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PDBsum entry 1tnf

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Top Page protein Protein-protein interface(s) links
Lymphokine PDB id
1tnf
Jmol
Contents
Protein chains
152 a.a. *
* Residue conservation analysis
HEADER    LYMPHOKINE                              25-AUG-89   1TNF
TITLE     THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT 2.6
TITLE    2 ANGSTROMS RESOLUTION. IMPLICATIONS FOR RECEPTOR BINDING
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR-ALPHA;
COMPND   3 CHAIN: A, B, C;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    LYMPHOKINE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.J.ECK,S.R.SPRANG
REVDAT   4   24-FEB-09 1TNF    1       VERSN
REVDAT   3   01-APR-03 1TNF    1       JRNL
REVDAT   2   15-JAN-91 1TNF    1       REMARK
REVDAT   1   15-JAN-90 1TNF    0
JRNL        AUTH   M.J.ECK,S.R.SPRANG
JRNL        TITL   THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT
JRNL        TITL 2 2.6 A RESOLUTION. IMPLICATIONS FOR RECEPTOR
JRNL        TITL 3 BINDING.
JRNL        REF    J.BIOL.CHEM.                  V. 264 17595 1989
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   2551905
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.J.ECK,B.BEUTLER,G.KUO,J.P.MERRYWEATHER,S.R.SPRANG
REMARK   1  TITL   CRYSTALLIZATION OF TRIMERIC RECOMBINANT HUMAN
REMARK   1  TITL 2 TUMOR NECROSIS FACTOR (CACHECTIN)
REMARK   1  REF    J.BIOL.CHEM.                  V. 263 12816 1988
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.230
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3552
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.015
REMARK   3   BOND ANGLES            (DEGREES) : 4.10
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1TNF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
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       58.50000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.50000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.50000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.25000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.50000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.50000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       87.75000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.50000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.50000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       29.25000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.50000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.50000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       87.75000
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       58.50000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK:
REMARK 300 THE MOLECULE EXISTS AS A TRIMER IN WHICH THE THREE SUBUNITS
REMARK 300 ARE RELATED BY APPROXIMATE THREE-FOLD SYMMETRY.  THE THREE
REMARK 300 SUBUNITS HAVE BEEN ASSIGNED CHAIN INDICATORS A, B, AND C.
REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW
REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED
REMARK 300 TO CHAIN A.  THE TRANSFORMATION PRESENTED ON *MTRIX 2*
REMARK 300 RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN
REMARK 300 C WHEN APPLIED TO CHAIN A.  THE TRANSFORMATION PRESENTED ON
REMARK 300 *MTRIX 3* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES
REMARK 300 FOR CHAIN C WHEN APPLIED TO CHAIN B.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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     VAL A     1
REMARK 465     ARG A     2
REMARK 465     SER A     3
REMARK 465     SER A     4
REMARK 465     SER A     5
REMARK 465     VAL B     1
REMARK 465     ARG B     2
REMARK 465     SER B     3
REMARK 465     SER B     4
REMARK 465     SER B     5
REMARK 465     VAL C     1
REMARK 465     ARG C     2
REMARK 465     SER C     3
REMARK 465     SER C     4
REMARK 465     SER C     5
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     ARG A   6    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B   6    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C   6    CG   CD   NE   CZ   NH1  NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS A  15   NE2   HIS A  15   CD2    -0.078
REMARK 500    HIS A  73   NE2   HIS A  73   CD2    -0.067
REMARK 500    HIS A  78   NE2   HIS A  78   CD2    -0.079
REMARK 500    HIS B  15   NE2   HIS B  15   CD2    -0.077
REMARK 500    HIS B  73   NE2   HIS B  73   CD2    -0.067
