HEADER SIGNALING PROTEIN 16-SEP-11 3TUF
TITLE STRUCTURE OF THE SPOIIQ-SPOIIIAH PORE FORMING COMPLEX.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STAGE II SPORULATION PROTEIN Q;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: STAGE III SPORULATION PROTEIN AH;
COMPND 8 CHAIN: A;
COMPND 9 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: BSU36550, SPOIIQ, YWNI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-YSBLIC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 13 ORGANISM_TAXID: 1423;
SOURCE 14 STRAIN: 168;
SOURCE 15 GENE: BSU24360, SPOIIIAH;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-YSBLIC
KEYWDS INTERCELLULAR SIGNALLING, INTERCELLULAR CHANNEL, SPORULATION, CELL
KEYWDS 2 ENGULFMENT AND SIGNALLING, INTERCELLULAR SPACE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.M.LEVDIKOV,E.V.BLAGOVA,A.J.WILKINSON
REVDAT 3 28-FEB-24 3TUF 1 SEQADV
REVDAT 2 18-JUL-12 3TUF 1 JRNL
REVDAT 1 14-MAR-12 3TUF 0
JRNL AUTH V.M.LEVDIKOV,E.V.BLAGOVA,A.MCFEAT,M.J.FOGG,K.S.WILSON,
JRNL AUTH 2 A.J.WILKINSON
JRNL TITL STRUCTURE OF COMPONENTS OF AN INTERCELLULAR CHANNEL COMPLEX
JRNL TITL 2 IN SPORULATING BACILLUS SUBTILIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 5441 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22431604
JRNL DOI 10.1073/PNAS.1120087109
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0086
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 22507
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1217
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 REFLECTION IN BIN (WORKING SET) : 905
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1670
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2096
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.96000
REMARK 3 B22 (A**2) : -1.31000
REMARK 3 B33 (A**2) : 3.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.140
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2118 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2854 ; 2.095 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 271 ; 6.543 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;38.852 ;27.128
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 405 ;21.564 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;24.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 335 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1546 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5884 ; 5.065 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 117 ;20.424 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2096 ;27.051 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 103 A 217
REMARK 3 ORIGIN FOR THE GROUP (A): 33.133 6.688 30.106
REMARK 3 T TENSOR
REMARK 3 T11: 0.0244 T22: 0.0685
REMARK 3 T33: 0.2576 T12: 0.0007
REMARK 3 T13: 0.0054 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.7122 L22: 0.1037
REMARK 3 L33: 0.0760 L12: -0.2204
REMARK 3 L13: 0.1933 L23: -0.0334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0114 S12: 0.0355 S13: 0.0348
REMARK 3 S21: -0.0058 S22: -0.0279 S23: -0.0235
REMARK 3 S31: 0.0025 S32: 0.0060 S33: 0.0165
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 103 B 217
REMARK 3 ORIGIN FOR THE GROUP (A): 16.211 28.591 30.576
REMARK 3 T TENSOR
REMARK 3 T11: 0.0229 T22: 0.0721
REMARK 3 T33: 0.2846 T12: -0.0013
