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PDBsum entry 3gu0

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Chaperone PDB id
3gu0
Jmol
Contents
Protein chain
406 a.a.
HEADER    CHAPERONE                               28-MAR-09   3GU0
TITLE     PROMISCUOUS SUBSTRATE RECOGNITION IN FOLDING AND ASSEMBLY ACTIVITIES
TITLE    2 OF THE TRIGGER FACTOR CHAPERONE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRIGGER FACTOR;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 1-405;
COMPND   5 SYNONYM: TF;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE   3 ORGANISM_TAXID: 2336;
SOURCE   4 GENE: TIG, TM_0694;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS    MOLECULAR CHAPERONE, CELL CYCLE, CELL DIVISION, CHAPERONE, ISOMERASE,
KEYWDS   2 ROTAMASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.MARTINEZ-HACKERT,W.A.HENDRICKSON
REVDAT   2   13-JUL-11 3GU0    1       VERSN
REVDAT   1   22-DEC-09 3GU0    0
JRNL        AUTH   E.MARTINEZ-HACKERT,W.A.HENDRICKSON
JRNL        TITL   PROMISCUOUS SUBSTRATE RECOGNITION IN FOLDING AND ASSEMBLY
JRNL        TITL 2 ACTIVITIES OF THE TRIGGER FACTOR CHAPERONE
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 138   923 2009
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   19737520
JRNL        DOI    10.1016/J.CELL.2009.07.044
REMARK   2
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.0
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) : 3.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 6111
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) : 0.250
REMARK   3   R VALUE            (WORKING SET) : 0.244
REMARK   3   FREE R VALUE                     : 0.358
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 288
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) : 3.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.58
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 396
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170
REMARK   3   BIN FREE R VALUE SET COUNT          : 22
REMARK   3   BIN FREE R VALUE                    : 0.3760
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3368
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
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) : 57.93
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.51000
REMARK   3    B22 (A**2) : -0.15000
REMARK   3    B33 (A**2) : -1.36000
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): 0.970
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.850
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 125.046
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.901
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.705
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3408 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4572 ; 1.226 ; 2.007
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   405 ; 5.744 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   181 ;40.899 ;25.028
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   722 ;21.866 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;17.416 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   508 ; 0.072 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2524 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1698 ; 0.236 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2252 ; 0.303 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   136 ; 0.184 ; 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):    95 ; 0.200 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.198 ; 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):  2098 ; 0.386 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3293 ; 0.705 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1453 ; 0.613 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1279 ; 1.119 ; 4.500
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     1        A   112
