HEADER TRANSCRIPTION REGULATOR 18-JAN-08 3C07
TITLE CRYSTAL STRUCTURE OF A TETR FAMILY TRANSCRIPTIONAL REGULATOR FROM
TITLE 2 STREPTOMYCES COELICOLOR A3(2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE TETR-FAMILY TRANSCRIPTIONAL REGULATOR;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR A3(2);
SOURCE 3 ORGANISM_TAXID: 100226;
SOURCE 4 STRAIN: A3(2) / M145;
SOURCE 5 ATCC: BAA-471;
SOURCE 6 GENE: SCO4850, SC5G8.18C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS APC6322, TETR, STREPTOMYCES COELICOLOR A3(2), STRUCTURAL GENOMICS,
KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, DNA-BINDING, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 4 REGULATION, TRANSCRIPTION REGULATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,X.XU,H.ZHENG,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 3 13-JUL-11 3C07 1 VERSN
REVDAT 2 24-FEB-09 3C07 1 VERSN
REVDAT 1 05-FEB-08 3C07 0
SPRSDE 05-FEB-08 3C07 2OFL
JRNL AUTH K.TAN,X.XU,H.ZHENG,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK
JRNL TITL THE STRUCTURE OF A TETR FAMILY TRANSCRIPTIONAL REGULATOR
JRNL TITL 2 FROM STREPTOMYCES COELICOLOR A3(2).
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 16127
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 854
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1152
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3514
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 0.87000
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): 0.794
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.372
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.298
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.242
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3603 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4874 ; 1.891 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 433 ; 6.480 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;33.127 ;21.556
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 612 ;25.420 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;19.309 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 530 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2758 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1868 ; 0.258 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2486 ; 0.326 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 122 ; 0.170 ; 0.200
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): 49 ; 0.241 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.311 ; 0.200
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): 2215 ; 1.240 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3468 ; 2.003 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1555 ; 1.359 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1406 ; 2.079 ; 3.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
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 15 A 63
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5620 76.3300 108.3420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1053 T22: 0.0509
REMARK 3 T33: -0.0635 T12: -0.1088
REMARK 3 T13: 0.1803 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 5.7942 L22: 11.9661
REMARK 3 L33: 10.4919 L12: -1.0200
REMARK 3 L13: -0.7849 L23: -5.1157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: 0.3059 S13: 0.5437
REMARK 3 S21: 0.2363 S22: -0.1984 S23: -0.2848
REMARK 3 S31: -0.4847 S32: 0.0801 S33: 0.2489
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 : A 64 A 235
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7510 48.8480 103.6430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0164 T22: 0.1904
REMARK 3 T33: -0.2278 T12: -0.1041
REMARK 3 T13: 0.1536 T23: -0.2053
REMARK 3 L TENSOR
REMARK 3 L11: 3.2609 L22: 5.2590
REMARK 3 L33: 2.7611 L12: 0.2815
REMARK 3 L13: 0.1977 L23: 1.2324
REMARK 3 S TENSOR
REMARK 3 S11: 0.0409 S12: 0.6361 S13: -0.2787
REMARK 3 S21: -0.6433 S22: 0.2208 S23: -0.8559
REMARK 3 S31: -0.0170 S32: 0.1386 S33: -0.2616
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 16 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5590 58.8420 143.9740
REMARK 3 T TENSOR
REMARK 3 T11: -0.0415 T22: 0.5749
REMARK 3 T33: -0.1460 T12: -0.0622
REMARK 3 T13: -0.0651 T23: -0.1978
REMARK 3 L TENSOR
REMARK 3 L11: 15.2891 L22: 6.2631
REMARK 3 L33: 11.3372 L12: -2.5319
REMARK 3 L13: 3.3185 L23: -0.3263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: -1.1463 S13: -0.5035
REMARK 3 S21: 0.0810 S22: -0.2936 S23: 1.1230
REMARK 3 S31: 0.3022 S32: -2.6109 S33: 0.2639
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 64 B 229
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7650 40.1690 125.1280
REMARK 3 T TENSOR
REMARK 3 T11: 0.3088 T22: 0.0615
REMARK 3 T33: -0.1126 T12: 0.0524
REMARK 3 T13: -0.3010 T23: -0.1657
REMARK 3 L TENSOR
REMARK 3 L11: 3.4294 L22: 5.1436
REMARK 3 L33: 4.9134 L12: 2.1902
REMARK 3 L13: 1.6270 L23: 2.1342
REMARK 3 S TENSOR
REMARK 3 S11: 0.2421 S12: -0.1349 S13: -0.7161
REMARK 3 S21: 1.2868 S22: 0.3177 S23: -1.0520
REMARK 3 S31: 0.8583 S32: 0.4530 S33: -0.5598
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3C07 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-08.
