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PDBsum entry 2e7a

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Top Page protein Protein-protein interface(s) links
Cytokine PDB id
2e7a
Jmol
Contents
Protein chains
150 a.a.
142 a.a.
Waters ×237
HEADER    CYTOKINE                                09-JAN-07   2E7A
TITLE     TNF RECEPTOR SUBTYPE ONE-SELECTIVE TNF MUTANT WITH
TITLE    2 ANTAGONISTIC ACTIVITY
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;
COMPND   3 CHAIN: A, B, C;
COMPND   4 SYNONYM: TNF;
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 BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PYAS(MODIFIED FROM PUC18);
SOURCE  10 OTHER_DETAILS: THIS MUTANT WAS CREATED BY PHAGE DISPLAY
SOURCE  11 SYSTEM
KEYWDS    TUMOR NECROSIS FACTOR, TRIMER, ANTAGONISTIC ACTIVITY, TNFR1
KEYWDS   2 SPECIFIC, PHAGE DISPLAY SYSTEM, CYTOKINE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.MUKAI,Y.YAMAGATA,Y.TSUTSUMI
REVDAT   3   24-FEB-09 2E7A    1       VERSN
REVDAT   2   25-MAR-08 2E7A    1       JRNL
REVDAT   1   13-NOV-07 2E7A    0
JRNL        AUTH   H.SHIBATA,Y.YOSHIOKA,A.OHKAWA,K.MINOWA,Y.MUKAI,
JRNL        AUTH 2 Y.ABE,M.TANIAI,T.NOMURA,H.KAYAMURO,H.NABESHI,
JRNL        AUTH 3 T.SUGITA,S.IMAI,K.NAGANO,T.YOSHIKAWA,T.FUJITA,
JRNL        AUTH 4 S.NAKAGAWA,A.YAMAMOTO,T.OHTA,T.HAYAKAWA,T.MAYUMI,
JRNL        AUTH 5 P.VANDENABEELE,B.B.AGGARWAL,T.NAKAMURA,Y.YAMAGATA,
JRNL        AUTH 6 S.TSUNODA,H.KAMADA,Y.TSUTSUMI
JRNL        TITL   CREATION AND X-RAY STRUCTURE ANALYSIS OF THE TUMOR
JRNL        TITL 2 NECROSIS FACTOR RECEPTOR-1-SELECTIVE MUTANT OF A
JRNL        TITL 3 TUMOR NECROSIS FACTOR-ALPHA ANTAGONIST
JRNL        REF    J.BIOL.CHEM.                  V. 283   998 2008
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   18003610
JRNL        DOI    10.1074/JBC.M707933200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.00
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             : 42155
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) : 0.198
REMARK   3   FREE R VALUE                     : 0.239
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            : 3387
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 237
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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 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 2E7A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-07.
REMARK 100 THE RCSB ID CODE IS RCSB026314.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL41XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42227
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 7.100
REMARK 200  R MERGE                    (I) : 0.06300
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) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.48400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.710
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1TNF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M HEPES PH7.5, 1.5%(W/V) 1,2,3-
REMARK 280  HEPTANETRIOL, 12.5% PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
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       32.28000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.78000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.48500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.78000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.28000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.48500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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: 6330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.6 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     THR A     7
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     THR B     7
REMARK 465     ARG B   103
REMARK 465     GLU B   104
REMARK 465     THR B   105
