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PDBsum entry 1ca9

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Top Page protein ligands Protein-protein interface(s) links
Tnf signaling PDB id
1ca9
Jmol
Contents
Protein chain
(+ 0 more) 191 a.a. *
Ligands
PRO-PHE-SER-LYS-
GLU-GLU-CYS
GLY-GLN-VAL-PRO-
PHE-SER-LYS-GLU-
GLU-CYS
Waters ×910
* Residue conservation analysis
HEADER    TNF SIGNALING                           25-FEB-99   1CA9
TITLE     STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX
TITLE    2 WITH A PEPTIDE FROM TNF-R2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (TNF RECEPTOR ASSOCIATED FACTOR 2);
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 FRAGMENT: TRAF DOMAIN;
COMPND   5 SYNONYM: TRAF2;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: PROTEIN (TNF-R2);
COMPND   9 CHAIN: G, H;
COMPND  10 FRAGMENT: TRAF-BINDING SITE;
COMPND  11 ENGINEERED: 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;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET24D;
SOURCE  10 MOL_ID: 2;
SOURCE  11 SYNTHETIC: YES;
SOURCE  12 OTHER_DETAILS: SEQUENCE FROM HUMAN TNF-R2, SWISS PROT
SOURCE  13 ACCESSION P20333
KEYWDS    TNF SIGNALING, TRAF, ADAPTER PROTEIN, CELL SURVIVAL
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.C.PARK,V.BURKITT,A.R.VILLA,L.TONG,H.WU
REVDAT   3   24-FEB-09 1CA9    1       VERSN
REVDAT   2   01-APR-03 1CA9    1       JRNL
REVDAT   1   12-APR-99 1CA9    0
JRNL        AUTH   Y.C.PARK,V.BURKITT,A.R.VILLA,L.TONG,H.WU
JRNL        TITL   STRUCTURAL BASIS FOR SELF-ASSOCIATION AND RECEPTOR
JRNL        TITL 2 RECOGNITION OF HUMAN TRAF2.
JRNL        REF    NATURE                        V. 398   533 1999
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   10206649
JRNL        DOI    10.1038/19110
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.3
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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
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)   (%) : 87.2
REMARK   3   NUMBER OF REFLECTIONS             : 51071
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) : 0.234
REMARK   3   FREE R VALUE                     : 0.289
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300
REMARK   3   FREE R VALUE TEST SET COUNT      : 3112
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            : 8644
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 910
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.10
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.47
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.89
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72
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 : RESTRAINTS
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  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1CA9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-99.
REMARK 100 THE RCSB ID CODE IS RCSB000541.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59650
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.04800
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REPLACE
REMARK 200 STARTING MODEL: 1CA4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       42.20000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H
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: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000       83.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000      -42.20000
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000        0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     ASP A   310
REMARK 465     ASP B   310
REMARK 465     ASP C   310
REMARK 465     ASP D   310
REMARK 465     GLN D   311
REMARK 465     ASP D   312
REMARK 465     LYS D   313
REMARK 465     ILE D   314
REMARK 465     GLU D   315
