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PDBsum entry 2iam

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Immune system PDB id
2iam
Jmol
Contents
Protein chains
179 a.a.
182 a.a.
15 a.a.
198 a.a.
239 a.a.
Waters ×40
HEADER    IMMUNE SYSTEM                           08-SEP-06   2IAM
TITLE     STRUCTURAL BASIS FOR RECOGNITION OF MUTANT SELF BY A TUMOR-
TITLE    2 SPECIFIC, MHC CLASS II-RESTRICTED TCR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR
COMPND   3 ALPHA CHAIN;
COMPND   4 CHAIN: A;
COMPND   5 FRAGMENT: RESIDUES 1-182 (26-207);
COMPND   6 SYNONYM: MHC CLASS II ANTIGEN DRA, MAJOR
COMPND   7 HISTOCOMPATIBILITY COMPLEX CLASS II HLA-DR1 ALPHA CHAIN;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1
COMPND  11 BETA CHAIN;
COMPND  12 CHAIN: B;
COMPND  13 FRAGMENT: RESIDUES 1-190 (30-219);
COMPND  14 SYNONYM: MHC CLASS I ANTIGEN DRB1*1, DR-1, DR1, MAJOR
COMPND  15 HISTOCOMPATIBILITY COMPLEX CLASS II HLA-DR1 BETA CHAIN;
COMPND  16 ENGINEERED: YES;
COMPND  17 MOL_ID: 3;
COMPND  18 MOLECULE: 15-MER PEPTIDE FROM TRIOSEPHOSPHATE ISOMERASE;
COMPND  19 CHAIN: P;
COMPND  20 FRAGMENT: RESIDUES 23-37 (22-36);
COMPND  21 EC: 5.3.1.1;
COMPND  22 ENGINEERED: YES;
COMPND  23 MUTATION: YES;
COMPND  24 MOL_ID: 4;
COMPND  25 MOLECULE: CD4+ T CELL RECEPTOR E8 ALPHA CHAIN;
COMPND  26 CHAIN: C;
COMPND  27 ENGINEERED: YES;
COMPND  28 MUTATION: YES;
COMPND  29 MOL_ID: 5;
COMPND  30 MOLECULE: CD4+ T CELL RECEPTOR E8 BETA CHAIN;
COMPND  31 CHAIN: D;
COMPND  32 ENGINEERED: YES;
COMPND  33 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DRA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 GENE: HLA-DRB1;
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE  21 MOL_ID: 3;
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  23 ORGANISM_COMMON: HUMAN;
SOURCE  24 ORGANISM_TAXID: 9606;
SOURCE  25 GENE: TPI1, TPI;
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE  31 MOL_ID: 4;
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  33 ORGANISM_COMMON: HUMAN;
SOURCE  34 ORGANISM_TAXID: 9606;
SOURCE  35 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE  36 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE  37 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  38 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  39 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE  40 MOL_ID: 5;
SOURCE  41 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  42 ORGANISM_COMMON: HUMAN;
SOURCE  43 ORGANISM_TAXID: 9606;
SOURCE  44 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE  45 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE  46 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  47 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  48 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS    X-RAY CRYSTALLOGRAPHY, MAJOR HISTOCOMPATIBILITY COMPLEX, T
KEYWDS   2 CELL RECEPTOR, T CELL STIMULATION, MELANOMA, TUMOR ANTIGEN,
KEYWDS   3 IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.DENG,R.J.LANGLEY,R.A.MARIUZZA
REVDAT   2   24-FEB-09 2IAM    1       VERSN
REVDAT   1   03-APR-07 2IAM    0
JRNL        AUTH   L.DENG,R.J.LANGLEY,P.H.BROWN,G.XU,L.TENG,Q.WANG,
JRNL        AUTH 2 M.I.GONZALES,G.G.CALLENDER,M.I.NISHIMURA,
JRNL        AUTH 3 S.L.TOPALIAN,R.A.MARIUZZA
JRNL        TITL   STRUCTURAL BASIS FOR THE RECOGNITION OF MUTANT
JRNL        TITL 2 SELF BY A TUMOR-SPECIFIC, MHC CLASS II-RESTRICTED
JRNL        TITL 3 T CELL RECEPTOR
JRNL        REF    NAT.IMMUNOL.                  V.   8   398 2007
JRNL        REFN                   ISSN 1529-2908
JRNL        PMID   17334368
JRNL        DOI    10.1038/NI1447
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.91
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.2
REMARK   3   NUMBER OF REFLECTIONS             : 25046
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 + TEST SET) : 0.211
REMARK   3   R VALUE            (WORKING SET) : 0.207
REMARK   3   FREE R VALUE                     : 0.279
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1329
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1825
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.50