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0200 -11.5850 -26.8480
REMARK   3    T TENSOR
REMARK   3      T11:   0.4231 T22:   0.4362
REMARK   3      T33:   0.1270 T12:  -0.1828
REMARK   3      T13:  -0.0802 T23:   0.0527
REMARK   3    L TENSOR
REMARK   3      L11:   0.0193 L22:   0.6882
REMARK   3      L33:   2.1375 L12:   0.1152
REMARK   3      L13:  -0.2030 L23:  -1.2128
REMARK   3    S TENSOR
REMARK   3      S11:   0.2827 S12:   0.0709 S13:   0.0176
REMARK   3      S21:  -0.1276 S22:  -0.0938 S23:  -0.1483
REMARK   3      S31:   0.4738 S32:   0.0696 S33:  -0.1889
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   113        A   125
REMARK   3    RESIDUE RANGE :   A   270        A   406
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9450 -33.1760   2.1450
REMARK   3    T TENSOR
REMARK   3      T11:   0.0797 T22:   0.4343
REMARK   3      T33:   0.1076 T12:  -0.0905
REMARK   3      T13:   0.0167 T23:  -0.0343
REMARK   3    L TENSOR
REMARK   3      L11:   0.4405 L22:   2.4870
REMARK   3      L33:   1.8774 L12:   0.7938
REMARK   3      L13:  -0.1930 L23:   0.5777
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0275 S12:  -0.0383 S13:   0.0244
REMARK   3      S21:  -0.0271 S22:   0.0014 S23:  -0.0473
REMARK   3      S31:   0.2441 S32:  -0.1463 S33:   0.0262
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 :   A   146        A   225
REMARK   3    ORIGIN FOR THE GROUP (A): -39.1940 -71.3390  15.8120
REMARK   3    T TENSOR
REMARK   3      T11:   0.0447 T22:   0.3168
REMARK   3      T33:   0.1863 T12:  -0.0750
REMARK   3      T13:   0.0152 T23:  -0.0274
REMARK   3    L TENSOR
REMARK   3      L11:   5.9783 L22:   2.5525
REMARK   3      L33:   5.2295 L12:  -0.7558
REMARK   3      L13:   2.7125 L23:  -2.5316
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0554 S12:  -0.1666 S13:  -0.1122
REMARK   3      S21:  -0.2807 S22:  -0.1690 S23:  -0.2933
REMARK   3      S31:   0.0254 S32:  -0.0829 S33:   0.2245
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   126        A   145
REMARK   3    RESIDUE RANGE :   A   226        A   269
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9230 -63.9630  24.2280
REMARK   3    T TENSOR
REMARK   3      T11:   0.1097 T22:   0.4455
REMARK   3      T33:   0.2009 T12:  -0.0546
REMARK   3      T13:  -0.0702 T23:   0.0079
REMARK   3    L TENSOR
REMARK   3      L11:   0.4188 L22:   7.8104
REMARK   3      L33:   2.8076 L12:  -0.1146
REMARK   3      L13:   0.9788 L23:  -2.2795
REMARK   3    S TENSOR
REMARK   3      S11:   0.0489 S12:  -0.4607 S13:  -0.0733
REMARK   3      S21:  -0.1676 S22:   0.0413 S23:  -0.4313
REMARK   3      S31:  -0.1878 S32:  -0.4224 S33:  -0.0902
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 3GU0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB052304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-OCT-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97903
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIFDAT
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6747
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.08100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.4920
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.57
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.32100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-15% PEG4000, 200 MGCL2, 100 TRIS,
REMARK 280  PH 8.0, 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       47.27900
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       47.27900
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       47.69350
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.24350
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.69350
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.24350
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       47.27900
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.69350
