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PDBsum entry 5tsw

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Top Page protein Protein-protein interface(s) links
Lymphokine PDB id
5tsw
Jmol
Contents
Protein chains
(+ 0 more) 149 a.a. *
Waters ×1068
* Residue conservation analysis
HEADER    LYMPHOKINE                              22-APR-99   5TSW
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF A HUMAN TNF-ALPHA
TITLE    2 MUTANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (TUMOR NECROSIS FACTOR-ALPHA);
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 ENGINEERED: YES;
COMPND   5 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 BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)
KEYWDS    LYMPHOKINE, LOW SYSTEMIC TOXICITY, MUTANT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.-S.CHA,J.-S.KIM,H.-S.CHO,B.-H.OH
REVDAT   3   24-FEB-09 5TSW    1       VERSN
REVDAT   2   23-SEP-03 5TSW    1       DBREF  SEQADV
REVDAT   1   07-MAY-99 5TSW    0
SPRSDE     30-APR-99 5TSW      4TSW
JRNL        AUTH   S.S.CHA,J.S.KIM,H.S.CHO,N.K.SHIN,W.JEONG,H.C.SHIN,
JRNL        AUTH 2 Y.J.KIM,J.H.HAHN,B.H.OH
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURE OF A HUMAN TUMOR
JRNL        TITL 2 NECROSIS FACTOR-ALPHA MUTANT WITH LOW SYSTEMIC
JRNL        TITL 3 TOXICITY.
JRNL        REF    J.BIOL.CHEM.                  V. 273  2153 1998
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   9442056
JRNL        DOI    10.1074/JBC.273.4.2153
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.J.ECK,S.R.SPRANG
REMARK   1  TITL   THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT
REMARK   1  TITL 2 2.6 A RESOLUTION. IMPLICATIONS FOR RECEPTOR BINDING
REMARK   1  REF    J.BIOL.CHEM.                  V. 264 17595 1989
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.01
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.5
REMARK   3   NUMBER OF REFLECTIONS             : 41282
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) : 0.207
REMARK   3   FREE R VALUE                     : 0.299
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
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            : 8190
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 1068
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) : 0.30
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) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.99
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 5TSW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-99.
REMARK 100 THE RCSB ID CODE IS RCSB000954.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-95
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 6.8
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          : MACSCIENCE M18XHF
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41282
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04000
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: SINGLE WAVELENGTH
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   (%): 42.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENEGLYCOL 4000, 0.1 M
REMARK 280  SODIUM CITRATE PH 5.6, PH 6.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       47.08500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.94500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.28000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.94500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.08500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.28000
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 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: 5980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 5940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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     PRO A     8
REMARK 465     PRO B     8
REMARK 465     PRO C     8
REMARK 465     PRO D     8
REMARK 465     PRO E     8
REMARK 465     PRO F     8
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     SER A   9    OG
REMARK 470     ASP A  10    CG   OD1  OD2
REMARK 470     GLU A  23    CG   CD   OE1  OE2