REMARK 500    HIS B  78   NE2   HIS B  78   CD2    -0.068
REMARK 500    HIS C  15   NE2   HIS C  15   CD2    -0.076
REMARK 500    HIS C  73   NE2   HIS C  73   CD2    -0.071
REMARK 500    HIS C  78   NE2   HIS C  78   CD2    -0.073
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    TRP A  28   CD1 -  CG  -  CD2 ANGL. DEV. =   7.6 DEGREES
REMARK 500    TRP A  28   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.8 DEGREES
REMARK 500    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES
REMARK 500    LEU A  37   N   -  CA  -  C   ANGL. DEV. = -18.5 DEGREES
REMARK 500    LEU A  43   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
REMARK 500    ARG A  44   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A  44   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    CYS A  69   CA  -  CB  -  SG  ANGL. DEV. = -15.4 DEGREES
REMARK 500    HIS A  73   CA  -  CB  -  CG  ANGL. DEV. = -13.6 DEGREES
REMARK 500    ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A  82   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES
REMARK 500    VAL A  85   CA  -  CB  -  CG2 ANGL. DEV. = -11.3 DEGREES
REMARK 500    TYR A  87   CA  -  CB  -  CG  ANGL. DEV. =  13.0 DEGREES
REMARK 500    CYS A 101   CA  -  CB  -  SG  ANGL. DEV. = -11.3 DEGREES
REMARK 500    GLN A 102   N   -  CA  -  C   ANGL. DEV. = -19.0 DEGREES
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    TRP A 114   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP A 114   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 138   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =   8.1 DEGREES
REMARK 500    THR B   7   N   -  CA  -  CB  ANGL. DEV. = -11.6 DEGREES
REMARK 500    TRP B  28   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP B  28   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    LEU B  29   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES
REMARK 500    SER B  71   CA  -  C   -  N   ANGL. DEV. = -13.9 DEGREES
REMARK 500    ARG B  82   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    GLN B  88   CA  -  CB  -  CG  ANGL. DEV. =  22.2 DEGREES
REMARK 500    ALA B 111   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES
REMARK 500    TRP B 114   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP B 114   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG B 131   NE  -  CZ  -  NH2 ANGL. DEV. =   5.2 DEGREES
REMARK 500    ARG B 138   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG B 138   NE  -  CZ  -  NH2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    TYR B 151   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    ASP C  10   CA  -  C   -  N   ANGL. DEV. = -14.5 DEGREES
REMARK 500    TRP C  28   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES
REMARK 500    TRP C  28   CB  -  CG  -  CD1 ANGL. DEV. =  -7.8 DEGREES
REMARK 500    TRP C  28   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES
REMARK 500    TRP C  28   CG  -  CD2 -  CE3 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG C  32   NE  -  CZ  -  NH2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ALA C  38   CA  -  C   -  N   ANGL. DEV. = -14.9 DEGREES
REMARK 500    ALA C  38   O   -  C   -  N   ANGL. DEV. =  10.2 DEGREES
REMARK 500    ARG C  44   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG C  44   CA  -  C   -  N   ANGL. DEV. =  16.0 DEGREES
REMARK 500    ARG C  82   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES
REMARK 500    TYR C  87   CA  -  CB  -  CG  ANGL. DEV. =  11.7 DEGREES
REMARK 500    TYR C  87   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    TYR C  87   N   -  CA  -  C   ANGL. DEV. = -18.8 DEGREES
REMARK 500    GLN C  88   CA  -  CB  -  CG  ANGL. DEV. = -14.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      58 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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    SER A   9      154.98     58.28
REMARK 500    ASP A  10       55.79    -90.64
REMARK 500    ALA A  22       98.18   -165.86
REMARK 500    ASN A  30     -133.94   -127.53
REMARK 500    ARG A  31      -33.09     60.04
REMARK 500    ARG A  32     -163.66    -65.01
REMARK 500    ALA A  35       78.59   -116.21
REMARK 500    ALA A  38     -131.11   -116.98
REMARK 500    ASN A  39       77.03    -65.69
REMARK 500    ARG A  44     -107.79   -124.84
REMARK 500    PRO A  70     -126.62    -87.44
REMARK 500    THR A  72      -60.61     31.06
REMARK 500    LEU A  75      103.22     55.43