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.24350
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       47.27900
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.69350
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.24350
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 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 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   407
REMARK 465     HIS A   408
REMARK 465     HIS A   409
REMARK 465     HIS A   410
REMARK 465     HIS A   411
REMARK 465     HIS A   412
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   5       96.15    -58.58
REMARK 500    LYS A  10     -108.58     54.88
REMARK 500    ASN A  11       68.35   -107.06
REMARK 500    ARG A  12       97.60   -178.98
REMARK 500    PRO A  42      145.14    -33.89
REMARK 500    LYS A  46       94.87    -55.42
REMARK 500    ARG A  48       61.06   -102.92
REMARK 500    ASP A  76       40.47    -80.79
REMARK 500    THR A  77      -36.39   -149.63
REMARK 500    LEU A  78       48.84   -103.09
REMARK 500    THR A  98      137.51   -176.06
REMARK 500    VAL A 121     -138.46    -99.25
REMARK 500    GLU A 122       68.78   -166.20
REMARK 500    ASP A 125       94.46    -65.28
REMARK 500    GLU A 143      -73.27    -55.97
REMARK 500    SER A 144        5.60    -60.89
REMARK 500    PRO A 154     -138.71    -94.01
REMARK 500    GLU A 156     -131.05    -99.11
REMARK 500    SER A 185     -159.12   -143.96
REMARK 500    PHE A 192       16.61     46.90
REMARK 500    LEU A 196       20.90    169.21
REMARK 500    GLU A 212      -64.30     52.30
REMARK 500    ILE A 233       94.32    -48.12
REMARK 500    ASN A 243     -157.93    -85.12
REMARK 500    GLU A 244      -95.02     64.74
REMARK 500    LYS A 252      -73.26    -57.10
REMARK 500    GLU A 253      -17.75    -46.19
REMARK 500    LYS A 256      -32.14    -36.67
REMARK 500    LYS A 257       28.61   -142.60
REMARK 500    ARG A 308       41.45    -70.60
REMARK 500    TYR A 309      -64.96   -102.25
REMARK 500    SER A 315       29.80   -167.14
REMARK 500    TYR A 316      -82.49   -127.83
REMARK 500    GLU A 317      -56.27   -145.34
REMARK 500    SER A 318     -134.36   -144.75
REMARK 500    GLU A 319      -56.35   -121.89
REMARK 500    LYS A 335      -70.75    -68.42
REMARK 500    LEU A 343      -29.59    -39.26
REMARK 500    ALA A 380      -72.36    -72.28
REMARK 500    ASP A 383      -31.00    -32.29
REMARK 500    GLN A 403       30.57    -71.39
REMARK 500    GLU A 404        7.81   -151.30
REMARK 500    VAL A 405       86.28    -67.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NSC   RELATED DB: PDB
REMARK 900 T MARITIMA TF N-TERMINAL DOMAIN
REMARK 900 RELATED ID: 2NSB   RELATED DB: PDB
REMARK 900 T MARITIMA TF N-TERMINAL DOMAIN
REMARK 900 RELATED ID: 2NSA   RELATED DB: PDB
REMARK 900 T MARITIMA TF C-TERMINAL DOMAIN FRAGMENT
REMARK 900 RELATED ID: 3GTY   RELATED DB: PDB
DBREF  3GU0 A    1   405  UNP    Q9WZF8   TIG_THEMA        1    405
SEQADV 3GU0 GLU A  406  UNP  Q9WZF8              EXPRESSION TAG
SEQADV 3GU0 HIS A  407  UNP  Q9WZF8              EXPRESSION TAG
SEQADV 3GU0 HIS A  408  UNP  Q9WZF8              EXPRESSION TAG
SEQADV 3GU0 HIS A  409  UNP  Q9WZF8              EXPRESSION TAG
SEQADV 3GU0 HIS A  410  UNP  Q9WZF8              EXPRESSION TAG
SEQADV 3GU0 HIS A  411  UNP  Q9WZF8              EXPRESSION TAG
SEQADV 3GU0 HIS A  412  UNP  Q9WZF8              EXPRESSION TAG
SEQRES   1 A  412  MET GLU VAL LYS GLU LEU GLU ARG ASP LYS ASN ARG VAL
SEQRES   2 A  412  VAL LEU GLU TYR VAL PHE GLY ALA GLU GLU ILE ALA GLN
SEQRES   3 A  412  ALA GLU ASP LYS ALA VAL ARG TYR LEU ASN GLN ARG VAL
SEQRES   4 A  412  GLU ILE PRO GLY PHE ARG LYS GLY ARG ILE PRO LYS ASN
SEQRES   5 A  412  VAL LEU LYS MET LYS LEU GLY GLU GLU PHE GLN GLU TYR
SEQRES   6 A  412  THR LEU ASP PHE LEU MET ASP LEU ILE PRO ASP THR LEU
SEQRES   7 A  412  LYS ASP ARG LYS LEU ILE LEU SER PRO ILE VAL THR GLU