REMARK 465     ASP E   310
REMARK 465     GLN E   311
REMARK 465     ASP E   312
REMARK 465     LYS E   313
REMARK 465     ILE E   314
REMARK 465     GLU E   315
REMARK 465     ASP F   310
REMARK 465     GLN F   311
REMARK 465     ASP F   312
REMARK 465     LYS F   313
REMARK 465     ILE F   314
REMARK 465     GLU F   315
REMARK 465     GLY G   419
REMARK 465     GLN G   420
REMARK 465     VAL G   421
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     GLN A 311    CG   CD   OE1  NE2
REMARK 470     ASP A 312    CG   OD1  OD2
REMARK 470     LYS A 313    CG   CD   CE   NZ
REMARK 470     ILE A 314    CG1  CG2  CD1
REMARK 470     LYS A 320    CG   CD   CE   NZ
REMARK 470     GLN A 322    CG   CD   OE1  NE2
REMARK 470     GLN A 323    CG   CD   OE1  NE2
REMARK 470     LEU A 324    CG   CD1  CD2
REMARK 470     GLU A 325    CG   CD   OE1  OE2
REMARK 470     ARG A 326    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER A 327    OG
REMARK 470     ILE A 328    CG1  CG2  CD1
REMARK 470     LYS A 331    CG   CD   CE   NZ
REMARK 470     ASP A 337    CG   OD1  OD2
REMARK 470     GLN A 340    CG   CD   OE1  NE2
REMARK 470     GLU A 344    CG   CD   OE1  OE2
REMARK 470     ARG A 403    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 423    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 440    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 441    CG   CD   OE1  OE2
REMARK 470     GLN B 311    CG   CD   OE1  NE2
REMARK 470     ASP B 312    CG   OD1  OD2
REMARK 470     LYS B 313    CG   CD   CE   NZ
REMARK 470     ILE B 314    CG1  CG2  CD1
REMARK 470     GLU B 315    CG   CD   OE1  OE2
REMARK 470     LEU B 317    CG   CD1  CD2
REMARK 470     SER B 318    OG
REMARK 470     SER B 319    OG
REMARK 470     LYS B 320    CG   CD   CE   NZ
REMARK 470     VAL B 321    CG1  CG2
REMARK 470     GLN B 322    CG   CD   OE1  NE2
REMARK 470     GLN B 323    CG   CD   OE1  NE2
REMARK 470     LEU B 324    CG   CD1  CD2
REMARK 470     GLU B 325    CG   CD   OE1  OE2
REMARK 470     ARG B 326    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER B 327    OG
REMARK 470     ILE B 328    CG1  CG2  CD1
REMARK 470     LEU B 330    CG   CD1  CD2
REMARK 470     LYS B 331    CG   CD   CE   NZ
REMARK 470     LEU B 333    CG   CD1  CD2
REMARK 470     GLN B 340    CG   CD   OE1  NE2
REMARK 470     LYS B 341    CG   CD   CE   NZ
REMARK 470     GLU B 344    CG   CD   OE1  OE2
REMARK 470     ARG B 403    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 423    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 440    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B 441    CG   CD   OE1  OE2
REMARK 470     GLN C 311    CG   CD   OE1  NE2
REMARK 470     ASP C 312    CG   OD1  OD2
REMARK 470     LYS C 313    CG   CD   CE   NZ
REMARK 470     ILE C 314    CG1  CG2  CD1
REMARK 470     GLU C 315    CG   CD   OE1  OE2
REMARK 470     LEU C 317    CG   CD1  CD2
REMARK 470     SER C 318    OG
REMARK 470     SER C 319    OG
REMARK 470     LYS C 320    CG   CD   CE   NZ
REMARK 470     VAL C 321    CG1  CG2
REMARK 470     GLN C 322    CG   CD   OE1  NE2
REMARK 470     GLN C 323    CG   CD   OE1  NE2
REMARK 470     ARG C 326    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE C 328    CG1  CG2  CD1
REMARK 470     LYS C 331    CG   CD   CE   NZ
REMARK 470     ASP C 332    CG   OD1  OD2
REMARK 470     ARG C 403    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C 423    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C 440    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C 441    CG   CD   OE1  OE2
REMARK 470     LEU D 317    CG   CD1  CD2
REMARK 470     SER D 318    OG
REMARK 470     SER D 319    OG
REMARK 470     LYS D 320    CG   CD   CE   NZ
REMARK 470     VAL D 321    CG1  CG2
REMARK 470     GLN D 322    CG   CD   OE1  NE2
REMARK 470     GLN D 323    CG   CD   OE1  NE2