REMARK 500    SER A  86      -60.69   -123.03
REMARK 500    PRO A 100     -110.81    -68.93
REMARK 500    ARG A 103      172.65     59.19
REMARK 500    GLU A 104      -58.23    143.33
REMARK 500    GLU A 107      -31.40     18.65
REMARK 500    GLU A 110      -87.20    -67.71
REMARK 500    GLN A 149      -73.58   -141.29
REMARK 500    ILE A 155      121.56   -174.04
REMARK 500    PRO B   8      -78.54    -50.97
REMARK 500    SER B   9      146.20    167.72
REMARK 500    ASP B  10       64.27   -103.98
REMARK 500    HIS B  15       77.63   -153.63
REMARK 500    GLN B  21       26.68    -73.04
REMARK 500    ASN B  30     -166.03   -107.29
REMARK 500    ASN B  34       42.98   -148.92
REMARK 500    LEU B  37       96.98    174.36
REMARK 500    ARG B  44      -91.17    -99.22
REMARK 500    ASP B  45       55.54    -93.50
REMARK 500    SER B  60      130.97   -171.65
REMARK 500    THR B  72     -123.74     47.18
REMARK 500    LEU B  75      109.50     52.56
REMARK 500    ALA B  84     -151.23    -49.81
REMARK 500    VAL B  85      -31.99   -140.06
REMARK 500    SER B  86     -102.29    -87.76
REMARK 500    GLN B  88       63.62    -57.32
REMARK 500    ARG B 103      163.73     61.78
REMARK 500    GLU B 104      -50.73    153.78
REMARK 500    PRO B 106       87.78    -67.85
REMARK 500    GLU B 107      -71.30    -56.25
REMARK 500    ALA B 109      -48.37   -148.90
REMARK 500    GLU B 110      -26.84     73.32
REMARK 500    ALA B 111      160.41     73.81
REMARK 500    ALA B 145       45.13    -93.71
REMARK 500    SER B 147      -78.36   -112.27
REMARK 500    GLN B 149      -26.37   -144.57
REMARK 500    PRO C   8     -169.31    -72.71
REMARK 500    SER C   9       75.82     53.10
REMARK 500    PRO C  12      127.54    -37.13
REMARK 500    ALA C  18     -164.34    -76.91
REMARK 500    PRO C  20       38.76    -80.12
REMARK 500    GLU C  23      -40.52    -14.82
REMARK 500    GLN C  25      -56.97   -155.27
REMARK 500    LEU C  26       58.28     88.63
REMARK 500    ARG C  31      -27.14    115.06
REMARK 500    ARG C  32      151.06    -43.68
REMARK 500    ALA C  33      -53.20    -16.54
REMARK 500    ASN C  39       76.83     33.42
REMARK 500    ARG C  44     -113.93   -121.98
REMARK 500    PRO C  51     -147.38    -83.35
REMARK 500    SER C  52      -90.56     36.91
REMARK 500    GLU C  53      158.88    136.41
REMARK 500    THR C  72      150.01     72.41
REMARK 500    LEU C  75       95.80     34.05
REMARK 500    SER C  86     -100.31    -93.20
REMARK 500    GLN C  88     -166.00    -69.95
REMARK 500    THR C  89      165.30     84.36
REMARK 500    GLU C 104      -48.98   -137.67
REMARK 500    PRO C 106       70.52    -20.35
REMARK 500    GLU C 107      -85.93    -90.44
REMARK 500    GLU C 110      128.42    -32.37
REMARK 500    ALA C 111       84.81     20.53
REMARK 500    LYS C 128      110.41    -38.55
REMARK 500    TYR C 141       30.61    -84.03
REMARK 500    ALA C 145       58.55   -172.39
REMARK 500    SER C 147      -78.19   -163.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 THR A    7     PRO A    8                  117.21
REMARK 500 THR A  105     PRO A  106                  -99.71
REMARK 500 THR B    7     PRO B    8                  144.02
REMARK 500 THR B  105     PRO B  106                 -142.83
REMARK 500 THR C    7     PRO C    8                   51.13
REMARK 500 LYS C   11     PRO C   12                  135.94
REMARK 500 GLU C  146     SER C  147                  141.65
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1TNF A    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  1TNF B    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  1TNF C    1   157  UNP    P01375   TNFA_HUMAN      77    233
SEQADV 1TNF ASP A   45  UNP  P01375    LEU   219 CONFLICT
SEQADV 1TNF ASP B   45  UNP  P01375    LEU   219 CONFLICT
SEQADV 1TNF ASP C   45  UNP  P01375    LEU   219 CONFLICT
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES   2 A  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 A  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 A  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 A  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES   6 A  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 A  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES  11 A  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES  12 A  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 A  157  LEU