REMARK 100 THE RCSB ID CODE IS RCSB046176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.97931
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17068
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 47.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 18.100
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 54.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 16.00
REMARK 200 R MERGE FOR SHELL (I) : 0.86700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, RESOLVE, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 AMMONIUM SULFATE, 0.1M TRIS-HCL,
REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 104.03750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.47350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.47350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 156.05625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.47350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.47350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.01875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.47350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.47350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 156.05625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.47350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.47350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.01875
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 104.03750
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: 3200 ANGSTROM**2
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 -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 ASN A 5
REMARK 465 ASP A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 8
REMARK 465 ASP A 9
REMARK 465 ASP A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 HIS A 13
REMARK 465 LEU A 14
REMARK 465 MSE A 236
REMARK 465 PRO A 237
REMARK 465 ASP A 238
REMARK 465 PRO A 239
REMARK 465 ALA A 240
REMARK 465 LYS A 241
REMARK 465 LYS A 242
REMARK 465 PRO A 243
REMARK 465 THR A 244
REMARK 465 ARG A 245
REMARK 465 ASP A 246
REMARK 465 ALA A 247
REMARK 465 GLY A 248
REMARK 465 PRO A 249
REMARK 465 GLN A 250
REMARK 465 ALA A 251
REMARK 465 MSE B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 ARG B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 3
REMARK 465 THR B 4
REMARK 465 ASN B 5
REMARK 465 ASP B 6
REMARK 465 GLY B 7
REMARK 465 PRO B 8
REMARK 465 ASP B 9
REMARK 465 ASP B 10
REMARK 465 GLY B 11
REMARK 465 ALA B 12
REMARK 465 HIS B 13
REMARK 465 LEU B 14
REMARK 465 SER B 15
REMARK 465 PRO B 230
REMARK 465 GLY B 231
REMARK 465 MSE B 232
REMARK 465 THR B 233
REMARK 465 LYS B 234
REMARK 465 VAL B 235
REMARK 465 MSE B 236
REMARK 465 PRO B 237
REMARK 465 ASP B 238
REMARK 465 PRO B 239
REMARK 465 ALA B 240
REMARK 465 LYS B 241
REMARK 465 LYS B 242
REMARK 465 PRO B 243
REMARK 465 THR B 244
REMARK 465 ARG B 245
REMARK 465 ASP B 246
REMARK 465 ALA B 247
REMARK 465 GLY B 248
REMARK 465 PRO B 249
REMARK 465 GLN B 250
REMARK 465 ALA B 251
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 GLU A 186 -83.04 -47.79
REMARK 500 ALA A 209 -0.38 -58.93
REMARK 500 ARG B 39 32.74 -85.57
REMARK 500 ALA B 61 72.15 -69.10
REMARK 500 ASP B 72 -53.63 -29.19
REMARK 500 SER B 132 158.78 -40.62
REMARK 500 ALA B 151 -23.81 -38.64
REMARK 500 PRO B 166 -64.45 -28.44
REMARK 500 GLU B 189 -53.92 -28.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 39 23.2 L L OUTSIDE RANGE
REMARK 500 ILE A 164 24.2 L L OUTSIDE RANGE
REMARK 500 PHE B 32 24.5 L L OUTSIDE RANGE
REMARK 500 ARG B 35 23.0 L L OUTSIDE RANGE
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 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 252
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC6322 RELATED DB: TARGETDB
DBREF 3C07 A 1 251 UNP Q9KZ96 Q9KZ96_STRCO 1 251
DBREF 3C07 B 1 251 UNP Q9KZ96 Q9KZ96_STRCO 1 251