REMARK 470     LEU D 324    CG   CD1  CD2
REMARK 470     GLU D 325    CG   CD   OE1  OE2
REMARK 470     SER D 327    OG
REMARK 470     ILE D 328    CG1  CG2  CD1
REMARK 470     ASP D 332    CG   OD1  OD2
REMARK 470     ASP D 337    CG   OD1  OD2
REMARK 470     LYS D 341    CG   CD   CE   NZ
REMARK 470     GLU D 344    CG   CD   OE1  OE2
REMARK 470     ARG D 403    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D 423    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D 440    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 441    CG   CD   OE1  OE2
REMARK 470     LEU E 317    CG   CD1  CD2
REMARK 470     SER E 318    OG
REMARK 470     SER E 319    OG
REMARK 470     LYS E 320    CG   CD   CE   NZ
REMARK 470     VAL E 321    CG1  CG2
REMARK 470     GLN E 322    CG   CD   OE1  NE2
REMARK 470     GLN E 323    CG   CD   OE1  NE2
REMARK 470     LEU E 324    CG   CD1  CD2
REMARK 470     GLU E 325    CG   CD   OE1  OE2
REMARK 470     LYS E 331    CG   CD   CE   NZ
REMARK 470     ASP E 332    CG   OD1  OD2
REMARK 470     LEU E 333    CG   CD1  CD2
REMARK 470     GLN E 340    CG   CD   OE1  NE2
REMARK 470     ARG E 403    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG E 423    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG E 440    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU E 441    CG   CD   OE1  OE2
REMARK 470     LEU F 317    CG   CD1  CD2
REMARK 470     SER F 318    OG
REMARK 470     SER F 319    OG
REMARK 470     LYS F 320    CG   CD   CE   NZ
REMARK 470     VAL F 321    CG1  CG2
REMARK 470     GLN F 322    CG   CD   OE1  NE2
REMARK 470     GLN F 323    CG   CD   OE1  NE2
REMARK 470     LEU F 324    CG   CD1  CD2
REMARK 470     GLU F 325    CG   CD   OE1  OE2
REMARK 470     ARG F 326    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER F 327    OG
REMARK 470     ILE F 328    CG1  CG2  CD1
REMARK 470     LEU F 330    CG   CD1  CD2
REMARK 470     LYS F 331    CG   CD   CE   NZ
REMARK 470     ASP F 332    CG   OD1  OD2
REMARK 470     LEU F 333    CG   CD1  CD2
REMARK 470     ARG F 403    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG F 423    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG F 440    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU F 441    CG   CD   OE1  OE2
REMARK 470     GLY H 419    N
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   N    VAL F   321     O    HOH F  6455              2.15
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    ALA A 370        4.26    -67.76
REMARK 500    THR A 401       -4.67    -53.78
REMARK 500    VAL A 451      -16.51    -38.45
REMARK 500    LEU A 471       41.39   -107.69
REMARK 500    LYS A 477        6.10    -63.64
REMARK 500    MET A 478      -22.82   -151.87
REMARK 500    ALA A 480     -147.66   -119.27
REMARK 500    ASP B 351       17.16   -140.58
REMARK 500    LEU B 396       -5.96    -58.38
REMARK 500    GLN B 437       10.48    -69.42
REMARK 500    ASN B 439       51.66     26.03
REMARK 500    LEU B 471       50.79   -113.06
REMARK 500    MET B 478      -56.20   -130.37
REMARK 500    GLU B 479       24.83    -60.41
REMARK 500    ALA B 480     -146.16   -138.87
REMARK 500    ARG C 440      -64.51    -90.94
REMARK 500    MET C 478      -31.71   -133.93
REMARK 500    GLU C 479       20.26    -74.74
REMARK 500    LEU D 317      -70.88    -44.10
REMARK 500    GLN D 322      -73.42    -63.13
REMARK 500    GLN D 323      -33.80    -38.42
REMARK 500    SER D 327      -11.06   -147.00
REMARK 500    THR D 401       -5.26    -54.53
REMARK 500    ASP D 419      -14.01    -48.57
REMARK 500    VAL D 451      -19.26    -44.88
REMARK 500    LYS D 477       10.72    -66.70
REMARK 500    MET D 478       -5.65   -159.25
REMARK 500    ALA D 480     -158.43   -138.68
REMARK 500    ILE E 373       89.06   -151.13