REMARK 470     GLN A  25    CG   CD   OE1  NE2
REMARK 470     TYR A  87    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLN A  88    CG   CD   OE1  NE2
REMARK 470     ARG A 103    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 107    CG   CD   OE1  OE2
REMARK 470     GLU A 110    CG   CD   OE1  OE2
REMARK 470     LEU A 157    O
REMARK 470     SER B   9    OG
REMARK 470     ASP B  10    CG   OD1  OD2
REMARK 470     GLU B  23    CG   CD   OE1  OE2
REMARK 470     GLN B  25    CG   CD   OE1  NE2
REMARK 470     TYR B  87    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLN B  88    CG   CD   OE1  NE2
REMARK 470     ARG B 103    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B 104    CG   CD   OE1  OE2
REMARK 470     GLU B 107    CG   CD   OE1  OE2
REMARK 470     GLU B 110    CG   CD   OE1  OE2
REMARK 470     GLU B 146    CG   CD   OE1  OE2
REMARK 470     LEU B 157    O
REMARK 470     SER C   9    OG
REMARK 470     ASP C  10    CG   OD1  OD2
REMARK 470     GLU C  23    CG   CD   OE1  OE2
REMARK 470     GLN C  25    CG   CD   OE1  NE2
REMARK 470     TYR C  87    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLN C  88    CG   CD   OE1  NE2
REMARK 470     ARG C 103    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C 104    CG   CD   OE1  OE2
REMARK 470     GLU C 107    CG   CD   OE1  OE2
REMARK 470     GLU C 110    CG   CD   OE1  OE2
REMARK 470     LEU C 157    O
REMARK 470     SER D   9    OG
REMARK 470     ASP D  10    CG   OD1  OD2
REMARK 470     GLU D  23    CG   CD   OE1  OE2
REMARK 470     GLN D  25    CG   CD   OE1  NE2
REMARK 470     TYR D  87    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLN D  88    CG   CD   OE1  NE2
REMARK 470     ARG D 103    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 104    CG   CD   OE1  OE2
REMARK 470     GLU D 107    CG   CD   OE1  OE2
REMARK 470     GLU D 110    CG   CD   OE1  OE2
REMARK 470     GLU D 146    CG   CD   OE1  OE2
REMARK 470     LEU D 157    O
REMARK 470     SER E   9    OG
REMARK 470     ASP E  10    CG   OD1  OD2
REMARK 470     GLU E  23    CG   CD   OE1  OE2
REMARK 470     GLN E  25    CG   CD   OE1  NE2
REMARK 470     TYR E  87    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLN E  88    CG   CD   OE1  NE2
REMARK 470     ARG E 103    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU E 104    CG   CD   OE1  OE2
REMARK 470     GLU E 107    CG   CD   OE1  OE2
REMARK 470     GLU E 110    CG   CD   OE1  OE2
REMARK 470     GLU E 146    CG   CD   OE1  OE2
REMARK 470     LEU E 157    O
REMARK 470     SER F   9    OG
REMARK 470     ASP F  10    CG   OD1  OD2
REMARK 470     GLU F  23    CG   CD   OE1  OE2
REMARK 470     GLN F  25    CG   CD   OE1  NE2
REMARK 470     TYR F  87    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLN F  88    CG   CD   OE1  NE2
REMARK 470     ARG F 103    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU F 104    CG   CD   OE1  OE2
REMARK 470     GLU F 107    CG   CD   OE1  OE2
REMARK 470     GLU F 110    CG   CD   OE1  OE2
REMARK 470     GLU F 146    CG   CD   OE1  OE2
REMARK 470     LEU F 157    O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    ALA E    84     N    SER E    86              2.15
REMARK 500
REMARK 500 REMARK: NULL
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   O    GLU B    53     NH2  ARG E    31     4455     2.05
REMARK 500   O    HOH A   177     O    HOH F   192     4555     2.08
REMARK 500   O    HOH A   180     O    HOH F  1578     4555     2.17
REMARK 500
REMARK 500 REMARK: NULL
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    GLN A  88   C     THR A  89   N      -0.229
REMARK 500    GLU B 110   C     ALA B 111   N      -0.156
REMARK 500    GLN C  88   C     THR C  89   N      -0.148
REMARK 500    PRO D  70   C     SER D  71   N      -0.207
REMARK 500    PRO E  70   C     SER E  71   N      -0.181
REMARK 500    ALA E  84   C     VAL E  85   N      -0.283
REMARK 500    GLU E 104   C     THR E 105   N       0.138
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    GLU B 104   O   -  C   -  N   ANGL. DEV. = -17.0 DEGREES