SEQRES   1 B  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES   2 B  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 B  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 B  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 B  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES   6 B  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 B  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL
SEQRES   8 B  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES   9 B  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES  10 B  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES  11 B  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES  12 B  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 B  157  LEU
SEQRES   1 C  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES   2 C  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 C  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 C  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 C  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES   6 C  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 C  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES  11 C  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 C  157  LEU
HELIX    1 H1A ARG A  138  LEU A  142  5                                   5
HELIX    2 H1B ARG B  138  LEU B  142  5                                   5
HELIX    3 H1C ARG C  138  LEU C  142  5                                   5
SHEET    1 S1A 5 LEU A  36  ALA A  38  0
SHEET    2 S1A 5 PRO A  12  ALA A  18 -1  N  HIS A  15   O  LEU A  36
SHEET    3 S1A 5 VAL A 150  LEU A 157 -1  O  VAL A 150   N  ALA A  18
SHEET    4 S1A 5 GLY A  54  GLY A  68 -1  O  GLN A  61   N  TYR A 151
SHEET    5 S1A 5 LYS A 112  LEU A 126 -1  N  LEU A 126   O  GLY A  54
SHEET    1 S2A 5 GLU A  42  ARG A  44  0
SHEET    2 S2A 5 GLN A  47  VAL A  50 -1  O  GLN A  47   N  ARG A  44
SHEET    3 S2A 5 GLY A 129  ILE A 136 -1  N  GLY A 129   O  VAL A  50
SHEET    4 S2A 5 LEU A  76  ALA A  84 -1  N  THR A  79   O  GLU A 135
SHEET    5 S2A 5 GLN A  88  LYS A  98 -1  N  VAL A  91   O  ARG A  82
SHEET    1 S1B 5 LEU B  36  ALA B  38  0
SHEET    2 S1B 5 PRO B  12  ALA B  18 -1  N  HIS B  15   O  LEU B  36
SHEET    3 S1B 5 VAL B 150  LEU B 157 -1  O  VAL B 150   N  ALA B  18
SHEET    4 S1B 5 GLY B  54  GLY B  68 -1  O  GLN B  61   N  TYR B 151
SHEET    5 S1B 5 LYS B 112  LEU B 126 -1  N  LEU B 126   O  GLY B  54
SHEET    1 S2B 5 GLU B  42  ARG B  44  0
SHEET    2 S2B 5 GLN B  47  VAL B  50 -1  O  GLN B  47   N  ARG B  44
SHEET    3 S2B 5 GLY B 129  ILE B 136 -1  N  GLY B 129   O  VAL B  50
SHEET    4 S2B 5 LEU B  76  ALA B  84 -1  N  THR B  79   O  GLU B 135
SHEET    5 S2B 5 GLN B  88  LYS B  98 -1  N  VAL B  91   O  ARG B  82
SHEET    1 S1C 5 LEU C  36  ALA C  38  0
SHEET    2 S1C 5 PRO C  12  ALA C  18 -1  N  HIS C  15   O  LEU C  36
SHEET    3 S1C 5 VAL C 150  LEU C 157 -1  O  VAL C 150   N  ALA C  18
SHEET    4 S1C 5 GLY C  54  GLY C  68 -1  O  GLN C  61   N  TYR C 151
SHEET    5 S1C 5 LYS C 112  LEU C 126 -1  N  LEU C 126   O  GLY C  54
SHEET    1 S2C 5 GLU C  42  ARG C  44  0
SHEET    2 S2C 5 GLN C  47  VAL C  50 -1  O  GLN C  47   N  ARG C  44
SHEET    3 S2C 5 GLY C 129  ILE C 136 -1  N  GLY C 129   O  VAL C  50
SHEET    4 S2C 5 LEU C  76  ALA C  84 -1  N  THR C  79   O  GLU C 135
SHEET    5 S2C 5 GLN C  88  LYS C  98 -1  N  VAL C  91   O  ARG C  82
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  1.99
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.03
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.02
CRYST1   95.000   95.000  117.000  90.00  90.00  90.00 P 41 21 2    24
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      0.010526  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010526  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008547        0.00000
MTRIX1   1  0.040460 -0.105750  0.993570      -16.17000    1
MTRIX2   1 -0.980650  0.186430  0.059780       57.43000    1
MTRIX3   1 -0.191550 -0.976760 -0.096160       96.33000    1
MTRIX1   2 -0.028960 -0.992710 -0.116990       74.40000    1
MTRIX2   2 -0.202020  0.120440 -0.971950       87.33000    1
MTRIX3   2  0.978950 -0.004510 -0.204040       28.89000    1
MTRIX1   3 -0.012020 -0.163460  0.986460      -11.46000    1
MTRIX2   3 -0.986560  0.162730  0.014940       60.62000    1
MTRIX3   3 -0.162970 -0.973040 -0.163220       97.89000    1
      
PROCHECK
Go to PROCHECK summary
 References