REMARK 500    LEU E 396       -3.14    -56.95
REMARK 500    THR E 401       12.10    -57.22
REMARK 500    ASN E 427       54.26   -144.25
REMARK 500    GLN E 437       23.84    -78.20
REMARK 500    ASN E 439       12.46     46.50
REMARK 500    ASP E 445      145.95   -170.15
REMARK 500    VAL E 451      -15.58    -48.80
REMARK 500    MET E 478      -19.13   -164.58
REMARK 500    GLU E 479       20.79    -79.60
REMARK 500    ALA E 480     -146.45   -140.47
REMARK 500    SER F 327      -24.68    -36.38
REMARK 500    ASP F 351       17.65   -140.41
REMARK 500    ASN F 427       47.41   -140.92
REMARK 500    ASN F 439       29.15     41.22
REMARK 500    LYS F 477       14.36    -65.80
REMARK 500    MET F 478      -20.78   -161.75
REMARK 500    ALA F 480     -142.48   -128.16
REMARK 500    GLN H 420      -68.19   -102.07
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 E6037        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH H6582        DISTANCE =  8.37 ANGSTROMS
REMARK 525    HOH G6746        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH H6695        DISTANCE =  7.53 ANGSTROMS
REMARK 525    HOH H6846        DISTANCE =  8.31 ANGSTROMS
REMARK 525    HOH H6906        DISTANCE =  9.03 ANGSTROMS
REMARK 525    HOH E6185        DISTANCE =  6.38 ANGSTROMS
REMARK 525    HOH E6310        DISTANCE =  8.89 ANGSTROMS
REMARK 525    HOH C6148        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH E6368        DISTANCE =  6.24 ANGSTROMS
REMARK 525    HOH D6442        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH D6447        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH E6409        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH A6369        DISTANCE =  5.52 ANGSTROMS
REMARK 525    HOH D6502        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH D6506        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH D6535        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH E6522        DISTANCE =  8.05 ANGSTROMS
REMARK 525    HOH E6523        DISTANCE =  6.56 ANGSTROMS
REMARK 525    HOH A6500        DISTANCE =  8.68 ANGSTROMS
REMARK 525    HOH A6504        DISTANCE =  6.23 ANGSTROMS
REMARK 525    HOH E6559        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH F6468        DISTANCE =  5.65 ANGSTROMS
REMARK 525    HOH D6657        DISTANCE =  5.81 ANGSTROMS
REMARK 525    HOH D6671        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH A6606        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH E6634        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH F6524        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH C6335        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH A6632        DISTANCE =  6.09 ANGSTROMS
REMARK 525    HOH A6641        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH B6520        DISTANCE =  7.21 ANGSTROMS
REMARK 525    HOH F6542        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH E6667        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH A6653        DISTANCE =  6.74 ANGSTROMS
REMARK 525    HOH E6694        DISTANCE =  6.64 ANGSTROMS
REMARK 525    HOH F6570        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH A6700        DISTANCE =  8.04 ANGSTROMS
REMARK 525    HOH E6731        DISTANCE =  7.51 ANGSTROMS
REMARK 525    HOH D6744        DISTANCE =  7.44 ANGSTROMS
REMARK 525    HOH E6753        DISTANCE =  6.37 ANGSTROMS
REMARK 525    HOH E6754        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH B6627        DISTANCE =  6.59 ANGSTROMS
REMARK 525    HOH C6463        DISTANCE =  5.63 ANGSTROMS
REMARK 525    HOH C6479        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH E6775        DISTANCE =  7.03 ANGSTROMS
