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PDBsum entry 1a8m

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Top Page protein Protein-protein interface(s) links
Lymphokine PDB id
1a8m
Jmol
Contents
Protein chains
152 a.a. *
Waters ×69
* Residue conservation analysis
HEADER    LYMPHOKINE                              27-MAR-98   1A8M
TITLE     TUMOR NECROSIS FACTOR ALPHA, R31D MUTANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR ALPHA;
COMPND   3 CHAIN: A, B, C;
COMPND   4 SYNONYM: TNF-ALPHA;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    LYMPHOKINE, CYTOKINE, CYTOTOXIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.REED,Z.-Q.FU,J.WU,Y.-N.XUE,R.W.HARRISON,M.-J.CHEN,
AUTHOR   2 I.T.WEBER
REVDAT   2   24-FEB-09 1A8M    1       VERSN
REVDAT   1   17-JUN-98 1A8M    0
JRNL        AUTH   C.REED,Z.Q.FU,J.WU,Y.N.XUE,R.W.HARRISON,M.J.CHEN,
JRNL        AUTH 2 I.T.WEBER
JRNL        TITL   CRYSTAL STRUCTURE OF TNF-ALPHA MUTANT R31D WITH
JRNL        TITL 2 GREATER AFFINITY FOR RECEPTOR R1 COMPARED WITH R2.
JRNL        REF    PROTEIN ENG.                  V.  10  1101 1997
JRNL        REFN                   ISSN 0269-2139
JRNL        PMID   9488135
JRNL        DOI    10.1093/PROTEIN/10.10.1101
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   Z.Q.FU,R.W.HARRISON,C.REED,J.WU,Y.N.XUE,M.J.CHEN,
REMARK   1  AUTH 2 I.T.WEBER
REMARK   1  TITL   MODEL COMPLEXES OF TUMOR NECROSIS FACTOR-ALPHA
REMARK   1  TITL 2 WITH RECEPTORS R1 AND R2
REMARK   1  REF    PROTEIN ENG.                  V.   8  1233 1995
REMARK   1  REFN                   ISSN 0269-2139
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.3
REMARK   3   NUMBER OF REFLECTIONS             : 21396
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 SET) : 0.218
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1171
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            : 4347
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 69
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.00
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) : 0.013
REMARK   3   BOND ANGLES            (DEGREES) : 2.30
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1A8M 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        : JUL-94
REMARK 200  TEMPERATURE           (KELVIN) : 290
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200  DATA SCALING SOFTWARE          : PROCESS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21396
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 4.000
REMARK 200  R MERGE                    (I) : 0.07800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40
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         : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1TNF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZED FROM 88% MGSO4, 1-2%
REMARK 280  PEG 400, 0.2 M MES, PH 5.5.
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       58.70000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.35000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.35000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.35000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.35000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.35000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       88.05000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.35000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.35000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       29.35000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.35000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.35000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       88.05000
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       58.70000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NH2  ARG B   131     O    HOH A   212     4454     1.82
REMARK 500   NE2  GLN A    88     O    ASP B    31     8665     1.90
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    LEU A 157   CA  -  CB  -  CG  ANGL. DEV. =  17.8 DEGREES
REMARK 500    PHE B 144   N   -  CA  -  C   ANGL. DEV. =  21.9 DEGREES
REMARK 500    SER B 147   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES
REMARK 500    LEU C  37   N   -  CA  -  C   ANGL. DEV. = -17.5 DEGREES
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      145.47     47.91
REMARK 500    HIS A  15       82.11   -172.50
REMARK 500    PRO A  20       37.07    -77.03
REMARK 500    ALA A  33     -136.42     49.00
REMARK 500    ASN A  34       41.31   -109.91
REMARK 500    ALA A  35       74.47    -61.82
REMARK 500    LEU A  37       61.83   -162.59
REMARK 500    ALA A  38     -159.43    -72.06
REMARK 500    ASN A  39       68.33    -27.60
REMARK 500    ARG A  44     -104.87   -111.60
REMARK 500    ASP A  45       42.80    -81.50
REMARK 500    ASN A  46       28.74     84.43
REMARK 500    GLU A  53      173.99    -56.99
REMARK 500    PRO A  70     -118.76    -89.23
REMARK 500    THR A  72      -29.97    -16.01
REMARK 500    LEU A  75       81.07     68.37
REMARK 500    CYS A 101       90.48     64.72