SEQRES   8 A  412  ARG GLU LEU LYS ASP VAL THR ALA ARG VAL VAL VAL GLU
SEQRES   9 A  412  VAL HIS GLU GLU PRO GLU VAL ARG ILE GLY ASP ILE SER
SEQRES  10 A  412  LYS ILE GLU VAL GLU LYS VAL ASP GLU GLU LYS VAL LEU
SEQRES  11 A  412  GLU LYS TYR VAL GLU ARG ARG ILE GLU ASP LEU ARG GLU
SEQRES  12 A  412  SER HIS ALA LEU LEU GLU PRO LYS GLU GLY PRO ALA GLU
SEQRES  13 A  412  ALA GLY ASP LEU VAL ARG VAL ASN MET GLU VAL TYR ASN
SEQRES  14 A  412  GLU GLU GLY LYS LYS LEU THR SER ARG GLU TYR GLU TYR
SEQRES  15 A  412  VAL ILE SER GLU ASP GLU ASP ARG PRO PHE VAL LYS ASP
SEQRES  16 A  412  LEU VAL GLY LYS LYS LYS GLY ASP VAL VAL GLU ILE GLU
SEQRES  17 A  412  ARG GLU TYR GLU GLY LYS LYS TYR THR TYR LYS LEU GLU
SEQRES  18 A  412  VAL GLU GLU VAL TYR LYS ARG THR LEU PRO GLU ILE GLY
SEQRES  19 A  412  ASP GLU LEU ALA LYS SER VAL ASN ASN GLU PHE GLU THR
SEQRES  20 A  412  LEU GLU GLN LEU LYS GLU SER LEU LYS LYS GLU GLY LYS
SEQRES  21 A  412  GLU ILE TYR ASP VAL GLU MET LYS GLU SER MET ARG GLU
SEQRES  22 A  412  GLN LEU LEU GLU LYS LEU PRO GLU ILE VAL GLU ILE GLU
SEQRES  23 A  412  ILE SER ASP ARG THR LEU GLU ILE LEU VAL ASN GLU ALA
SEQRES  24 A  412  ILE ASN ARG LEU LYS ARG GLU GLY ARG TYR GLU GLN ILE
SEQRES  25 A  412  VAL SER SER TYR GLU SER GLU GLU LYS PHE ARG GLU GLU
SEQRES  26 A  412  LEU LYS GLU ARG ILE LEU ASP ASP ILE LYS ARG ASP ARG
SEQRES  27 A  412  VAL ILE GLU VAL LEU ALA GLN GLU LYS GLY ILE SER VAL
SEQRES  28 A  412  ASN ASP GLU GLU LEU GLU LYS GLU ALA GLU GLU LEU ALA
SEQRES  29 A  412  PRO PHE TRP GLY ILE SER PRO ASP ARG ALA LYS SER LEU
SEQRES  30 A  412  VAL LYS ALA ARG GLN ASP LEU ARG GLU GLU LEU ARG TRP
SEQRES  31 A  412  ALA ILE LEU LYS ARG LYS VAL LEU ASP LEU LEU LEU GLN
SEQRES  32 A  412  GLU VAL GLU HIS HIS HIS HIS HIS HIS
HELIX    1   1 GLY A   20  ASP A   29  1                                  10
HELIX    2   2 ALA A   31  GLN A   37  1                                   7
HELIX    3   3 PRO A   50  GLY A   59  1                                  10
HELIX    4   4 GLY A   59  ASP A   72  1                                  14
HELIX    5   5 ASP A  125  SER A  144  1                                  20
HELIX    6   6 GLU A  236  VAL A  241  5                                   6
HELIX    7   7 LEU A  248  LYS A  256  1                                   9
HELIX    8   8 GLY A  259  LEU A  279  1                                  21
HELIX    9   9 SER A  288  GLY A  307  1                                  20
HELIX   10  10 ILE A  312  TYR A  316  5                                   5
HELIX   11  11 GLU A  319  GLU A  346  1                                  28
HELIX   12  12 ASN A  352  ALA A  364  1                                  13
HELIX   13  13 PRO A  365  TRP A  367  5                                   3
HELIX   14  14 SER A  370  ARG A  381  1                                  12
HELIX   15  15 ARG A  381  LEU A  402  1                                  22
HELIX   16  16 GLN A  403  VAL A  405  5                                   3
SHEET    1   A 4 GLU A   2  ARG A   8  0
SHEET    2   A 4 VAL A  13  PHE A  19 -1  O  VAL A  14   N  GLU A   7
SHEET    3   A 4 THR A  98  GLU A 107 -1  O  VAL A 105   N  VAL A  13
SHEET    4   A 4 LEU A  83  LYS A  95 -1  N  GLU A  93   O  ARG A 100
SHEET    1   B 2 VAL A 111  ILE A 113  0
SHEET    2   B 2 VAL A 283  ILE A 285 -1  O  GLU A 284   N  ARG A 112
SHEET    1   C 4 LYS A 174  VAL A 183  0
SHEET    2   C 4 ASP A 159  TYR A 168 -1  N  VAL A 167   O  LEU A 175
SHEET    3   C 4 LYS A 215  LYS A 227 -1  O  GLU A 221   N  ASN A 164
SHEET    4   C 4 VAL A 204  GLU A 210 -1  N  VAL A 205   O  LEU A 220
CRYST1   95.387  114.487   94.558  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      0.010484  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008735  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010576        0.00000
      
PROCHECK
Go to PROCHECK summary
 References