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PDBsum entry 2nsc

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Chaperone PDB id
2nsc
Jmol
Contents
Protein chain
109 a.a.
Waters ×138
HEADER    CHAPERONE                               03-NOV-06   2NSC
TITLE     STRUCTURES OF AND INTERACTIONS BETWEEN DOMAINS OF TRIGGER FACTOR FROM
TITLE    2 THEMOTOGA MARITIMA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRIGGER FACTOR;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: TF;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE   3 ORGANISM_TAXID: 2336;
SOURCE   4 GENE: TIG;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: CODONPLUS RIL;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS    CHAPERONE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.MARTINEZ-HACKERT,W.A.HENDRICKSON
REVDAT   4   13-JUL-11 2NSC    1       VERSN
REVDAT   3   24-FEB-09 2NSC    1       VERSN
REVDAT   2   20-MAY-08 2NSC    1       JRNL
REVDAT   1   27-MAR-07 2NSC    0
JRNL        AUTH   E.MARTINEZ-HACKERT,W.A.HENDRICKSON
JRNL        TITL   STRUCTURES OF AND INTERACTIONS BETWEEN DOMAINS OF TRIGGER
JRNL        TITL 2 FACTOR FROM THERMOTOGA MARITIMA.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  63   536 2007
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   17372359
JRNL        DOI    10.1107/S090744490700964X
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.62
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 6404
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.195
REMARK   3   FREE R VALUE                     : 0.260
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 297
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) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 424
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020
REMARK   3   BIN FREE R VALUE SET COUNT          : 17
REMARK   3   BIN FREE R VALUE                    : 0.2970
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 898
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 138
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) : 29.98
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.53000
REMARK   3    B22 (A**2) : 0.39000
REMARK   3    B33 (A**2) : 0.14000
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): 0.316
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.239
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.161
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.164
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   909 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1222 ; 1.164 ; 2.002
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   108 ; 4.561 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    46 ;40.705 ;24.348
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   186 ;12.803 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;24.532 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   140 ; 0.073 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   671 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   381 ; 0.217 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   613 ; 0.303 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    76 ; 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):    80 ; 0.182 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.158 ; 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):   568 ; 0.838 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   888 ; 1.290 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   378 ; 2.094 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   334 ; 3.320 ; 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 : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A    21
REMARK   3    RESIDUE RANGE :   A    84        A   109
REMARK   3    ORIGIN FOR THE GROUP (A):  43.8371  -2.5773  21.4033
REMARK   3    T TENSOR
REMARK   3      T11:   0.0048 T22:  -0.0415
REMARK   3      T33:  -0.0089 T12:   0.0279
REMARK   3      T13:   0.0075 T23:  -0.0133
REMARK   3    L TENSOR
REMARK   3      L11:   3.3081 L22:   1.1084
REMARK   3      L33:   0.4767 L12:   1.7604
REMARK   3      L13:   0.2019 L23:  -0.0909
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0082 S12:   0.1043 S13:  -0.0257
REMARK   3      S21:  -0.0618 S22:  -0.0128 S23:  -0.0142
REMARK   3      S31:  -0.0158 S32:  -0.0265 S33:   0.0210
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    22        A    39
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4689 -10.0369  41.7072
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0301 T22:   0.0150
REMARK   3      T33:  -0.0570 T12:   0.0074
REMARK   3      T13:   0.0084 T23:  -0.0414
REMARK   3    L TENSOR
REMARK   3      L11:   2.5856 L22:  17.4845
REMARK   3      L33:   9.3725 L12:  -3.7290
REMARK   3      L13:   2.1101 L23: -11.2177