REMARK 525    HOH B6658        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH F6654        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH D6810        DISTANCE =  9.13 ANGSTROMS
REMARK 525    HOH E6806        DISTANCE =  7.37 ANGSTROMS
REMARK 525    HOH A6823        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH B6711        DISTANCE =  9.30 ANGSTROMS
REMARK 525    HOH B6714        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH D6843        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH E6844        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH B6735        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH E6852        DISTANCE =  6.99 ANGSTROMS
REMARK 525    HOH D6881        DISTANCE =  5.61 ANGSTROMS
REMARK 525    HOH E6875        DISTANCE =  6.06 ANGSTROMS
REMARK 525    HOH C6593        DISTANCE =  6.05 ANGSTROMS
REMARK 525    HOH E6886        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH F6800        DISTANCE =  6.10 ANGSTROMS
REMARK 525    HOH E6894        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH F6838        DISTANCE =  5.99 ANGSTROMS
REMARK 525    HOH F6868        DISTANCE =  6.54 ANGSTROMS
REMARK 525    HOH F6883        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH C6729        DISTANCE =  7.82 ANGSTROMS
REMARK 525    HOH F6896        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH C6820        DISTANCE =  7.58 ANGSTROMS
REMARK 525    HOH C6887        DISTANCE =  9.38 ANGSTROMS
DBREF  1CA9 A  310   501  UNP    Q12933   TRAF2_HUMAN    310    501
DBREF  1CA9 B  310   501  UNP    Q12933   TRAF2_HUMAN    310    501
DBREF  1CA9 C  310   501  UNP    Q12933   TRAF2_HUMAN    310    501
DBREF  1CA9 D  310   501  UNP    Q12933   TRAF2_HUMAN    310    501
DBREF  1CA9 E  310   501  UNP    Q12933   TRAF2_HUMAN    310    501
DBREF  1CA9 F  310   501  UNP    Q12933   TRAF2_HUMAN    310    501
DBREF  1CA9 G  419   428  UNP    P20333   TNR1B_HUMAN    420    428
DBREF  1CA9 H  419   428  UNP    P20333   TNR1B_HUMAN    420    428
SEQRES   1 A  192  ASP GLN ASP LYS ILE GLU ALA LEU SER SER LYS VAL GLN
SEQRES   2 A  192  GLN LEU GLU ARG SER ILE GLY LEU LYS ASP LEU ALA MET
SEQRES   3 A  192  ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU ALA SER
SEQRES   4 A  192  THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER ASP PHE
SEQRES   5 A  192  ALA ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG ILE PRO
SEQRES   6 A  192  ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG TYR GLY
SEQRES   7 A  192  TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY ASP GLY
SEQRES   8 A  192  THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE VAL VAL
SEQRES   9 A  192  MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP PRO PHE
SEQRES  10 A  192  ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN ASN ASN
SEQRES  11 A  192  ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP VAL THR
SEQRES  12 A  192  SER SER SER PHE GLN ARG PRO VAL ASN ASP MET ASN ILE
SEQRES  13 A  192  ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER LYS MET
SEQRES  14 A  192  GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA ILE PHE
SEQRES  15 A  192  ILE LYS ALA ILE VAL ASP LEU THR GLY LEU
SEQRES   1 B  192  ASP GLN ASP LYS ILE GLU ALA LEU SER SER LYS VAL GLN
SEQRES   2 B  192  GLN LEU GLU ARG SER ILE GLY LEU LYS ASP LEU ALA MET
SEQRES   3 B  192  ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU ALA SER
SEQRES   4 B  192  THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER ASP PHE
SEQRES   5 B  192  ALA ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG ILE PRO
SEQRES   6 B  192  ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG TYR GLY
SEQRES   7 B  192  TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY ASP GLY
SEQRES   8 B  192  THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE VAL VAL
