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PDBsum entry 2tun

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Lymphokine PDB id
2tun
Jmol
Contents
Protein chains
(+ 0 more) 151 a.a. *
* Residue conservation analysis
HEADER    LYMPHOKINE                              06-OCT-93   2TUN
TITLE     CONFORMATIONAL CHANGES IN THE (ALA-84-VAL) MUTANT OF TUMOR NECROSIS
TITLE    2 FACTOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 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
KEYWDS    LYMPHOKINE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.SALUDJIAN,T.PRANGE
REVDAT   4   19-JUN-13 2TUN    1       REMARK SEQADV
REVDAT   3   13-JUL-11 2TUN    1       VERSN
REVDAT   2   24-FEB-09 2TUN    1       VERSN
REVDAT   1   31-JAN-94 2TUN    0
JRNL        AUTH   P.SALUDJIAN,T.PRANGE,R.KAHN,R.FOURME,J.TAVERNIER,
JRNL        AUTH 2 X.VAN-OOSTADE,W.FIERS,G.NAVAZA
JRNL        TITL   CONFORMATIONAL CHANGES IN THE (ALA-84-VAL) MUTANT OF TUMOR
JRNL        TITL 2 NECROSIS FACTOR
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   E.Y.JONES,N.P.WALKER,D.I.STUART
REMARK   1  TITL   METHODOLOGY EMPLOYED FOR THE STRUCTURE DETERMINATION OF
REMARK   1  TITL 2 TUMOR NECROSIS FACTOR, A CASE OF HIGH NON-CRYSTALLOGRAPHIC
REMARK   1  TITL 3 SYMMETRY
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.A      V.  47   753 1991
REMARK   1  REFN                   ISSN 0108-7673
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M.J.ECK,S.R.SPRANG
REMARK   1  TITL   THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT 2.6
REMARK   1  TITL 2 ANGSTROMS RESOLUTION. IMPLICATIONS FOR RECEPTOR BINDING
REMARK   1  REF    J.BIOL.CHEM.                  V. 264 17595 1989
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 3
REMARK   1  AUTH   E.Y.JONES,D.I.STUART,N.P.WALKER
REMARK   1  TITL   STRUCTURE OF TUMOR NECROSIS FACTOR
REMARK   1  REF    NATURE                        V. 338   225 1989
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1 REFERENCE 4
REMARK   1  AUTH   A.LEWITT-BENTLEY,R.FOURME,R.KAHN,T.PRANGE,P.VACHETTE,
REMARK   1  AUTH 2 J.TAVERNIER,G.HAUQUIER,W.FIERS
REMARK   1  TITL   STRUCTURE OF TUMOR NECROSIS FACTOR BY X-RAY SOLUTION
REMARK   1  TITL 2 SCATTERING AND PRELIMINARY STUDIES BY SINGLE CRYSTAL X-RAY
REMARK   1  TITL 3 DIFFRACTION
REMARK   1  REF    J.MOL.BIOL.                   V. 199   389 1988
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 15325
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 + TEST SET) : 0.198
REMARK   3   R VALUE            (WORKING SET) : NULL
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
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7086
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.018 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.037 ; 0.030
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.070 ; 0.040
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.007 ; 0.010
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.050 ; 0.030
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.230 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.290 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : 0.180 ; 0.300
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : 7.300 ; 2.000
REMARK   3    STAGGERED                 (DEGREES) : 17.700; 10.000
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.807 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 3.210 ; 3.000
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.837 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 3.301 ; 3.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  THE STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT (PROGRAM
REMARK   3  *AMORE*) STARTING FROM THE COORDINATES IN PROTEIN DATA BANK
REMARK   3  ENTRY 1TNF.
REMARK   3
REMARK   3  ONLY FAINT ELECTRON DENSITY IS OBSERVED FOR RESIDUES 1 - 6
REMARK   3  AT THE N-TERMINUS OF EACH CHAIN AND, THEREFORE, NO
REMARK   3  COORDINATES FOR THESE RESIDUES ARE PRESENT IN THIS ENTRY.
