LYS GLU PHE ASP
SEQRES 6 B 102 GLU THR ASP PRO GLU LEU SER ARG ALA LEU LYS ASP ALA
SEQRES 7 B 102 TYR TYR VAL GLY ILE ARG THR GLY ARG GLY LEU LYS VAL
SEQRES 8 B 102 ASP LEU PRO LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 4ZUY MSE A 1 MET MODIFIED RESIDUE
MODRES 4ZUY MSE B 1 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 37 8
HET MSE B 1 8
HET MSE B 37 8
HET CL A 201 1
HET CL A 202 1
HET CL A 203 1
HET CL B 201 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 CL 4(CL 1-)
FORMUL 7 HOH *98(H2 O)
HELIX 1 AA1 THR A 2 TYR A 21 1 20
HELIX 2 AA2 TYR A 24 ASP A 43 1 20
HELIX 3 AA3 ARG A 48 LEU A 54 5 7
HELIX 4 AA4 THR A 55 ASP A 65 1 11
HELIX 5 AA5 ASP A 68 ARG A 84 1 17
HELIX 6 AA6 THR A 85 LEU A 89 5 5
HELIX 7 AA7 THR B 2 TYR B 21 1 20
HELIX 8 AA8 TYR B 24 ASP B 43 1 20
HELIX 9 AA9 ALA B 50 LEU B 54 5 5
HELIX 10 AB1 THR B 55 ASP B 65 1 11
HELIX 11 AB2 ASP B 68 ARG B 84 1 17
LINK C MSE A 1 N THR A 2 1555 1555 1.32
LINK C TYR A 36 N MSE A 37 1555 1555 1.33
LINK C MSE A 37 N ARG A 38 1555 1555 1.33
LINK C MSE B 1 N THR B 2 1555 1555 1.33
LINK C TYR B 36 N MSE B 37 1555 1555 1.33
LINK C MSE B 37 N ARG B 38 1555 1555 1.33
SITE 1 AC1 2 LYS A 76 THR B 85
SITE 1 AC2 2 THR A 85 LYS B 76
SITE 1 AC3 3 ARG A 84 LYS A 90 ASP A 92
SITE 1 AC4 2 ARG B 73 ASP B 77
CRYST1 54.511 100.956 93.098 90.00 90.00 90.00 C 2 2 21 16
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 0.018345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009905 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010741 0.00000
HETATM 1 N MSE A 1 -20.474 -3.156 5.919 1.00 56.03 N
ANISOU 1 N MSE A 1 7053 6227 8008 2050 979 -838 N
HETATM 2 CA MSE A 1 -19.356 -3.879 6.505 1.00 58.16 C
ANISOU 2 CA MSE A 1 7501 6550 8048 1777 989 -891 C
HETATM 3 C MSE A 1 -18.066 -3.568 5.773 1.00 54.86 C
ANISOU 3 C MSE A 1 7386 5935 7522 1647 807 -920 C
HETATM 4 O MSE A 1 -18.047 -3.422 4.548 1.00 53.94 O
ANISOU 4 O MSE A 1 7288 5706 7499 1673 610 -835 O
HETATM 5 CB MSE A 1 -19.606 -5.382 6.475 1.00 56.53 C
ANISOU 5 CB MSE A 1 7053 6562 7864 1574 909 -748 C
HETATM 6 CG MSE A 1 -20.674 -5.852 7.429 1.00 65.50 C
ANISOU 6 CG MSE A 1 7893 7929 9066 1622 1125 -700 C
HETATM 7 SE MSE A 1 -19.944 -6.307 9.164 0.77 78.88 SE
ANISOU 7 SE MSE A 1 9771 9748 10453 1461 1387 -819 SE
HETATM 8 CE MSE A 1 -18.916 -7.899 8.695 1.00 65.02 C
ANISOU 8 CE MSE A 1 8067 8042 8595 1098 1118 -698 C
(ATOM LINES ARE NOT SHOWN.)
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