REMARK 3 T13: 0.0058 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.0541 L22: 0.1200
REMARK 3 L33: 0.1275 L12: 0.0083
REMARK 3 L13: -0.0050 L23: 0.1197
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: -0.0026 S13: -0.0350
REMARK 3 S21: 0.0163 S22: -0.0059 S23: 0.0013
REMARK 3 S31: 0.0090 S32: -0.0172 S33: 0.0055
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3TUF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000067932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL
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 : 23724
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
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 (%) : 83.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 32.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE,50% PEG 400, 0.5
REMARK 280 MM SPERMIDINE, PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
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 0.00000
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 39.39850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.54400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.04650
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.39850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.54400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.04650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.39850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.54400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.04650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.39850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.54400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.04650
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 78.79700
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY B 39
REMARK 465 PRO B 40
REMARK 465 ALA B 41
REMARK 465 MET B 42
REMARK 465 GLN B 43
REMARK 465 SER B 44
REMARK 465 VAL B 45
REMARK 465 SER B 46
REMARK 465 ASN B 47
REMARK 465 ASP B 48
REMARK 465 GLU B 49
REMARK 465 VAL B 50
REMARK 465 LYS B 51
REMARK 465 ASP B 52
REMARK 465 GLN B 53
REMARK 465 LEU B 54
REMARK 465 ALA B 55
REMARK 465 ASP B 56
REMARK 465 ASN B 57
REMARK 465 GLY B 58
REMARK 465 GLY B 59
REMARK 465 ASN B 60
REMARK 465 SER B 61
REMARK 465 ALA B 62
REMARK 465 TYR B 63
REMARK 465 ASP B 64
REMARK 465 ASN B 65
REMARK 465 ASN B 66
REMARK 465 ASP B 67
REMARK 465 ASP B 68
REMARK 465 ALA B 69
REMARK 465 VAL B 70
REMARK 465 GLU B 71
REMARK 465 VAL B 72
REMARK 465 GLY B 73
REMARK 465 LYS B 74
REMARK 465 GLN B 233
REMARK 465 GLU B 234
REMARK 465 THR B 235
REMARK 465 GLU B 236
REMARK 465 GLU B 237
REMARK 465 SER B 238
REMARK 465 ILE B 239
REMARK 465 GLN B 240
REMARK 465 GLN B 241
REMARK 465 SER B 242
REMARK 465 SER B 243
REMARK 465 GLU B 244
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 ASP B 247
REMARK 465 GLY B 248
REMARK 465 SER B 249
REMARK 465 THR B 250
REMARK 465 GLU B 251
REMARK 465 LYS B 252
REMARK 465 GLY B 253
REMARK 465 THR B 254
REMARK 465 GLU B 255
REMARK 465 GLU B 256
REMARK 465 LYS B 257
REMARK 465 SER B 258
REMARK 465 GLY B 259
REMARK 465 GLU B 260
REMARK 465 LYS B 261
REMARK 465 LYS B 262
REMARK 465 ASP B 263
REMARK 465 ASP B 264
REMARK 465 SER B 265
REMARK 465 THR B 266
REMARK 465 ASP B 267
REMARK 465 LYS B 268
REMARK 465 SER B 269
REMARK 465 GLY B 270
REMARK 465 SER B 271