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1973 S12:  -0.2424 S13:   0.1038
REMARK   3      S21:   0.3702 S22:   0.2575 S23:  -0.0774
REMARK   3      S31:  -0.2764 S32:  -0.0019 S33:  -0.0602
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    40        A    60
REMARK   3    ORIGIN FOR THE GROUP (A):  52.4335 -14.6939  46.1619
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1627 T22:   0.0014
REMARK   3      T33:   0.0508 T12:   0.0702
REMARK   3      T13:  -0.0608 T23:  -0.0030
REMARK   3    L TENSOR
REMARK   3      L11:   2.6722 L22:   8.8326
REMARK   3      L33:  14.3220 L12:  -2.6830
REMARK   3      L13:   3.5226 L23:  -0.3074
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1105 S12:   0.0081 S13:   0.2958
REMARK   3      S21:   0.3967 S22:   0.1394 S23:  -0.5711
REMARK   3      S31:  -0.0290 S32:   0.9912 S33:  -0.0289
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 :   A    61        A    83
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6626  -9.2948  31.2040
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0302 T22:   0.0298
REMARK   3      T33:  -0.0383 T12:  -0.0007
REMARK   3      T13:   0.0202 T23:  -0.0177
REMARK   3    L TENSOR
REMARK   3      L11:  10.9193 L22:   1.8353
REMARK   3      L33:   3.2784 L12:  -3.5689
REMARK   3      L13:   5.7154 L23:  -1.7568
REMARK   3    S TENSOR
REMARK   3      S11:   0.0339 S12:  -0.2196 S13:  -0.1672
REMARK   3      S21:   0.0993 S22:   0.0244 S23:   0.1054
REMARK   3      S31:   0.1886 S32:  -0.2330 S33:  -0.0584
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 2NSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB040243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.50
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) : 0.91994
REMARK 200  MONOCHROMATOR                  : DOUBLE MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6440
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 6.200
REMARK 200  R MERGE                    (I) : 0.04200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 34.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.27600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 7.756
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   (%): 46.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.2M POTASSIUM CHLORIDE,
REMARK 280  0.1M MES, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290       4555   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        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       25.60700
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.93550
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.60700
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.93550
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: STRAND SWAPPED DIMER IS PROBABLY A CONSTRUCT ARTIFACT
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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      102.42800
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PRO A 109    CG   CD
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    LYS A  10     -116.24     65.68
REMARK 500    LYS A  46      109.84    -51.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NSA   RELATED DB: PDB
REMARK 900 C-TERMINAL TRIGGER FACTOR DOMAIN
REMARK 900 RELATED ID: 2NSB   RELATED DB: NDB
REMARK 900 N-TERMINAL TRIGGER FACTOR DOMAIN LOW RESOLUTION
DBREF  2NSC A    1   109  UNP    Q9WZF8   TIG_THEMA        1    109
SEQRES   1 A  109  MET GLU VAL LYS GLU LEU GLU ARG ASP LYS ASN ARG VAL
SEQRES   2 A  109  VAL LEU GLU TYR VAL PHE GLY ALA GLU GLU ILE ALA GLN
SEQRES   3 A  109  ALA GLU ASP LYS ALA VAL ARG TYR LEU ASN GLN ARG VAL
SEQRES   4 A  109  GLU ILE PRO GLY PHE ARG LYS GLY ARG ILE PRO LYS ASN
SEQRES   5 A  109  VAL LEU LYS MET LYS LEU GLY GLU GLU PHE GLN GLU TYR
SEQRES   6 A  109  THR LEU ASP PHE LEU MET ASP LEU ILE PRO ASP THR LEU
SEQRES   7 A  109  LYS ASP ARG LYS LEU ILE LEU SER PRO ILE VAL THR GLU
SEQRES   8 A  109  ARG GLU LEU LYS ASP VAL THR ALA ARG VAL VAL VAL GLU
SEQRES   9 A  109  VAL HIS GLU GLU PRO
FORMUL   2  HOH   *138(H2 O)
HELIX    1   1 GLY A   20  GLN A   37  1                                  18
HELIX    2   2 PRO A   50  GLY A   59  1                                  10
HELIX    3   3 GLU A   61  ASP A   72  1                                  12
HELIX    4   4 LEU A   73  LEU A   78  1                                   6
SHEET    1   A 2 GLU A   2  ASP A   9  0
SHEET    2   A 2 ARG A  12  VAL A  18 -1  O  ARG A  12   N  ASP A   9
CRYST1   51.214   75.871   30.514  90.00  90.00  90.00 P 21 21 2     4
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      0.019526  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013180  0.000000        0.00000
SCALE3      0.000000  0.000000  0.032772        0.00000
      
PROCHECK
Go to PROCHECK summary
 References