REMARK 500    PRO C  70   O   -  C   -  N   ANGL. DEV. = -11.1 DEGREES
REMARK 500    ALA D  84   O   -  C   -  N   ANGL. DEV. = -10.7 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    HIS A  15       87.88   -159.72
REMARK 500    ALA A  22      112.49    -27.15
REMARK 500    GLU A  23       86.79    -64.07
REMARK 500    ARG A  31       40.77   -100.59
REMARK 500    LEU A  37       89.57   -176.87
REMARK 500    ASP A  45       33.92     71.16
REMARK 500    PRO A  70       59.82    -54.52
REMARK 500    SER A  71     -159.66     56.49
REMARK 500    THR A  72      163.86     56.85
REMARK 500    ALA A  84     -158.87    -73.04
REMARK 500    VAL A  85     -115.60     32.72
REMARK 500    TYR A  87      101.19     64.75
REMARK 500    GLN A  88     -101.68   -112.01
REMARK 500    GLU A 104      108.89    158.30
REMARK 500    THR A 105      -49.56   -157.27
REMARK 500    ALA A 109     -173.79    164.50
REMARK 500    ALA A 111      134.00     76.11
REMARK 500    LYS A 112       84.78    168.92
REMARK 500    ASP A 143       76.62   -106.92
REMARK 500    SER A 147     -160.67     41.80
REMARK 500    HIS B  15       93.98   -162.79
REMARK 500    ARG B  31       57.15    -96.25
REMARK 500    SER B  60      146.63   -178.97
REMARK 500    CYS B  69       56.95   -158.26
REMARK 500    PRO B  70       83.46    -38.78
REMARK 500    SER B  71      161.42     71.88
REMARK 500    THR B  72      147.40     62.86
REMARK 500    VAL B  85      -79.51     51.91
REMARK 500    SER B  86      100.83    174.75
REMARK 500    GLU B 104      109.48   -173.65
REMARK 500    GLU B 107      156.77     84.22
REMARK 500    ALA B 111       74.93    -19.28
REMARK 500    PRO C  20        1.01    -64.84
REMARK 500    LEU C  37       83.06   -174.18
REMARK 500    SER C  60      151.52    174.83
REMARK 500    GLN C  67      127.88   -171.73
REMARK 500    PRO C  70       72.54    -60.10
REMARK 500    SER C  71      173.05     54.58
REMARK 500    THR C  72       92.02     54.23
REMARK 500    VAL C  85      -91.55     57.43
REMARK 500    SER C  86       64.40   -161.79
REMARK 500    TYR C  87       69.77     77.48
REMARK 500    GLN C  88     -134.73    -99.24
REMARK 500    GLU C 104      -14.32    165.95
REMARK 500    THR C 105      136.43    -14.59
REMARK 500    GLU C 107      129.17     64.07
REMARK 500    ALA C 109     -156.04    -78.91
REMARK 500    GLU C 110      156.65    173.96
REMARK 500    PRO D  20        8.45    -64.86
REMARK 500    LEU D  37       97.20   -175.37
REMARK 500    ARG D  44     -104.61    -87.62
REMARK 500    PRO D  70       62.58    -46.60
REMARK 500    SER D  71     -149.50     58.70
REMARK 500    THR D  72      156.72     41.44
REMARK 500    VAL D  85      -77.34     59.51
REMARK 500    SER D  86       85.91    164.25
REMARK 500    TYR D  87       94.12     71.70
REMARK 500    GLN D  88      -80.51   -132.26
REMARK 500    GLU D 104       97.44   -171.58
REMARK 500    GLU D 107     -163.45     62.21
REMARK 500    ALA D 109     -150.64     82.97
REMARK 500    GLU D 110     -166.19    173.11
REMARK 500    ALA D 111      112.97     83.63
REMARK 500    LYS D 112      108.03   -163.69
REMARK 500    ASP D 143       79.79   -116.61
REMARK 500    HIS E  15       84.87   -159.14
REMARK 500    ASN E  34       46.87     75.60
REMARK 500    LEU E  37       76.64   -175.74
REMARK 500    ARG E  44     -108.10    -89.23
REMARK 500    PRO E  70       72.66    -46.71
REMARK 500    SER E  71     -147.38     43.65
REMARK 500    THR E  72     -156.19     28.40
REMARK 500    ALA E  84       86.23    -27.58
REMARK 500    VAL E  85      -74.58     47.12
REMARK 500    TYR E  87        9.02     50.69
REMARK 500    THR E  89      113.96    -29.18
REMARK 500    GLU E 104       62.62    179.61
REMARK 500    THR E 105      -98.44   -120.87
REMARK 500    GLU E 107     -159.00    -84.16
REMARK 500    LEU F  37       84.46    158.06
REMARK 500    ASN F  46        8.96     59.44
REMARK 500    CYS F  69       63.46   -157.33
REMARK 500    PRO F  70       88.04    -62.07
REMARK 500    SER F  71      154.25     76.21
REMARK 500    THR F  72      131.50     61.53
REMARK 500    ALA F  84     -175.06    -65.65