REMARK 465     PRO B   106
REMARK 465     GLU B   107
REMARK 465     GLY B   108
REMARK 465     ALA B   109
REMARK 465     GLU B   110
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     THR C     7
REMARK 465     GLU C   104
REMARK 465     THR C   105
REMARK 465     PRO C   106
REMARK 465     GLU C   107
REMARK 465     GLY C   108
REMARK 465     ALA C   109
REMARK 465     GLU C   110
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     -138.76     49.18
REMARK 500    ASP A  10      -27.02     81.22
REMARK 500    LEU A  37       98.39   -167.97
REMARK 500    HIS A  87       52.93   -154.15
REMARK 500    ASN A  88      -54.79    -18.26
REMARK 500    GLN A  89      105.27    -33.00
REMARK 500    ALA B  22       73.46   -104.51
REMARK 500    ARG B  31       80.57    -68.96
REMARK 500    LEU B  37       87.95   -164.64
REMARK 500    ASN B 112       -5.80   -152.47
REMARK 500    ALA C  22       55.29   -103.44
REMARK 500    LEU C  37       92.32   -167.16
REMARK 500    HIS C  87      115.54   -171.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TNF   RELATED DB: PDB
REMARK 900 RELATED ID: 1TNR   RELATED DB: PDB
DBREF  2E7A A    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  2E7A B    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  2E7A C    1   157  UNP    P01375   TNFA_HUMAN      77    233
SEQADV 2E7A MET A   11  UNP  P01375    LYS    87 ENGINEERED
SEQADV 2E7A SER A   65  UNP  P01375    LYS   141 ENGINEERED
SEQADV 2E7A SER A   84  UNP  P01375    ALA   160 ENGINEERED
SEQADV 2E7A THR A   85  UNP  P01375    VAL   161 ENGINEERED
SEQADV 2E7A THR A   86  UNP  P01375    SER   162 ENGINEERED
SEQADV 2E7A HIS A   87  UNP  P01375    TYR   163 ENGINEERED
SEQADV 2E7A ASN A   88  UNP  P01375    GLN   164 ENGINEERED
SEQADV 2E7A GLN A   89  UNP  P01375    THR   165 ENGINEERED
SEQADV 2E7A PRO A   90  UNP  P01375    LYS   166 ENGINEERED
SEQADV 2E7A ARG A   98  UNP  P01375    LYS   174 ENGINEERED
SEQADV 2E7A ASN A  112  UNP  P01375    LYS   188 ENGINEERED
SEQADV 2E7A PRO A  128  UNP  P01375    LYS   204 ENGINEERED
SEQADV 2E7A MET B   11  UNP  P01375    LYS    87 ENGINEERED
SEQADV 2E7A SER B   65  UNP  P01375    LYS   141 ENGINEERED
SEQADV 2E7A SER B   84  UNP  P01375    ALA   160 ENGINEERED
SEQADV 2E7A THR B   85  UNP  P01375    VAL   161 ENGINEERED
SEQADV 2E7A THR B   86  UNP  P01375    SER   162 ENGINEERED
SEQADV 2E7A HIS B   87  UNP  P01375    TYR   163 ENGINEERED
SEQADV 2E7A ASN B   88  UNP  P01375    GLN   164 ENGINEERED
SEQADV 2E7A GLN B   89  UNP  P01375    THR   165 ENGINEERED
SEQADV 2E7A PRO B   90  UNP  P01375    LYS   166 ENGINEERED
SEQADV 2E7A ARG B   98  UNP  P01375    LYS   174 ENGINEERED
SEQADV 2E7A ASN B  112  UNP  P01375    LYS   188 ENGINEERED
SEQADV 2E7A PRO B  128  UNP  P01375    LYS   204 ENGINEERED
SEQADV 2E7A MET C   11  UNP  P01375    LYS    87 ENGINEERED
SEQADV 2E7A SER C   65  UNP  P01375    LYS   141 ENGINEERED
SEQADV 2E7A SER C   84  UNP  P01375    ALA   160 ENGINEERED
SEQADV 2E7A THR C   85  UNP  P01375    VAL   161 ENGINEERED
SEQADV 2E7A THR C   86  UNP  P01375    SER   162 ENGINEERED
SEQADV 2E7A HIS C   87  UNP  P01375    TYR   163 ENGINEERED
SEQADV 2E7A ASN C   88  UNP  P01375    GLN   164 ENGINEERED
SEQADV 2E7A GLN C   89  UNP  P01375    THR   165 ENGINEERED
SEQADV 2E7A PRO C   90  UNP  P01375    LYS   166 ENGINEERED
SEQADV 2E7A ARG C   98  UNP  P01375    LYS   174 ENGINEERED
SEQADV 2E7A ASN C  112  UNP  P01375    LYS   188 ENGINEERED
SEQADV 2E7A PRO C  128  UNP  P01375    LYS   204 ENGINEERED
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET 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 SER
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 SER THR THR HIS ASN GLN PRO VAL
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO 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 MET 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 SER