SEQADV 3C07 MSE A -21 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLY A -20 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER A -19 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER A -18 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS A -17 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS A -16 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS A -15 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS A -14 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS A -13 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS A -12 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER A -11 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER A -10 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLY A -9 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 ARG A -8 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLU A -7 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 ASN A -6 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 LEU A -5 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 TYR A -4 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 PHE A -3 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLN A -2 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLY A -1 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS A 0 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 MSE B -21 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLY B -20 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER B -19 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER B -18 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS B -17 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS B -16 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS B -15 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS B -14 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS B -13 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS B -12 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER B -11 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 SER B -10 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLY B -9 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 ARG B -8 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLU B -7 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 ASN B -6 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 LEU B -5 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 TYR B -4 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 PHE B -3 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLN B -2 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 GLY B -1 UNP Q9KZ96 EXPRESSION TAG
SEQADV 3C07 HIS B 0 UNP Q9KZ96 EXPRESSION TAG
SEQRES 1 A 273 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 273 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE PRO ALA THR
SEQRES 3 A 273 ASN ASP GLY PRO ASP ASP GLY ALA HIS LEU SER LYS SER
SEQRES 4 A 273 GLU GLN THR ARG ALA LEU ILE LEU GLU THR ALA MSE ARG
SEQRES 5 A 273 LEU PHE GLN GLU ARG GLY TYR ASP ARG THR THR MSE ARG
SEQRES 6 A 273 ALA ILE ALA GLN GLU ALA GLY VAL SER VAL GLY ASN ALA
SEQRES 7 A 273 TYR TYR TYR PHE ALA GLY LYS GLU HIS LEU ILE GLN GLY
SEQRES 8 A 273 PHE TYR ASP ARG ILE ALA ALA GLU HIS ARG ALA ALA VAL
SEQRES 9 A 273 ARG GLU VAL LEU ALA ARG GLU THR ASP LEU GLU ALA ARG
SEQRES 10 A 273 LEU ALA GLY VAL LEU LYS VAL TRP LEU ASP ILE ALA THR
SEQRES 11 A 273 PRO TYR HIS GLU PHE ALA VAL GLN PHE PHE LYS ASN ALA
SEQRES 12 A 273 ALA ASP PRO ASP SER PRO LEU SER PRO PHE SER PRO GLU
SEQRES 13 A 273 SER GLU HIS ALA ARG VAL GLU ALA ILE GLY ILE HIS ARG
SEQRES 14 A 273 ALA VAL LEU ALA GLY ALA LYS THR LYS VAL PRO GLU GLU
SEQRES 15 A 273 LEU ARG ASP ILE LEU PRO GLU LEU MSE TRP LEU SER GLN
SEQRES 16 A 273 MSE GLY LEU VAL LEU TYR TRP ILE PHE ASP ARG THR GLU
SEQRES 17 A 273 GLY ARG GLU ARG SER TYR ARG LEU ALA GLU ARG GLY ALA
SEQRES 18 A 273 ARG LEU THR ALA ARG GLY VAL VAL LEU ALA ARG PHE ARG
SEQRES 19 A 273 VAL LEU ARG PRO LEU VAL ARG GLU VAL HIS GLU LEU PHE
SEQRES 20 A 273 THR ASP PHE LEU PRO GLY MSE THR LYS VAL MSE PRO ASP
SEQRES 21 A 273 PRO ALA LYS LYS PRO THR ARG ASP ALA GLY PRO GLN ALA
SEQRES 1 B 273 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 273 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE PRO ALA THR
