HEADER TRANSCRIPTION 27-SEP-12 4HAM
TITLE CRYSTAL STRUCTURE OF TRANSCRIPTIONAL ANTITERMINATOR FROM LISTERIA
TITLE 2 MONOCYTOGENES EGD-E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LMO2241 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSCRIPTIONAL ANTITERMINATOR BGLG;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 169963;
SOURCE 4 STRAIN: EGD-E;
SOURCE 5 GENE: LMO2241;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, WINGED HELIX-TURN-HELIX, FOUR HELIX BUNDLE,
KEYWDS 3 TRANSCRIPTIONAL REGULATOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,G.CHHOR,M.ENDRES,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 1 17-OCT-12 4HAM 0
JRNL AUTH Y.KIM,G.CHHOR,M.ENDRES,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF TRANSCRIPTIONAL ANTITERMINATOR FROM
JRNL TITL 2 LISTERIA MONOCYTOGENES EGD-E
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1161)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 12249
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1221
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 32.2530 - 3.9606 0.95 1284 143 0.1701 0.1929
REMARK 3 2 3.9606 - 3.1445 0.97 1252 139 0.1644 0.2009
REMARK 3 3 3.1445 - 2.7473 0.97 1248 139 0.1768 0.2292
REMARK 3 4 2.7473 - 2.4962 0.98 1233 138 0.1801 0.2205
REMARK 3 5 2.4962 - 2.3173 0.97 1224 135 0.1724 0.2524
REMARK 3 6 2.3173 - 2.1807 0.97 1222 135 0.1658 0.2270
REMARK 3 7 2.1807 - 2.0715 0.97 1209 134 0.1691 0.2522
REMARK 3 8 2.0715 - 1.9814 0.96 1211 134 0.1862 0.2311
REMARK 3 9 1.9814 - 1.9051 0.92 1145 124 0.2218 0.2541
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.90
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 : 0.006 1180
REMARK 3 ANGLE : 0.854 1596
REMARK 3 CHIRALITY : 0.061 182
REMARK 3 PLANARITY : 0.003 207
REMARK 3 DIHEDRAL : 15.344 465
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 -2 through 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5178 28.9087 44.1480
REMARK 3 T TENSOR
REMARK 3 T11: 0.3477 T22: 0.2913
REMARK 3 T33: 0.3187 T12: -0.0019
REMARK 3 T13: 0.0396 T23: 0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 3.6167 L22: 2.0471
REMARK 3 L33: 2.1916 L12: 0.1284
REMARK 3 L13: 0.4682 L23: 2.1276
REMARK 3 S TENSOR
REMARK 3 S11: 0.2654 S12: -0.1750 S13: 0.0432
REMARK 3 S21: -0.3380 S22: -0.5005 S23: 0.1522
REMARK 3 S31: 0.0221 S32: 0.5765 S33: -0.0226
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 12 through 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4578 32.3691 50.3781
REMARK 3 T TENSOR
REMARK 3 T11: 0.2086 T22: 0.1961
REMARK 3 T33: 0.2069 T12: -0.0201
REMARK 3 T13: 0.0072 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 3.1312 L22: 0.5548
REMARK 3 L33: 0.6157 L12: 0.0180
REMARK 3 L13: -0.8239 L23: 0.3131
REMARK 3 S TENSOR
REMARK 3 S11: 0.0437 S12: 0.1775 S13: 0.6054
REMARK 3 S21: -0.1333 S22: 0.0383 S23: 0.0520
REMARK 3 S31: -0.1556 S32: -0.1145 S33: -0.0743
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 27 through 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1897 23.3205 59.9162
REMARK 3 T TENSOR
REMARK 3 T11: 0.2519 T22: 0.2782
REMARK 3 T33: 0.1891 T12: -0.0174
REMARK 3 T13: 0.0023 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 2.1025 L22: 1.7504
REMARK 3 L33: 0.1225 L12: -0.1058
REMARK 3 L13: -0.0004 L23: -0.4675
REMARK 3 S TENSOR
REMARK 3 S11: -0.0661 S12: -0.0892 S13: -0.0095
REMARK 3 S21: 0.2138 S22: 0.1060 S23: 0.1817
REMARK 3 S31: -0.0476 S32: 0.0296 S33: -0.0412
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 38 through 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6251 21.3911 50.1312
REMARK 3 T TENSOR
REMARK 3 T11: 0.1732 T22: 0.2228
REMARK 3 T33: 0.1936 T12: -0.0018
REMARK 3 T13: 0.0079 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 2.8279 L22: 4.0724
REMARK 3 L33: 1.4695 L12: 2.1133
REMARK 3 L13: -1.3414 L23: 0.2881
REMARK 3 S TENSOR
REMARK 3 S11: -0.1394 S12: -0.3350 S13: -0.4655
REMARK 3 S21: -0.1142 S22: -0.1006 S23: -0.0263
REMARK 3 S31: 0.2948 S32: 0.3208 S33: 0.0566
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 49 through 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2727 32.4524 55.4082
REMARK 3 T TENSOR
REMARK 3 T11: 0.2126 T22: 0.2601
REMARK 3 T33: 0.2759 T12: -0.0267
REMARK 3 T13: -0.0306 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 1.2436 L22: 3.7461
REMARK 3 L33: 1.6970 L12: -2.1648
REMARK 3 L13: -1.2496 L23: 2.2689
REMARK 3 S TENSOR