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720
REMARK   3   BIN FREE R VALUE SET COUNT          : 90
REMARK   3   BIN FREE R VALUE                    : 0.3720
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6511
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 40
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -5.39000
REMARK   3    B22 (A**2) : 4.95000
REMARK   3    B33 (A**2) : 0.43000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.747
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.362
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.270
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.523
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6689 ; 0.019 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9110 ; 1.960 ; 1.936
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   807 ;10.920 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   340 ;38.547 ;24.265
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1060 ;21.109 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;18.690 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   983 ; 0.117 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5221 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2923 ; 0.253 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4441 ; 0.322 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   266 ; 0.178 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    45 ; 0.256 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.043 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4164 ; 0.752 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6594 ; 1.278 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2909 ; 1.908 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2516 ; 2.944 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2IAM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-SEP-06.
REMARK 100 THE RCSB ID CODE IS RCSB039345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-AUG-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
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 : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26581
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
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     (%) : 92.8
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.09100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.94
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.51300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1FYT, 1IAL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG6000, 0.1M DI-AMMONIUM
REMARK 280  PHOSPHATE, 0.1M TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z
REMARK 290       7555   -X+1/2,Y+1/2,-Z
REMARK 290       8555   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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       43.19550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      135.27100
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.19550
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      135.27100
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.19550
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      135.27100
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.19550
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      135.27100
REMARK 290   SMTRY3   8  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 300 REMARK: EACH ASYMMETRIC UNIT CONTAINS ONE BIOLOGICAL UNIT.
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: 13960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, C, D
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     ILE A     1
REMARK 465     LYS A     2
REMARK 465     ALA A   182
REMARK 465     LYS B   105
REMARK 465     THR B   106
REMARK 465     GLN B   107
REMARK 465     PRO B   108
REMARK 465     LEU B   109
REMARK 465     GLN B   110
REMARK 465     HIS B   111
REMARK 465     HIS B   112
REMARK 465     PRO C   199
REMARK 465     GLU C   200
REMARK 465     SER C   201
REMARK 465     SER C   202
REMARK 465     ASN D     1
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    GLU A 179   CD    GLU A 179   OE1     0.067