SEQRES 3 B 273 ASN ASP GLY PRO ASP ASP GLY ALA HIS LEU SER LYS SER
SEQRES 4 B 273 GLU GLN THR ARG ALA LEU ILE LEU GLU THR ALA MSE ARG
SEQRES 5 B 273 LEU PHE GLN GLU ARG GLY TYR ASP ARG THR THR MSE ARG
SEQRES 6 B 273 ALA ILE ALA GLN GLU ALA GLY VAL SER VAL GLY ASN ALA
SEQRES 7 B 273 TYR TYR TYR PHE ALA GLY LYS GLU HIS LEU ILE GLN GLY
SEQRES 8 B 273 PHE TYR ASP ARG ILE ALA ALA GLU HIS ARG ALA ALA VAL
SEQRES 9 B 273 ARG GLU VAL LEU ALA ARG GLU THR ASP LEU GLU ALA ARG
SEQRES 10 B 273 LEU ALA GLY VAL LEU LYS VAL TRP LEU ASP ILE ALA THR
SEQRES 11 B 273 PRO TYR HIS GLU PHE ALA VAL GLN PHE PHE LYS ASN ALA
SEQRES 12 B 273 ALA ASP PRO ASP SER PRO LEU SER PRO PHE SER PRO GLU
SEQRES 13 B 273 SER GLU HIS ALA ARG VAL GLU ALA ILE GLY ILE HIS ARG
SEQRES 14 B 273 ALA VAL LEU ALA GLY ALA LYS THR LYS VAL PRO GLU GLU
SEQRES 15 B 273 LEU ARG ASP ILE LEU PRO GLU LEU MSE TRP LEU SER GLN
SEQRES 16 B 273 MSE GLY LEU VAL LEU TYR TRP ILE PHE ASP ARG THR GLU
SEQRES 17 B 273 GLY ARG GLU ARG SER TYR ARG LEU ALA GLU ARG GLY ALA
SEQRES 18 B 273 ARG LEU THR ALA ARG GLY VAL VAL LEU ALA ARG PHE ARG
SEQRES 19 B 273 VAL LEU ARG PRO LEU VAL ARG GLU VAL HIS GLU LEU PHE
SEQRES 20 B 273 THR ASP PHE LEU PRO GLY MSE THR LYS VAL MSE PRO ASP
SEQRES 21 B 273 PRO ALA LYS LYS PRO THR ARG ASP ALA GLY PRO GLN ALA
MODRES 3C07 MSE A 29 MET SELENOMETHIONINE
MODRES 3C07 MSE A 42 MET SELENOMETHIONINE
MODRES 3C07 MSE A 169 MET SELENOMETHIONINE
MODRES 3C07 MSE A 174 MET SELENOMETHIONINE
MODRES 3C07 MSE A 232 MET SELENOMETHIONINE
MODRES 3C07 MSE B 29 MET SELENOMETHIONINE
MODRES 3C07 MSE B 42 MET SELENOMETHIONINE
MODRES 3C07 MSE B 169 MET SELENOMETHIONINE
MODRES 3C07 MSE B 174 MET SELENOMETHIONINE
HET MSE A 29 8
HET MSE A 42 8
HET MSE A 169 8
HET MSE A 174 8
HET MSE A 232 8
HET MSE B 29 8
HET MSE B 42 8
HET MSE B 169 8
HET MSE B 174 8
HET SO4 A 252 5
HET SO4 A 253 5
HET SO4 B 252 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 3 SO4 3(O4 S 2-)
HELIX 1 1 SER A 15 ARG A 35 1 21
HELIX 2 2 THR A 41 GLY A 50 1 10
HELIX 3 3 SER A 52 PHE A 60 1 9
HELIX 4 4 GLY A 62 VAL A 82 1 21
HELIX 5 5 GLU A 84 GLU A 89 1 6
HELIX 6 6 ASP A 91 THR A 108 1 18
HELIX 7 7 TYR A 110 ALA A 122 1 13
HELIX 8 8 SER A 132 GLU A 134 5 3
HELIX 9 9 SER A 135 GLY A 152 1 18
HELIX 10 10 PRO A 158 ARG A 162 5 5
HELIX 11 11 ASP A 163 ASP A 183 1 21
HELIX 12 12 ARG A 188 ALA A 209 1 22
HELIX 13 13 LEU A 214 LEU A 229 1 16
HELIX 14 14 LYS B 16 GLY B 36 1 21
HELIX 15 15 THR B 41 GLY B 50 1 10
HELIX 16 16 SER B 52 PHE B 60 1 9
HELIX 17 17 GLY B 62 ARG B 79 1 18
HELIX 18 18 VAL B 82 ARG B 88 1 7
HELIX 19 19 ASP B 91 THR B 108 1 18
HELIX 20 20 TYR B 110 ALA B 122 1 13
HELIX 21 21 SER B 135 GLY B 152 1 18
HELIX 22 22 PRO B 158 ASP B 163 1 6
HELIX 23 23 ILE B 164 ASP B 183 1 20
HELIX 24 24 THR B 185 GLY B 187 5 3
HELIX 25 25 ARG B 188 ARG B 210 1 23
HELIX 26 26 PHE B 211 VAL B 213 5 3
HELIX 27 27 LEU B 214 PHE B 228 1 15
LINK C ALA A 28 N MSE A 29 1555 1555 1.33
LINK C MSE A 29 N ARG A 30 1555 1555 1.33
LINK C THR A 41 N MSE A 42 1555 1555 1.33
LINK C MSE A 42 N ARG A 43 1555 1555 1.32
LINK C LEU A 168 N MSE A 169 1555 1555 1.33
LINK C MSE A 169 N TRP A 170 1555 1555 1.34
LINK C GLN A 173 N MSE A 174 1555 1555 1.33
LINK C MSE A 174 N GLY A 175 1555 1555 1.33
LINK C GLY A 231 N MSE A 232 1555 1555 1.34
LINK C MSE A 232 N THR A 233 1555 1555 1.34
LINK C ALA B 28 N MSE B 29 1555 1555 1.34
LINK C MSE B 29 N ARG B 30 1555 1555 1.34
LINK C THR B 41 N MSE B 42 1555 1555 1.32
LINK C MSE B 42 N ARG B 43 1555 1555 1.32
LINK C LEU B 168 N MSE B 169 1555 1555 1.32
LINK C MSE B 169 N TRP B 170 1555 1555 1.33
LINK C GLN B 173 N MSE B 174 1555 1555 1.34
LINK C MSE B 174 N GLY B 175 1555 1555 1.34
SITE 1 AC1 3 PRO A 158 GLU A 159 GLU A 160
SITE 1 AC2 4 SER A 15 LYS A 16 LYS B 156 ARG B 210
SITE 1 AC3 5 ASP A 227 ARG B 43 ARG B 190 ARG B 193
SITE 2 AC3 5 ARG B 197
CRYST1 74.947 74.947 208.075 90.00 90.00 90.00 P 43 21 2 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 0.013343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