REMARK 3 S11: 0.1415 S12: -0.3304 S13: 0.6398
REMARK 3 S21: 0.0575 S22: 0.1245 S23: -0.5355
REMARK 3 S31: -0.5497 S32: 0.4953 S33: -0.0973
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 62 through 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5750 27.6788 64.2830
REMARK 3 T TENSOR
REMARK 3 T11: 0.2147 T22: 0.2780
REMARK 3 T33: 0.1649 T12: 0.0112
REMARK 3 T13: 0.0063 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 1.5994 L22: 3.2649
REMARK 3 L33: 1.9690 L12: -0.8580
REMARK 3 L13: 0.8040 L23: -2.0556
REMARK 3 S TENSOR
REMARK 3 S11: -0.1652 S12: -0.1532 S13: 0.3979
REMARK 3 S21: 0.2409 S22: -0.0325 S23: -0.7592
REMARK 3 S31: -0.0554 S32: 0.1461 S33: 0.0825
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'A' and (resid 76 through 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1850 35.8900 65.7999
REMARK 3 T TENSOR
REMARK 3 T11: 0.6957 T22: 0.7219
REMARK 3 T33: 0.5938 T12: 0.1707
REMARK 3 T13: 0.2409 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 0.3282 L22: 6.5356
REMARK 3 L33: 0.9870 L12: -0.6067
REMARK 3 L13: 0.5742 L23: -1.1531
REMARK 3 S TENSOR
REMARK 3 S11: -0.2897 S12: 0.1589 S13: 0.3394
REMARK 3 S21: 1.8750 S22: -0.4427 S23: 1.7920
REMARK 3 S31: -0.9068 S32: -1.3771 S33: -0.5914
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'A' and (resid 85 through 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8638 50.4468 48.6727
REMARK 3 T TENSOR
REMARK 3 T11: 0.2586 T22: 0.1587
REMARK 3 T33: 0.2707 T12: 0.0001
REMARK 3 T13: -0.0157 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.6831 L22: 1.7484
REMARK 3 L33: 4.8315 L12: 0.4394
REMARK 3 L13: 0.2590 L23: -2.5655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0849 S12: -0.0977 S13: 0.2240
REMARK 3 S21: 0.4385 S22: -0.1588 S23: -0.3516
REMARK 3 S31: -0.3451 S32: 0.3368 S33: 0.0515
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'A' and (resid 105 through 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8174 41.9495 41.3354
REMARK 3 T TENSOR
REMARK 3 T11: 0.2700 T22: 0.2345
REMARK 3 T33: 0.3295 T12: -0.0410
REMARK 3 T13: -0.0514 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.4653 L22: 3.0094
REMARK 3 L33: 1.1261 L12: 0.4731
REMARK 3 L13: -0.6086 L23: -1.5652
REMARK 3 S TENSOR
REMARK 3 S11: -0.0975 S12: 0.3786 S13: -0.1527
REMARK 3 S21: -0.5504 S22: 0.2998 S23: 0.5579
REMARK 3 S31: 0.5298 S32: -0.5003 S33: -0.1269
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'A' and (resid 125 through 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6744 20.5562 54.7818
REMARK 3 T TENSOR
REMARK 3 T11: 0.7512 T22: 0.3685
REMARK 3 T33: 0.5212 T12: 0.0520
REMARK 3 T13: 0.0684 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.0285 L22: 0.1120
REMARK 3 L33: 0.1104 L12: -0.0026
REMARK 3 L13: 0.0541 L23: -0.0818
REMARK 3 S TENSOR
REMARK 3 S11: -0.2305 S12: -0.2654 S13: -0.4542
REMARK 3 S21: 1.1258 S22: -0.0182 S23: -0.3364
REMARK 3 S31: 1.0396 S32: 0.0440 S33: 0.1339
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 4HAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB075228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12529
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.56100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000, PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 0.1 M HEPES PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 45.99950
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 45.99950
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 18.56100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.07600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 18.56100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.07600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.99950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 18.56100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.07600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.99950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 18.56100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.07600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: DIMER IS FORMED BY: X,Y,Z AND X,-Y+1,-Z+1
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: 6400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 92.15200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 91.99900
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 367 LIES ON A SPECIAL POSITION.