REMARK 500    GLU B 169   CD    GLU B 169   OE1     0.106
REMARK 500    GLU B 169   CD    GLU B 169   OE2     0.401
REMARK 500    ALA B 190   C     ALA B 190   O       0.135
REMARK 500    CYS C  86   CB    CYS C  86   SG     -0.123
REMARK 500    GLU D 111   CG    GLU D 111   CD      0.114
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    PRO A 114   C   -  N   -  CA  ANGL. DEV. =  17.4 DEGREES
REMARK 500    PRO A 114   C   -  N   -  CD  ANGL. DEV. = -16.3 DEGREES
REMARK 500    GLN C  94   C   -  N   -  CA  ANGL. DEV. = -15.5 DEGREES
REMARK 500    CYS C 156   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES
REMARK 500    ARG D 183   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 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    GLU A   4      -52.28   -167.19
REMARK 500    VAL A   6      117.48   -164.02
REMARK 500    ASN A  94      -73.33    -60.73
REMARK 500    PRO A  96      100.76    -47.12
REMARK 500    VAL A  97       91.38    -57.75
REMARK 500    LEU A  99      128.53    -30.59
REMARK 500    PRO A 102      126.04    -38.94
REMARK 500    PRO A 114      126.75     24.51
REMARK 500    PRO A 115       69.96    -65.90
REMARK 500    GLU A 134      146.49   -173.40
REMARK 500    VAL A 136     -154.29    -95.77
REMARK 500    HIS A 143        4.78     90.21
REMARK 500    PRO A 173      135.36    -39.94
REMARK 500    ASP B   2      177.79    -35.13
REMARK 500    THR B   3     -175.07    166.61
REMARK 500    ASN B  19       76.52     47.04
REMARK 500    GLN B  34       10.50     81.73
REMARK 500    GLU B  87      -61.05     -8.11
REMARK 500    TYR B 102      161.65    179.95
REMARK 500    TYR B 123      101.90   -164.37
REMARK 500    THR B 145       -9.85    -59.03
REMARK 500    GLU B 169      126.57      5.21
REMARK 500    PRO B 178        5.59    -69.04
REMARK 500    ALA P  31      131.21    -37.57
REMARK 500    SER C   6     -151.47    -76.15
REMARK 500    ASN C  30       66.86     70.45
REMARK 500    ILE C  48       70.03   -156.94
REMARK 500    ASN C  55       81.22   -154.32
REMARK 500    GLU C  66       -5.71   -144.28
REMARK 500    ARG C  67       46.79     72.30
REMARK 500    GLN C  94       55.04   -106.29
REMARK 500    PRO C 113      131.71    -39.52
REMARK 500    SER C 125      112.38     74.32
REMARK 500    ASP C 127      -70.10    -32.63
REMARK 500    LYS C 176     -161.24    -66.18
REMARK 500    SER C 177        8.06   -158.64
REMARK 500    ASN C 186       11.16    -63.75
REMARK 500    GLU C 192      -38.22    -21.05
REMARK 500    PRO C 197      165.68    -20.12
REMARK 500    PRO D   8      102.18     19.48
REMARK 500    VAL D  60       44.59   -143.38
REMARK 500    PRO D  61        0.19    -61.95
REMARK 500    THR D  71      -43.23    -25.42
REMARK 500    TYR D  95      -68.68   -158.01
REMARK 500    PRO D 148      139.77      3.58
REMARK 500    ASP D 149       43.74    -55.71
REMARK 500    ASN D 158       58.43     38.14
REMARK 500    ALA D 178      -70.04    -70.48
REMARK 500    LEU D 179      132.49    -34.73
REMARK 500    ASP D 181       59.13    -90.71
REMARK 500    ALA D 239       11.91    -64.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 THR A  113     PRO A  114                 -102.24
REMARK 500 THR B    3     ARG B    4                 -149.62
REMARK 500 TYR B  123     PRO B  124                   77.95
REMARK 500 ILE C    1     GLN C    2                 -144.53
REMARK 500 SER C    6     PRO C    7                 -120.30
REMARK 500 THR D    7     PRO D    8                 -102.69
REMARK 500 SER D   18     MET D   19                 -144.58
REMARK 500 PHE D  147     PRO D  148                  -75.48
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    GLU B 169         0.07    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KLU   RELATED DB: PDB
REMARK 900 UNBOUND FORM OF E8 LIGAND
REMARK 900 RELATED ID: 1KLG   RELATED DB: PDB
REMARK 900 UNBOUND FORM OF E8 LIGAND
REMARK 900 RELATED ID: 2IAL   RELATED DB: PDB
REMARK 900 CD4+ T CELL RECEPTOR E8
REMARK 900 RELATED ID: 2IAN   RELATED DB: PDB
REMARK 900 THE SAME COMPLEX IN DIFFERENT SPACE GROUP
DBREF  2IAM A    1   182  UNP    P01903   2DRA_HUMAN      26    207