REMARK 500    VAL F  85      -81.46     32.45
REMARK 500    SER F  86      109.64   -161.17
REMARK 500    GLU F 104      104.45   -167.31
REMARK 500    PRO F 106       79.83    -60.55
REMARK 500    GLU F 107      -93.48     64.01
REMARK 500    ALA F 111       77.18     81.46
REMARK 500    SER F 147     -141.05     35.90
REMARK 500    PHE F 152      125.64   -171.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR D 119         0.07    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    ALA A  84        -12.63
REMARK 500    PRO B  70         14.26
REMARK 500    GLU B 104         21.18
REMARK 500    PRO C  70        -18.96
REMARK 500    ALA C  84        -21.49
REMARK 500    ALA D  84        -17.14
REMARK 500    GLU D 104         11.19
REMARK 500    PRO F  70         10.93
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 D 167        DISTANCE =  7.11 ANGSTROMS
REMARK 525    HOH E 216        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH D 191        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A 197        DISTANCE = 10.71 ANGSTROMS
REMARK 525    HOH C 201        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH F 304        DISTANCE =  6.29 ANGSTROMS
REMARK 525    HOH A 204        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH A 205        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH F1532        DISTANCE =  5.45 ANGSTROMS
REMARK 525    HOH E1537        DISTANCE =  6.99 ANGSTROMS
REMARK 525    HOH A 208        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH F1534        DISTANCE =  6.99 ANGSTROMS
REMARK 525    HOH B 218        DISTANCE =  8.60 ANGSTROMS
REMARK 525    HOH B 219        DISTANCE =  8.62 ANGSTROMS
DBREF  5TSW A    8   157  UNP    P01375   TNFA_HUMAN      84    233
DBREF  5TSW B    8   157  UNP    P01375   TNFA_HUMAN      84    233
DBREF  5TSW C    8   157  UNP    P01375   TNFA_HUMAN      84    233
DBREF  5TSW D    8   157  UNP    P01375   TNFA_HUMAN      84    233
DBREF  5TSW E    8   157  UNP    P01375   TNFA_HUMAN      84    233
DBREF  5TSW F    8   157  UNP    P01375   TNFA_HUMAN      84    233
SEQADV 5TSW SER A   29  UNP  P01375    LEU   105 ENGINEERED
SEQADV 5TSW ILE A   52  UNP  P01375    SER   128 ENGINEERED
SEQADV 5TSW PHE A   56  UNP  P01375    TYR   132 ENGINEERED
SEQADV 5TSW SER B   29  UNP  P01375    LEU   105 ENGINEERED
SEQADV 5TSW ILE B   52  UNP  P01375    SER   128 ENGINEERED
SEQADV 5TSW PHE B   56  UNP  P01375    TYR   132 ENGINEERED
SEQADV 5TSW SER C   29  UNP  P01375    LEU   105 ENGINEERED
SEQADV 5TSW ILE C   52  UNP  P01375    SER   128 ENGINEERED
SEQADV 5TSW PHE C   56  UNP  P01375    TYR   132 ENGINEERED
SEQADV 5TSW SER D   29  UNP  P01375    LEU   105 ENGINEERED
SEQADV 5TSW ILE D   52  UNP  P01375    SER   128 ENGINEERED
SEQADV 5TSW PHE D   56  UNP  P01375    TYR   132 ENGINEERED
SEQADV 5TSW SER E   29  UNP  P01375    LEU   105 ENGINEERED
SEQADV 5TSW ILE E   52  UNP  P01375    SER   128 ENGINEERED
SEQADV 5TSW PHE E   56  UNP  P01375    TYR   132 ENGINEERED
SEQADV 5TSW SER F   29  UNP  P01375    LEU   105 ENGINEERED
SEQADV 5TSW ILE F   52  UNP  P01375    SER   128 ENGINEERED
SEQADV 5TSW PHE F   56  UNP  P01375    TYR   132 ENGINEERED
SEQRES   1 A  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO
SEQRES   2 A  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA
SEQRES   3 A  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN
SEQRES   4 A  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR
SEQRES   5 A  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR
SEQRES   6 A  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL
SEQRES   7 A  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS
SEQRES   8 A  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA
SEQRES   9 A  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE
SEQRES  10 A  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN
SEQRES  11 A  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL
SEQRES  12 A  150  TYR PHE GLY ILE ILE ALA LEU
SEQRES   1 B  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO
SEQRES   2 B  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA