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 122 O HOH A 348 2.16
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 SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 206
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC106881 RELATED DB: TARGETTRACK
DBREF 4HAM A 1 131 UNP Q8Y535 Q8Y535_LISMO 1 131
SEQADV 4HAM SER A -2 UNP Q8Y535 EXPRESSION TAG
SEQADV 4HAM ASN A -1 UNP Q8Y535 EXPRESSION TAG
SEQADV 4HAM ALA A 0 UNP Q8Y535 EXPRESSION TAG
SEQRES 1 A 134 SER ASN ALA MSE PHE THR ILE ASN THR LYS SER GLN LEU
SEQRES 2 A 134 PRO ILE TYR GLU GLN ILE VAL GLN LYS ILE LYS GLU GLN
SEQRES 3 A 134 VAL VAL LYS GLY VAL LEU GLN GLU GLY GLU LYS ILE LEU
SEQRES 4 A 134 SER ILE ARG GLU PHE ALA SER ARG ILE GLY VAL ASN PRO
SEQRES 5 A 134 ASN THR VAL SER LYS ALA TYR GLN GLU LEU GLU ARG GLN
SEQRES 6 A 134 GLU VAL ILE ILE THR VAL LYS GLY LYS GLY THR PHE ILE
SEQRES 7 A 134 ALA ASN GLN THR ASP LYS LEU SER SER PRO LYS LYS LEU
SEQRES 8 A 134 ALA GLU THR ARG THR LYS LEU LYS GLU THR ILE LEU ASP
SEQRES 9 A 134 LEU VAL TYR LEU GLY VAL ASN ILE GLU GLU ILE HIS LYS
SEQRES 10 A 134 LEU ALA ASP GLU TYR SER GLN ASP ILE ILE GLY GLY ASP
SEQRES 11 A 134 VAL VAL GLU GLY
MODRES 4HAM MSE A 1 MET SELENOMETHIONINE
HET MSE A 1 8
HET SO4 A 201 5
HET SO4 A 202 5
HET GOL A 203 6
HET GOL A 204 6
HET GOL A 205 6
HET GOL A 206 6
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE C5 H11 N O2 SE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 8 HOH *95(H2 O)
HELIX 1 1 PRO A 11 LYS A 26 1 16
HELIX 2 2 SER A 37 GLY A 46 1 10
HELIX 3 3 ASN A 48 GLN A 62 1 15
HELIX 4 4 SER A 84 LEU A 105 1 22
HELIX 5 5 ASN A 108 GLY A 125 1 18
SHEET 1 A 3 LYS A 34 ILE A 35 0
SHEET 2 A 3 GLY A 72 ILE A 75 -1 O THR A 73 N ILE A 35
SHEET 3 A 3 ILE A 65 VAL A 68 -1 N VAL A 68 O GLY A 72
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N PHE A 2 1555 1555 1.33
SITE 1 AC1 3 SER A 8 GLN A 9 THR A 93
SITE 1 AC2 5 ALA A 0 MSE A 1 ARG A 44 ASN A 48
SITE 2 AC2 5 HOH A 366
SITE 1 AC3 3 SER A 37 ILE A 38 ARG A 39
SITE 1 AC4 4 GLN A 78 LYS A 81 VAL A 103 TYR A 104
SITE 1 AC5 4 GLU A 33 LYS A 34 LYS A 71 HOH A 376
SITE 1 AC6 5 PRO A 11 ILE A 12 HOH A 305 HOH A 314
SITE 2 AC6 5 HOH A 377
CRYST1 37.122 92.152 91.999 90.00 90.00 90.00 C 2 2 21 8
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 0.026938 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010852 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010870 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