REMARK 500    ARG A 103      -83.08     61.39
REMARK 500    GLU A 104      -90.22     47.75
REMARK 500    THR A 105       67.88     61.22
REMARK 500    ALA A 109       49.61   -102.35
REMARK 500    LEU A 120      147.04    169.47
REMARK 500    PHE A 144       -0.36   -140.02
REMARK 500    SER A 147      -82.34    -90.56
REMARK 500    GLN A 149      -76.49   -125.59
REMARK 500    PHE A 152      120.25   -175.71
REMARK 500    PRO B   8       30.73    -76.32
REMARK 500    SER B   9     -160.71     48.08
REMARK 500    ALA B  14      129.44    179.53
REMARK 500    ASP B  31       22.33    162.25
REMARK 500    LEU B  37       70.05   -166.04
REMARK 500    ARG B  44      -96.07   -103.89
REMARK 500    THR B  72      111.11     63.62
REMARK 500    SER B  86      -77.44    -65.98
REMARK 500    LEU B  93      -92.09    -81.63
REMARK 500    ALA B  96      140.13   -172.26
REMARK 500    GLN B 102      -50.46   -129.93
REMARK 500    ARG B 103      161.84    -31.01
REMARK 500    THR B 105       95.25     80.71
REMARK 500    PRO B 106      153.96     -1.74
REMARK 500    GLU B 107      -92.08   -158.78
REMARK 500    ALA B 109      119.31   -169.29
REMARK 500    GLU B 110     -168.24    -73.93
REMARK 500    ALA B 111     -139.21     49.74
REMARK 500    LYS B 112       96.21     73.94
REMARK 500    SER B 133      117.83   -171.18
REMARK 500    PHE B 144       45.64   -154.12
REMARK 500    ALA B 145       48.39    -93.56
REMARK 500    GLU B 146      -95.77    -74.54
REMARK 500    SER B 147       94.39     79.66
REMARK 500    SER C   9      115.62     52.80
REMARK 500    ASP C  10     -137.06    -87.99
REMARK 500    LYS C  11      132.53     77.60
REMARK 500    PRO C  20      -87.14    -59.03
REMARK 500    GLN C  21       84.18    -53.57
REMARK 500    ALA C  22       63.73   -165.92
REMARK 500    GLU C  23      109.68    -30.23
REMARK 500    GLN C  25      -30.06   -136.24
REMARK 500    LEU C  26       78.29     61.66
REMARK 500    ASP C  31      -39.42     95.20
REMARK 500    ARG C  32      177.34    -55.96
REMARK 500    ALA C  33     -112.02     15.17
REMARK 500    LEU C  37      119.19   -167.05
REMARK 500    VAL C  41       62.84   -110.30
REMARK 500    GLU C  42      152.08    -47.00
REMARK 500    SER C  52      144.84     88.69
REMARK 500    SER C  60      148.52   -173.20
REMARK 500    SER C  71       47.27   -101.51
REMARK 500    THR C  72       22.42   -144.79
REMARK 500    HIS C  73       99.82     47.78
REMARK 500    SER C  86      -89.51    -70.40
REMARK 500    GLN C  88      -19.78     64.15
REMARK 500    ARG C 103      107.00     34.19
REMARK 500    GLU C 104      -58.01   -124.10
REMARK 500    THR C 105       96.78     64.66
REMARK 500    PRO C 106      109.06    -54.25
REMARK 500    ALA C 111      177.14     97.01
REMARK 500    LYS C 112      108.26    136.15
REMARK 500    LYS C 128      109.96    -33.25
REMARK 500    ARG C 138       75.89   -113.71
REMARK 500    TYR C 141       54.05   -110.30
REMARK 500    GLU C 146       92.26     19.38
REMARK 500    SER C 147      -75.67    -93.86
REMARK 500    ILE C 155      135.87   -175.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 200        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH B 215        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH C 231        DISTANCE =  6.64 ANGSTROMS
REMARK 525    HOH C 232        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH B 221        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH C 239        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH C 241        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH B 227        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH B 251        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH B 252        DISTANCE =  8.20 ANGSTROMS
DBREF  1A8M A    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  1A8M B    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  1A8M C    1   157  UNP    P01375   TNFA_HUMAN      77    233
SEQADV 1A8M ASP A   31  UNP  P01375    ARG   107 ENGINEERED
SEQADV 1A8M ASP B   31  UNP  P01375    ARG   107 ENGINEERED
SEQADV 1A8M ASP C   31  UNP  P01375    ARG   107 ENGINEERED
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 ASP 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 ASP
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 ASP 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 ASP
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 ASP 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 ASP
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 C  157  LEU
FORMUL   4  HOH   *69(H2 O)
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  2.56
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.40
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.36
CRYST1   94.700   94.700  117.400  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      0.010560  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010560  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008518        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