REMARK 465 LYS B 272
REMARK 465 GLU B 273
REMARK 465 SER B 274
REMARK 465 SER B 275
REMARK 465 THR B 276
REMARK 465 THR B 277
REMARK 465 GLU B 278
REMARK 465 ASP B 279
REMARK 465 THR B 280
REMARK 465 GLU B 281
REMARK 465 GLN B 282
REMARK 465 SER B 283
REMARK 465 GLY A 22
REMARK 465 PRO A 23
REMARK 465 ALA A 24
REMARK 465 MET A 25
REMARK 465 SER A 26
REMARK 465 PRO A 27
REMARK 465 GLU A 28
REMARK 465 SER A 29
REMARK 465 LYS A 30
REMARK 465 ASN A 31
REMARK 465 ALA A 32
REMARK 465 VAL A 33
REMARK 465 GLN A 34
REMARK 465 MET A 35
REMARK 465 GLN A 36
REMARK 465 SER A 37
REMARK 465 GLU A 38
REMARK 465 LYS A 39
REMARK 465 SER A 40
REMARK 465 ALA A 41
REMARK 465 SER A 42
REMARK 465 ASP A 43
REMARK 465 SER A 44
REMARK 465 GLY A 45
REMARK 465 GLU A 46
REMARK 465 VAL A 47
REMARK 465 ALA A 48
REMARK 465 THR A 49
REMARK 465 GLU A 50
REMARK 465 LYS A 51
REMARK 465 ALA A 52
REMARK 465 PRO A 53
REMARK 465 ALA A 54
REMARK 465 LYS A 55
REMARK 465 GLN A 56
REMARK 465 ASP A 57
REMARK 465 THR A 58
REMARK 465 LYS A 59
REMARK 465 GLU A 60
REMARK 465 LYS A 61
REMARK 465 SER A 62
REMARK 465 GLY A 63
REMARK 465 THR A 64
REMARK 465 GLU A 65
REMARK 465 THR A 66
REMARK 465 GLU A 67
REMARK 465 LYS A 68
REMARK 465 GLY A 69
REMARK 465 LYS A 70
REMARK 465 GLU A 71
REMARK 465 ASP A 72
REMARK 465 GLY A 73
REMARK 465 THR A 74
REMARK 465 LYS A 75
REMARK 465 GLY A 76
REMARK 465 THR A 77
REMARK 465 LYS A 78
REMARK 465 ASP A 79
REMARK 465 SER A 80
REMARK 465 SER A 81
REMARK 465 ALA A 82
REMARK 465 ASP A 83
REMARK 465 LYS A 84
REMARK 465 GLU A 85
REMARK 465 THR A 86
REMARK 465 SER A 87
REMARK 465 ALA A 88
REMARK 465 GLU A 89
REMARK 465 ALA A 90
REMARK 465 SER A 91
REMARK 465 GLU A 92
REMARK 465 LYS A 93
REMARK 465 GLY A 94
REMARK 465 THR A 95
REMARK 465 VAL A 96
REMARK 465 VAL A 97
REMARK 465 THR A 98
REMARK 465 GLU A 99
REMARK 465 THR A 100
REMARK 465 ALA A 101
REMARK 465 ASP A 102
REMARK 465 LYS A 218
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 MET B 76 -10.53 68.89
REMARK 500 PRO B 82 43.07 -83.18
REMARK 500 TYR B 112 -78.96 -98.87
REMARK 500 ASN B 113 -86.76 -125.86
REMARK 500 HIS B 159 -159.03 -115.82
REMARK 500 ASP B 210 47.80 39.56
REMARK 500 PRO B 223 157.10 -47.00
REMARK 500 SER A 185 142.13 -178.74
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3TUF B 43 283 UNP P71044 SP2Q_BACSU 43 283
DBREF 3TUF A 25 218 UNP P49785 SP3AH_BACSU 25 218
SEQADV 3TUF GLY B 39 UNP P71044 EXPRESSION TAG
SEQADV 3TUF PRO B 40 UNP P71044 EXPRESSION TAG
SEQADV 3TUF ALA B 41 UNP P71044 EXPRESSION TAG
SEQADV 3TUF MET B 42 UNP P71044 EXPRESSION TAG
SEQADV 3TUF GLY A 22 UNP P49785 EXPRESSION TAG
SEQADV 3TUF PRO A 23 UNP P49785 EXPRESSION TAG
SEQADV 3TUF ALA A 24 UNP P49785 EXPRESSION TAG
SEQRES 1 B 245 GLY PRO ALA MET GLN SER VAL SER ASN ASP GLU VAL LYS
SEQRES 2 B 245 ASP GLN LEU ALA ASP ASN GLY GLY ASN SER ALA TYR ASP
SEQRES 3 B 245 ASN ASN ASP ASP ALA VAL GLU VAL GLY LYS SER MET GLU
SEQRES 4 B 245 ASN VAL ALA MET PRO VAL VAL ASP SER GLU ASN VAL SER
SEQRES 5 B 245 VAL VAL LYS LYS PHE TYR GLU THR ASP ALA ALA LYS GLU
SEQRES 6 B 245 GLU LYS GLU ALA ALA LEU VAL THR TYR ASN ASN THR TYR
SEQRES 7 B 245 SER LEU SER LYS GLY ILE ASP LEU ALA GLU LYS ASP GLY
SEQRES 8 B 245 LYS ASP PHE ASP VAL SER ALA SER LEU SER GLY THR VAL
SEQRES 9 B 245 VAL LYS ALA GLU LYS ASP PRO VAL LEU GLY TYR VAL VAL