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 SER THR THR HIS ASN GLN PRO VAL
SEQRES   8 B  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 B  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 B  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO 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 MET 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 SER
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 SER THR THR HIS ASN GLN PRO VAL
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO 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   *237(H2 O)
HELIX    1   1 SER A   84  ASN A   88  5                                   5
HELIX    2   2 ARG A  138  LEU A  142  5                                   5
HELIX    3   3 ARG B  138  LEU B  142  5                                   5
SHEET    1   A 3 TRP A  28  LEU A  29  0
SHEET    2   A 3 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29
SHEET    3   A 3 LEU A  36  ALA A  38 -1  O  ALA A  38   N  VAL A  13
SHEET    1   B 5 TRP A  28  LEU A  29  0
SHEET    2   B 5 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29
SHEET    3   B 5 TYR A 151  ALA A 156 -1  O  PHE A 152   N  VAL A  16
SHEET    4   B 5 GLY A  54  GLN A  67 -1  N  TYR A  59   O  GLY A 153
SHEET    5   B 5 PRO A 113  LEU A 126 -1  O  GLY A 122   N  ILE A  58
SHEET    1   C 5 GLU A  42  ARG A  44  0
SHEET    2   C 5 GLN A  47  VAL A  49 -1  O  GLN A  47   N  ARG A  44
SHEET    3   C 5 ARG A 131  ILE A 136 -1  O  LEU A 132   N  LEU A  48
SHEET    4   C 5 LEU A  76  ILE A  83 -1  N  ILE A  83   O  ARG A 131
SHEET    5   C 5 VAL A  91  ARG A  98 -1  O  ARG A  98   N  LEU A  76
SHEET    1   D 3 TRP B  28  LEU B  29  0
SHEET    2   D 3 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29
SHEET    3   D 3 LEU B  36  ALA B  38 -1  O  LEU B  36   N  HIS B  15
SHEET    1   E 5 TRP B  28  LEU B  29  0
SHEET    2   E 5 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29
SHEET    3   E 5 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16
SHEET    4   E 5 GLY B  54  GLY B  66 -1  N  TYR B  59   O  GLY B 153
SHEET    5   E 5 TRP B 114  LEU B 126 -1  O  TRP B 114   N  GLY B  66
SHEET    1   F 5 GLU B  42  ARG B  44  0
SHEET    2   F 5 GLN B  47  VAL B  49 -1  O  VAL B  49   N  GLU B  42
SHEET    3   F 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48
SHEET    4   F 5 LEU B  76  SER B  84 -1  N  ILE B  83   O  ARG B 131
SHEET    5   F 5 HIS B  87  ARG B  98 -1  O  ARG B  98   N  LEU B  76
SHEET    1   G 3 TRP C  28  LEU C  29  0
SHEET    2   G 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29
SHEET    3   G 3 LEU C  36  ALA C  38 -1  O  ALA C  38   N  VAL C  13
SHEET    1   H 5 TRP C  28  LEU C  29  0
SHEET    2   H 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29
SHEET    3   H 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16
SHEET    4   H 5 GLY C  54  GLN C  67 -1  N  TYR C  59   O  GLY C 153
SHEET    5   H 5 PRO C 113  LEU C 126 -1  O  LEU C 126   N  GLY C  54
SHEET    1   I 5 GLU C  42  ARG C  44  0
SHEET    2   I 5 GLN C  47  VAL C  49 -1  O  VAL C  49   N  GLU C  42
SHEET    3   I 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48
SHEET    4   I 5 LEU C  76  SER C  84 -1  N  ILE C  83   O  ARG C 131
SHEET    5   I 5 HIS C  87  ARG C  98 -1  O  ARG C  98   N  LEU C  76
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.03
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.04
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.03
CRYST1   64.560   66.970  103.560  90.00  90.00  90.00 P 21 21 21   12
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      0.015489  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014932  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009656        0.00000
      
PROCHECK
Go to PROCHECK summary
 References