SEQRES   9 B  192  MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP PRO PHE
SEQRES  10 B  192  ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN ASN ASN
SEQRES  11 B  192  ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP VAL THR
SEQRES  12 B  192  SER SER SER PHE GLN ARG PRO VAL ASN ASP MET ASN ILE
SEQRES  13 B  192  ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER LYS MET
SEQRES  14 B  192  GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA ILE PHE
SEQRES  15 B  192  ILE LYS ALA ILE VAL ASP LEU THR GLY LEU
SEQRES   1 C  192  ASP GLN ASP LYS ILE GLU ALA LEU SER SER LYS VAL GLN
SEQRES   2 C  192  GLN LEU GLU ARG SER ILE GLY LEU LYS ASP LEU ALA MET
SEQRES   3 C  192  ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU ALA SER
SEQRES   4 C  192  THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER ASP PHE
SEQRES   5 C  192  ALA ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG ILE PRO
SEQRES   6 C  192  ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG TYR GLY
SEQRES   7 C  192  TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY ASP GLY
SEQRES   8 C  192  THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE VAL VAL
SEQRES   9 C  192  MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP PRO PHE
SEQRES  10 C  192  ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN ASN ASN
SEQRES  11 C  192  ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP VAL THR
SEQRES  12 C  192  SER SER SER PHE GLN ARG PRO VAL ASN ASP MET ASN ILE
SEQRES  13 C  192  ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER LYS MET
SEQRES  14 C  192  GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA ILE PHE
SEQRES  15 C  192  ILE LYS ALA ILE VAL ASP LEU THR GLY LEU
SEQRES   1 D  192  ASP GLN ASP LYS ILE GLU ALA LEU SER SER LYS VAL GLN
SEQRES   2 D  192  GLN LEU GLU ARG SER ILE GLY LEU LYS ASP LEU ALA MET
SEQRES   3 D  192  ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU ALA SER
SEQRES   4 D  192  THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER ASP PHE
SEQRES   5 D  192  ALA ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG ILE PRO
SEQRES   6 D  192  ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG TYR GLY
SEQRES   7 D  192  TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY ASP GLY
SEQRES   8 D  192  THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE VAL VAL
SEQRES   9 D  192  MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP PRO PHE
SEQRES  10 D  192  ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN ASN ASN
SEQRES  11 D  192  ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP VAL THR
SEQRES  12 D  192  SER SER SER PHE GLN ARG PRO VAL ASN ASP MET ASN ILE
SEQRES  13 D  192  ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER LYS MET
SEQRES  14 D  192  GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA ILE PHE
SEQRES  15 D  192  ILE LYS ALA ILE VAL ASP LEU THR GLY LEU
SEQRES   1 E  192  ASP GLN ASP LYS ILE GLU ALA LEU SER SER LYS VAL GLN
SEQRES   2 E  192  GLN LEU GLU ARG SER ILE GLY LEU LYS ASP LEU ALA MET
SEQRES   3 E  192  ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU ALA SER
SEQRES   4 E  192  THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER ASP PHE
SEQRES   5 E  192  ALA ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG ILE PRO
SEQRES   6 E  192  ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG TYR GLY
SEQRES   7 E  192  TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY ASP GLY
SEQRES   8 E  192  THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE VAL VAL
SEQRES   9 E  192  MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP PRO PHE
SEQRES  10 E  192  ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN ASN ASN
SEQRES  11 E  192  ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP VAL THR