SEQRES 10 B 245 GLU VAL GLU HIS ALA ASP GLY LEU SER THR VAL TYR GLN
SEQRES 11 B 245 SER LEU SER GLU VAL SER VAL GLU GLN GLY ASP LYS VAL
SEQRES 12 B 245 LYS GLN ASN GLN VAL ILE GLY LYS SER GLY LYS ASN LEU
SEQRES 13 B 245 TYR SER GLU ASP SER GLY ASN HIS VAL HIS PHE GLU ILE
SEQRES 14 B 245 ARG LYS ASP GLY VAL ALA MET ASN PRO LEU ASN PHE MET
SEQRES 15 B 245 ASP LYS PRO VAL SER SER ILE GLU LYS ALA ALA THR GLN
SEQRES 16 B 245 GLU THR GLU GLU SER ILE GLN GLN SER SER GLU LYS LYS
SEQRES 17 B 245 ASP GLY SER THR GLU LYS GLY THR GLU GLU LYS SER GLY
SEQRES 18 B 245 GLU LYS LYS ASP ASP SER THR ASP LYS SER GLY SER LYS
SEQRES 19 B 245 GLU SER SER THR THR GLU ASP THR GLU GLN SER
SEQRES 1 A 197 GLY PRO ALA MET SER PRO GLU SER LYS ASN ALA VAL GLN
SEQRES 2 A 197 MET GLN SER GLU LYS SER ALA SER ASP SER GLY GLU VAL
SEQRES 3 A 197 ALA THR GLU LYS ALA PRO ALA LYS GLN ASP THR LYS GLU
SEQRES 4 A 197 LYS SER GLY THR GLU THR GLU LYS GLY LYS GLU ASP GLY
SEQRES 5 A 197 THR LYS GLY THR LYS ASP SER SER ALA ASP LYS GLU THR
SEQRES 6 A 197 SER ALA GLU ALA SER GLU LYS GLY THR VAL VAL THR GLU
SEQRES 7 A 197 THR ALA ASP ASP ASP LEU PHE THR THR TYR ARG LEU ASP
SEQRES 8 A 197 LEU GLU ASP ALA ARG SER LYS GLU ARG GLU GLU LEU ASN
SEQRES 9 A 197 ALA ILE VAL SER SER ASP ASP ALA THR ALA LYS GLU LYS
SEQRES 10 A 197 SER GLU ALA TYR ASP LYS MET THR ALA LEU SER GLU VAL
SEQRES 11 A 197 GLU GLY THR GLU LYS GLN LEU GLU THR LEU ILE LYS THR
SEQRES 12 A 197 GLN GLY TYR GLU ASP ALA LEU VAL ASN ALA GLU GLY ASP
SEQRES 13 A 197 LYS ILE ASN ILE THR VAL LYS SER ASP LYS HIS SER LYS
SEQRES 14 A 197 SER LYS ALA THR ALA ILE ILE ASP LEU VAL ALA LYS GLU
SEQRES 15 A 197 ILE LYS THR MET LYS ASP VAL ALA VAL THR PHE GLU PRO
SEQRES 16 A 197 SER LYS
FORMUL 3 HOH *104(H2 O)
HELIX 1 1 ASP B 85 GLU B 87 5 3
HELIX 2 2 ALA B 101 ALA B 108 1 8
HELIX 3 3 SER B 196 GLY B 200 5 5
HELIX 4 4 ASN B 215 PHE B 219 5 5
HELIX 5 5 PRO B 223 GLU B 228 5 6
HELIX 6 6 ASP A 104 SER A 129 1 26
HELIX 7 7 THR A 134 GLN A 165 1 32
HELIX 8 8 SER A 189 LEU A 199 1 11
HELIX 9 9 ALA A 201 THR A 206 1 6
SHEET 1 A 7 VAL B 89 LYS B 93 0
SHEET 2 A 7 ILE B 122 GLU B 126 -1 O ASP B 123 N VAL B 92
SHEET 3 A 7 VAL B 203 LYS B 209 -1 O PHE B 205 N ILE B 122
SHEET 4 A 7 LEU B 163 LEU B 170 -1 N SER B 164 O ARG B 208
SHEET 5 A 7 GLY B 152 GLU B 158 -1 N VAL B 155 O TYR B 167
SHEET 6 A 7 GLY B 140 ASP B 148 -1 N THR B 141 O GLU B 158
SHEET 7 A 7 LYS B 180 VAL B 181 -1 O VAL B 181 N GLY B 140
SHEET 1 B 4 VAL B 89 LYS B 93 0
SHEET 2 B 4 ILE B 122 GLU B 126 -1 O ASP B 123 N VAL B 92
SHEET 3 B 4 VAL B 203 LYS B 209 -1 O PHE B 205 N ILE B 122
SHEET 4 B 4 VAL B 212 MET B 214 -1 O MET B 214 N ILE B 207
SHEET 1 C 5 LEU B 109 THR B 111 0
SHEET 2 C 5 THR B 115 LEU B 118 -1 O SER B 117 N VAL B 110
SHEET 3 C 5 ASP A 209 GLU A 215 -1 O VAL A 212 N TYR B 116
SHEET 4 C 5 LYS A 178 LYS A 184 1 N ILE A 179 O ALA A 211
SHEET 5 C 5 ALA A 170 ASN A 173 -1 N LEU A 171 O THR A 182
SHEET 1 D 3 ASP B 133 SER B 135 0
SHEET 2 D 3 VAL B 186 LYS B 189 -1 O ILE B 187 N VAL B 134
SHEET 3 D 3 GLU B 172 VAL B 173 -1 N GLU B 172 O LYS B 189
CISPEP 1 ALA B 230 ALA B 231 0 1.84
CRYST1 78.797 111.088 136.093 90.00 90.00 90.00 I 2 2 2 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 0.012691 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007348 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