SEQRES   3 B  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN
SEQRES   4 B  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR
SEQRES   5 B  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR
SEQRES   6 B  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL
SEQRES   7 B  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS
SEQRES   8 B  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA
SEQRES   9 B  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE
SEQRES  10 B  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN
SEQRES  11 B  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL
SEQRES  12 B  150  TYR PHE GLY ILE ILE ALA LEU
SEQRES   1 C  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO
SEQRES   2 C  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA
SEQRES   3 C  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN
SEQRES   4 C  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR
SEQRES   5 C  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR
SEQRES   6 C  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL
SEQRES   7 C  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS
SEQRES   8 C  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA
SEQRES   9 C  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE
SEQRES  10 C  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN
SEQRES  11 C  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL
SEQRES  12 C  150  TYR PHE GLY ILE ILE ALA LEU
SEQRES   1 D  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO
SEQRES   2 D  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA
SEQRES   3 D  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN
SEQRES   4 D  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR
SEQRES   5 D  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR
SEQRES   6 D  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL
SEQRES   7 D  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS
SEQRES   8 D  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA
SEQRES   9 D  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE
SEQRES  10 D  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN
SEQRES  11 D  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL
SEQRES  12 D  150  TYR PHE GLY ILE ILE ALA LEU
SEQRES   1 E  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO
SEQRES   2 E  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA
SEQRES   3 E  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN
SEQRES   4 E  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR
SEQRES   5 E  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR
SEQRES   6 E  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL
SEQRES   7 E  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS
SEQRES   8 E  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA
SEQRES   9 E  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE
SEQRES  10 E  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN
SEQRES  11 E  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL
SEQRES  12 E  150  TYR PHE GLY ILE ILE ALA LEU
SEQRES   1 F  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO
SEQRES   2 F  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA
SEQRES   3 F  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN
SEQRES   4 F  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR
SEQRES   5 F  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR
SEQRES   6 F  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL
SEQRES   7 F  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS
SEQRES   8 F  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA
SEQRES   9 F  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE
SEQRES  10 F  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN
SEQRES  11 F  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL
SEQRES  12 F  150  TYR PHE GLY ILE ILE ALA LEU
FORMUL   7  HOH   *356(H2 O)
HELIX    1   1 PRO B  139  TYR B  141  5                                   3
HELIX    2   2 PRO C  139  TYR C  141  5                                   3