SEQRES  12 E  192  SER SER SER PHE GLN ARG PRO VAL ASN ASP MET ASN ILE
SEQRES  13 E  192  ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER LYS MET
SEQRES  14 E  192  GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA ILE PHE
SEQRES  15 E  192  ILE LYS ALA ILE VAL ASP LEU THR GLY LEU
SEQRES   1 F  192  ASP GLN ASP LYS ILE GLU ALA LEU SER SER LYS VAL GLN
SEQRES   2 F  192  GLN LEU GLU ARG SER ILE GLY LEU LYS ASP LEU ALA MET
SEQRES   3 F  192  ALA ASP LEU GLU GLN LYS VAL LEU GLU MET GLU ALA SER
SEQRES   4 F  192  THR TYR ASP GLY VAL PHE ILE TRP LYS ILE SER ASP PHE
SEQRES   5 F  192  ALA ARG LYS ARG GLN GLU ALA VAL ALA GLY ARG ILE PRO
SEQRES   6 F  192  ALA ILE PHE SER PRO ALA PHE TYR THR SER ARG TYR GLY
SEQRES   7 F  192  TYR LYS MET CYS LEU ARG ILE TYR LEU ASN GLY ASP GLY
SEQRES   8 F  192  THR GLY ARG GLY THR HIS LEU SER LEU PHE PHE VAL VAL
SEQRES   9 F  192  MET LYS GLY PRO ASN ASP ALA LEU LEU ARG TRP PRO PHE
SEQRES  10 F  192  ASN GLN LYS VAL THR LEU MET LEU LEU ASP GLN ASN ASN
SEQRES  11 F  192  ARG GLU HIS VAL ILE ASP ALA PHE ARG PRO ASP VAL THR
SEQRES  12 F  192  SER SER SER PHE GLN ARG PRO VAL ASN ASP MET ASN ILE
SEQRES  13 F  192  ALA SER GLY CYS PRO LEU PHE CYS PRO VAL SER LYS MET
SEQRES  14 F  192  GLU ALA LYS ASN SER TYR VAL ARG ASP ASP ALA ILE PHE
SEQRES  15 F  192  ILE LYS ALA ILE VAL ASP LEU THR GLY LEU
SEQRES   1 G   10  GLY GLN VAL PRO PHE SER LYS GLU GLU CYS
SEQRES   1 H   10  GLY GLN VAL PRO PHE SER LYS GLU GLU CYS
FORMUL   9  HOH   *910(H2 O)
HELIX    1   1 GLU A  315  SER A  318  1                                   4
HELIX    2   2 LYS A  320  ALA A  347  1                                  28
HELIX    3   3 PHE A  361  VAL A  369  1                                   9
HELIX    4   4 GLY A  400  GLY A  402  5                                   3
HELIX    5   5 ASP A  419  LEU A  421  5                                   3
HELIX    6   6 SER A  454  PHE A  456  5                                   3
HELIX    7   7 VAL A  475  GLU A  479  5                                   5
HELIX    8   8 ASP B  312  ALA B  347  1                                  36
HELIX    9   9 PHE B  361  VAL B  369  1                                   9
HELIX   10  10 GLY B  400  GLY B  402  5                                   3
HELIX   11  11 ASP B  419  LEU B  421  5                                   3
HELIX   12  12 VAL B  475  LYS B  477  5                                   3
HELIX   13  13 ASP C  312  ALA C  347  1                                  36
HELIX   14  14 PHE C  361  VAL C  369  1                                   9
HELIX   15  15 GLY C  400  GLY C  402  5                                   3
HELIX   16  16 ASP C  419  LEU C  421  5                                   3
HELIX   17  17 SER C  454  PHE C  456  5                                   3
HELIX   18  18 VAL C  475  LYS C  477  5                                   3
HELIX   19  19 LEU D  317  GLU D  325  1                                   9
HELIX   20  20 ILE D  328  ALA D  347  1                                  20
HELIX   21  21 PHE D  361  VAL D  369  1                                   9
HELIX   22  22 GLY D  400  GLY D  402  5                                   3
HELIX   23  23 SER D  454  PHE D  456  5                                   3
HELIX   24  24 VAL D  475  LYS D  477  5                                   3
HELIX   25  25 LEU E  317  ALA E  347  1                                  31
HELIX   26  26 PHE E  361  VAL E  369  1                                   9
HELIX   27  27 GLY E  400  GLY E  402  5                                   3
HELIX   28  28 ASP E  419  LEU E  421  5                                   3
HELIX   29  29 VAL E  475  LYS E  477  5                                   3
HELIX   30  30 SER F  319  ALA F  347  1                                  29
HELIX   31  31 PHE F  361  VAL F  369  1                                   9