REMARK   3  ELECTRON DENSITY FOR THE LOOP 103 - 110 IS ALSO RATHER WEAK
REMARK   3  IN CHAINS A, B, D, AND F.   SEVERE DISTORSIONS ARE ALSO
REMARK   3  OBSERVED IN THE SEGMENTS 7-9
REMARK   4
REMARK   4 2TUN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 65.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       31.23333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.46667
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.46667
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.23333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18070 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 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     ARG A     6
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     ARG B     6
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 465     ARG C     6
REMARK 465     VAL D     1
REMARK 465     ARG D     2
REMARK 465     SER D     3
REMARK 465     SER D     4
REMARK 465     SER D     5
REMARK 465     ARG D     6
REMARK 465     VAL E     1
REMARK 465     ARG E     2
REMARK 465     SER E     3
REMARK 465     SER E     4
REMARK 465     SER E     5
REMARK 465     ARG E     6
REMARK 465     VAL F     1
REMARK 465     ARG F     2
REMARK 465     SER F     3
REMARK 465     SER F     4
REMARK 465     SER F     5
REMARK 465     ARG F     6
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PROTEIN DATA BANK ADVISORY NOTICE:
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999      SWISS-PROT ENTRY NAME: TNFA_HUMAN
REMARK 999
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE
REMARK 999        ASP    220            LEU          137
DBREF  2TUN A    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  2TUN B    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  2TUN C    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  2TUN D    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  2TUN E    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  2TUN F    1   157  UNP    P01375   TNFA_HUMAN      77    233
SEQADV 2TUN VAL A   84  UNP  P01375    ALA   160 ENGINEERED MUTATION
SEQADV 2TUN LEU A  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 2TUN VAL B   84  UNP  P01375    ALA   160 ENGINEERED MUTATION
SEQADV 2TUN LEU B  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 2TUN VAL C   84  UNP  P01375    ALA   160 ENGINEERED MUTATION
SEQADV 2TUN LEU C  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 2TUN VAL D   84  UNP  P01375    ALA   160 ENGINEERED MUTATION
SEQADV 2TUN LEU D  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 2TUN VAL E   84  UNP  P01375    ALA   160 ENGINEERED MUTATION
SEQADV 2TUN LEU E  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 2TUN VAL F   84  UNP  P01375    ALA   160 ENGINEERED MUTATION
SEQADV 2TUN LEU F  143  UNP  P01375    ASP   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 VAL 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 VAL 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 VAL 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
SEQRES   1 D  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES   2 D  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 D  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 D  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 D  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES   6 D  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 D  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES   8 D  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES   9 D  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES  10 D  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES  11 D  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES  12 D  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 D  157  LEU
SEQRES   1 E  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES   2 E  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 E  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 E  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 E  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES   6 E  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 E  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES   8 E  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES   9 E  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES  10 E  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES  11 E  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES  12 E  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 E  157  LEU
SEQRES   1 F  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL
SEQRES   2 F  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 F  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 F  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 F  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS
SEQRES   6 F  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 F  157  THR ILE SER ARG ILE VAL VAL SER TYR GLN THR LYS VAL
SEQRES   8 F  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU
SEQRES   9 F  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO
SEQRES  10 F  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP
SEQRES  11 F  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU LEU
SEQRES  12 F  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 F  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
HELIX    4 H1D ARG D  138  LEU D  142  5                                   5
HELIX    5 H1E ARG E  138  LEU E  142  5                                   5
HELIX    6 H1F ARG F  138  LEU F  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  VAL 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  VAL 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  VAL 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
SHEET    1 S1D 5 LEU D  36  ALA D  38  0
SHEET    2 S1D 5 PRO D  12  ALA D  18 -1  N  HIS D  15   O  LEU D  36
SHEET    3 S1D 5 VAL D 150  LEU D 157 -1  O  VAL D 150   N  ALA D  18
SHEET    4 S1D 5 GLY D  54  GLY D  68 -1  O  GLN D  61   N  TYR D 151
SHEET    5 S1D 5 LYS D 112  LEU D 126 -1  N  LEU D 126   O  GLY D  54
SHEET    1 S2D 5 GLU D  42  ARG D  44  0
SHEET    2 S2D 5 GLN D  47  VAL D  50 -1  O  GLN D  47   N  ARG D  44
SHEET    3 S2D 5 GLY D 129  ILE D 136 -1  N  GLY D 129   O  VAL D  50
SHEET    4 S2D 5 LEU D  76  VAL D  84 -1  N  THR D  79   O  GLU D 135
SHEET    5 S2D 5 GLN D  88  LYS D  98 -1  N  VAL D  91   O  ARG D  82
SHEET    1 S1E 5 LEU E  36  ALA E  38  0
SHEET    2 S1E 5 PRO E  12  ALA E  18 -1  N  HIS E  15   O  LEU E  36
SHEET    3 S1E 5 VAL E 150  LEU E 157 -1  O  VAL E 150   N  ALA E  18
SHEET    4 S1E 5 GLY E  54  GLY E  68 -1  O  GLN E  61   N  TYR E 151
SHEET    5 S1E 5 LYS E 112  LEU E 126 -1  N  LEU E 126   O  GLY E  54
SHEET    1 S2E 5 GLU E  42  ARG E  44  0
SHEET    2 S2E 5 GLN E  47  VAL E  50 -1  O  GLN E  47   N  ARG E  44
SHEET    3 S2E 5 GLY E 129  ILE E 136 -1  N  GLY E 129   O  VAL E  50
SHEET    4 S2E 5 LEU E  76  VAL E  84 -1  N  THR E  79   O  GLU E 135
SHEET    5 S2E 5 GLN E  88  LYS E  98 -1  N  VAL E  91   O  ARG E  82
SHEET    1 S1F 5 LEU F  36  ALA F  38  0
SHEET    2 S1F 5 PRO F  12  ALA F  18 -1  N  HIS F  15   O  LEU F  36
SHEET    3 S1F 5 VAL F 150  LEU F 157 -1  O  VAL F 150   N  ALA F  18
SHEET    4 S1F 5 GLY F  54  GLY F  68 -1  O  GLN F  61   N  TYR F 151
SHEET    5 S1F 5 LYS F 112  LEU F 126 -1  N  LEU F 126   O  GLY F  54
SHEET    1 S2F 5 GLU F  42  ARG F  44  0
SHEET    2 S2F 5 GLN F  47  VAL F  50 -1  O  GLN F  47   N  ARG F  44
SHEET    3 S2F 5 GLY F 129  ILE F 136 -1  N  GLY F 129   O  VAL F  50
SHEET    4 S2F 5 LEU F  76  VAL F  84 -1  N  THR F  79   O  GLU F 135
SHEET    5 S2F 5 GLN F  88  LYS F  98 -1  N  VAL F  91   O  ARG F  82
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.07
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.08
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.07
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.07
SSBOND   5 CYS E   69    CYS E  101                          1555   1555  2.09
SSBOND   6 CYS F   69    CYS F  101                          1555   1555  2.08
CISPEP   1 THR B    7    PRO B    8          0        27.64
CRYST1  166.000  166.000   93.700  90.00  90.00 120.00 P 31 2 1     36
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      0.006024  0.003478  0.000000        0.00000
SCALE2      0.000000  0.006956  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010672        0.00000
      
PROCHECK
Go to PROCHECK summary
 References