HELIX    3   3 PRO E   20  ALA E   22  5                                   3
HELIX    4   4 PRO E  139  TYR E  141  5                                   3
HELIX    5   5 PRO F  139  TYR F  141  5                                   3
SHEET    1   A 5 LEU A  36  ALA A  38  0
SHEET    2   A 5 VAL A  13  VAL A  17 -1  N  HIS A  15   O  LEU A  36
SHEET    3   A 5 TYR A 151  ALA A 156 -1  N  ILE A 154   O  ALA A  14
SHEET    4   A 5 GLY A  54  GLN A  67 -1  N  GLN A  61   O  TYR A 151
SHEET    5   A 5 PRO A 113  LEU A 126 -1  N  LEU A 126   O  GLY A  54
SHEET    1   B 3 ARG A 131  ILE A 136  0
SHEET    2   B 3 LEU A  76  ILE A  83 -1  N  ILE A  83   O  ARG A 131
SHEET    3   B 3 VAL A  91  LYS A  98 -1  N  LYS A  98   O  LEU A  76
SHEET    1   C 5 LEU B  36  ALA B  38  0
SHEET    2   C 5 VAL B  13  VAL B  17 -1  N  HIS B  15   O  LEU B  36
SHEET    3   C 5 TYR B 151  ALA B 156 -1  N  ILE B 154   O  ALA B  14
SHEET    4   C 5 GLY B  54  GLN B  67 -1  N  GLN B  61   O  TYR B 151
SHEET    5   C 5 PRO B 113  LEU B 126 -1  N  LEU B 126   O  GLY B  54
SHEET    1   D 2 GLU B  42  ARG B  44  0
SHEET    2   D 2 GLN B  47  VAL B  49 -1  N  VAL B  49   O  GLU B  42
SHEET    1   E 3 ARG B 131  ILE B 136  0
SHEET    2   E 3 LEU B  76  ILE B  83 -1  N  ILE B  83   O  ARG B 131
SHEET    3   E 3 LYS B  90  LYS B  98 -1  N  LYS B  98   O  LEU B  76
SHEET    1   F 5 LEU C  36  ALA C  38  0
SHEET    2   F 5 VAL C  13  VAL C  17 -1  N  HIS C  15   O  LEU C  36
SHEET    3   F 5 TYR C 151  ALA C 156 -1  N  ILE C 154   O  ALA C  14
SHEET    4   F 5 GLY C  54  GLN C  67 -1  N  GLN C  61   O  TYR C 151
SHEET    5   F 5 PRO C 113  LEU C 126 -1  N  LEU C 126   O  GLY C  54
SHEET    1   G 2 GLU C  42  ARG C  44  0
SHEET    2   G 2 GLN C  47  VAL C  49 -1  N  VAL C  49   O  GLU C  42
SHEET    1   H 3 ARG C 131  ILE C 136  0
SHEET    2   H 3 LEU C  75  ILE C  83 -1  N  ILE C  83   O  ARG C 131
SHEET    3   H 3 LYS C  90  SER C  99 -1  N  LYS C  98   O  LEU C  76
SHEET    1   I 5 LEU D  36  ALA D  38  0
SHEET    2   I 5 VAL D  13  VAL D  17 -1  N  HIS D  15   O  LEU D  36
SHEET    3   I 5 TYR D 151  ALA D 156 -1  N  ILE D 154   O  ALA D  14
SHEET    4   I 5 GLY D  54  GLN D  67 -1  N  GLN D  61   O  TYR D 151
SHEET    5   I 5 PRO D 113  LEU D 126 -1  N  LEU D 126   O  GLY D  54
SHEET    1   J 3 ARG D 131  ILE D 136  0
SHEET    2   J 3 LEU D  76  ILE D  83 -1  N  ILE D  83   O  ARG D 131
SHEET    3   J 3 LYS D  90  LYS D  98 -1  N  LYS D  98   O  LEU D  76
SHEET    1   K 5 LEU E  36  ALA E  38  0
SHEET    2   K 5 VAL E  13  VAL E  17 -1  N  HIS E  15   O  LEU E  36
SHEET    3   K 5 TYR E 151  ALA E 156 -1  N  ILE E 154   O  ALA E  14
SHEET    4   K 5 GLY E  54  GLN E  67 -1  N  GLN E  61   O  TYR E 151
SHEET    5   K 5 PRO E 113  LEU E 126 -1  N  LEU E 126   O  GLY E  54
SHEET    1   L 3 ARG E 131  ILE E 136  0
SHEET    2   L 3 LEU E  75  ILE E  83 -1  N  ILE E  83   O  ARG E 131
SHEET    3   L 3 LYS E  90  SER E  99 -1  N  LYS E  98   O  LEU E  76
SHEET    1   M 5 LEU F  36  ALA F  38  0
SHEET    2   M 5 VAL F  13  VAL F  17 -1  N  HIS F  15   O  LEU F  36
SHEET    3   M 5 TYR F 151  ALA F 156 -1  N  ILE F 154   O  ALA F  14
SHEET    4   M 5 GLY F  54  GLN F  67 -1  N  GLN F  61   O  TYR F 151
SHEET    5   M 5 PRO F 113  LEU F 126 -1  N  LEU F 126   O  GLY F  54
SHEET    1   N 2 GLU F  42  ARG F  44  0
SHEET    2   N 2 GLN F  47  VAL F  49 -1  N  VAL F  49   O  GLU F  42
SHEET    1   O 3 ARG F 131  ILE F 136  0
SHEET    2   O 3 LEU F  76  ILE F  83 -1  N  ILE F  83   O  ARG F 131
SHEET    3   O 3 LYS F  90  LYS F  98 -1  N  LYS F  98   O  LEU F  76
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.47
SSBOND   2 CYS E   69    CYS E  101                          1555   1555  2.24
SSBOND   3 CYS F   69    CYS F  101                          1555   1555  2.45
CRYST1   94.170   94.560   95.890  90.00  90.00  90.00 P 21 21 21   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      0.010619  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010575  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010429        0.00000
      
PROCHECK
Go to PROCHECK summary
 References