HELIX   32  32 GLY F  400  GLY F  402  5                                   3
HELIX   33  33 ASP F  419  LEU F  421  5                                   3
HELIX   34  34 SER F  454  PHE F  456  5                                   3
HELIX   35  35 VAL F  475  LYS F  477  5                                   3
SHEET    1   A 4 VAL A 353  SER A 359  0
SHEET    2   A 4 ALA A 489  VAL A 496 -1  N  ALA A 494   O  PHE A 354
SHEET    3   A 4 VAL A 430  LEU A 434 -1  N  MET A 433   O  LYS A 493
SHEET    4   A 4 VAL A 443  PHE A 447 -1  N  PHE A 447   O  VAL A 430
SHEET    1   B 3 LYS A 389  TYR A 395  0
SHEET    2   B 3 SER A 408  MET A 414 -1  N  MET A 414   O  LYS A 389
SHEET    3   B 3 SER A 467  CYS A 469 -1  N  CYS A 469   O  LEU A 409
SHEET    1   C 4 VAL B 353  SER B 359  0
SHEET    2   C 4 ALA B 489  VAL B 496 -1  N  ALA B 494   O  PHE B 354
SHEET    3   C 4 VAL B 430  LEU B 434 -1  N  MET B 433   O  LYS B 493
SHEET    4   C 4 VAL B 443  PHE B 447 -1  N  PHE B 447   O  VAL B 430
SHEET    1   D 3 LYS B 389  TYR B 395  0
SHEET    2   D 3 SER B 408  MET B 414 -1  N  MET B 414   O  LYS B 389
SHEET    3   D 3 SER B 467  CYS B 469 -1  N  CYS B 469   O  LEU B 409
SHEET    1   E 4 VAL C 353  SER C 359  0
SHEET    2   E 4 ALA C 489  VAL C 496 -1  N  ALA C 494   O  PHE C 354
SHEET    3   E 4 VAL C 430  LEU C 434 -1  N  MET C 433   O  LYS C 493
SHEET    4   E 4 VAL C 443  PHE C 447 -1  N  PHE C 447   O  VAL C 430
SHEET    1   F 4 ALA C 375  PHE C 377  0
SHEET    2   F 4 LYS C 389  TYR C 395 -1  N  ILE C 394   O  ILE C 376
SHEET    3   F 4 SER C 408  MET C 414 -1  N  MET C 414   O  LYS C 389
SHEET    4   F 4 SER C 467  CYS C 469 -1  N  CYS C 469   O  LEU C 409
SHEET    1   G 4 VAL D 353  ILE D 358  0
SHEET    2   G 4 ILE D 490  VAL D 496 -1  N  ALA D 494   O  PHE D 354
SHEET    3   G 4 VAL D 430  LEU D 434 -1  N  MET D 433   O  LYS D 493
SHEET    4   G 4 VAL D 443  PHE D 447 -1  N  PHE D 447   O  VAL D 430
SHEET    1   H 3 LYS D 389  TYR D 395  0
SHEET    2   H 3 SER D 408  MET D 414 -1  N  MET D 414   O  LYS D 389
SHEET    3   H 3 SER D 467  CYS D 469 -1  N  CYS D 469   O  LEU D 409
SHEET    1   I 4 VAL E 353  SER E 359  0
SHEET    2   I 4 ALA E 489  VAL E 496 -1  N  ALA E 494   O  PHE E 354
SHEET    3   I 4 VAL E 430  LEU E 434 -1  N  MET E 433   O  LYS E 493
SHEET    4   I 4 VAL E 443  PHE E 447 -1  N  PHE E 447   O  VAL E 430
SHEET    1   J 4 ALA E 375  PHE E 377  0
SHEET    2   J 4 LYS E 389  TYR E 395 -1  N  ILE E 394   O  ILE E 376
SHEET    3   J 4 SER E 408  MET E 414 -1  N  MET E 414   O  LYS E 389
SHEET    4   J 4 SER E 467  CYS E 469 -1  N  CYS E 469   O  LEU E 409
SHEET    1   K 4 VAL F 353  SER F 359  0
SHEET    2   K 4 ALA F 489  VAL F 496 -1  N  ALA F 494   O  PHE F 354
SHEET    3   K 4 VAL F 430  LEU F 434 -1  N  MET F 433   O  LYS F 493
SHEET    4   K 4 VAL F 443  PHE F 447 -1  N  PHE F 447   O  VAL F 430
SHEET    1   L 3 LYS F 389  TYR F 395  0
SHEET    2   L 3 SER F 408  MET F 414 -1  N  MET F 414   O  LYS F 389
SHEET    3   L 3 SER F 467  CYS F 469 -1  N  CYS F 469   O  LEU F 409
CISPEP   1 TRP A  424    PRO A  425          0        -0.61
CISPEP   2 TRP B  424    PRO B  425          0         0.27
CISPEP   3 TRP C  424    PRO C  425          0         0.20
CISPEP   4 TRP D  424    PRO D  425          0        -0.05
CISPEP   5 TRP E  424    PRO E  425          0         0.07
CISPEP   6 TRP F  424    PRO F  425          0        -0.28
CRYST1   83.000   84.400  100.700  90.00 108.70  90.00 P 1 21 1     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      0.012048  0.000000  0.004078        0.00000
SCALE2      0.000000  0.011848  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010484        0.00000
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1
      
PROCHECK
Go to PROCHECK summary
 References