DBREF  2IAM B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  2IAM P   23    37  UNP    P60174   TPIS_HUMAN      22     36
DBREF  2IAM C  108   202  UNP    P01848   TCA_HUMAN        1     95
DBREF  2IAM D  111   240  UNP    P01850   TCB_HUMAN        1    130
SEQADV 2IAM ILE P   28  UNP  P60174    THR    27 ENGINEERED
SEQRES   1 A  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 A  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 A  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 A  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 A  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 A  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 A  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 A  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 A  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 A  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 A  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 A  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 A  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 A  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 B  190  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 B  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 B  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 B  190  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 B  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 B  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 B  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 B  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 B  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 B  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 B  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 B  190  PRO LEU THR VAL GLU TRP ARG ALA
SEQRES   1 P   15  GLY GLU LEU ILE GLY ILE LEU ASN ALA ALA LYS VAL PRO
SEQRES   2 P   15  ALA ASP
SEQRES   1 C  202  ILE GLN VAL GLU GLN SER PRO PRO ASP LEU ILE LEU GLN
SEQRES   2 C  202  GLU GLY ALA ASN SER THR LEU ARG CYS ASN PHE SER ASP
SEQRES   3 C  202  SER VAL ASN ASN LEU GLN TRP PHE HIS GLN ASN PRO TRP
SEQRES   4 C  202  GLY GLN LEU ILE ASN LEU PHE TYR ILE PRO SER GLY THR
SEQRES   5 C  202  LYS GLN ASN GLY ARG LEU SER ALA THR THR VAL ALA THR
SEQRES   6 C  202  GLU ARG TYR SER LEU LEU TYR ILE SER SER SER GLN THR
SEQRES   7 C  202  THR ASP SER GLY VAL TYR PHE CYS ALA ALA LEU ILE GLN
SEQRES   8 C  202  GLY ALA GLN LYS LEU VAL PHE GLY GLN GLY THR ARG LEU
SEQRES   9 C  202  THR ILE ASN PRO ASN ILE GLN ASN PRO ASP PRO ALA VAL
SEQRES  10 C  202  TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER VAL
SEQRES  11 C  202  CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL SER
SEQRES  12 C  202  GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS CYS
SEQRES  13 C  202  VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN SER
SEQRES  14 C  202  ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS ALA
SEQRES  15 C  202  ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR PHE
SEQRES  16 C  202  PHE PRO SER PRO GLU SER SER
SEQRES   1 D  240  ASN ALA GLY VAL THR GLN THR PRO LYS PHE ARG ILE LEU
SEQRES   2 D  240  LYS ILE GLY GLN SER MET THR LEU GLN CYS THR GLN ASP
SEQRES   3 D  240  MET ASN HIS ASN TYR MET TYR TRP TYR ARG GLN ASP PRO
SEQRES   4 D  240  GLY MET GLY LEU LYS LEU ILE TYR TYR SER VAL GLY ALA
SEQRES   5 D  240  GLY ILE THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN
SEQRES   6 D  240  VAL SER ARG SER THR THR GLU ASP PHE PRO LEU ARG LEU
SEQRES   7 D  240  GLU LEU ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES   8 D  240  ALA SER THR TYR HIS GLY THR GLY TYR PHE GLY GLU GLY
SEQRES   9 D  240  SER TRP LEU THR VAL VAL GLU ASP LEU ASN LYS VAL PHE
SEQRES  10 D  240  PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU ALA GLU
SEQRES  11 D  240  ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS LEU ALA
SEQRES  12 D  240  THR GLY PHE PHE PRO ASP HIS VAL GLU LEU SER TRP TRP
SEQRES  13 D  240  VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS THR ASP
SEQRES  14 D  240  PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN ASP SER
SEQRES  15 D  240  ARG TYR ALA LEU SER SER ARG LEU ARG VAL SER ALA THR
SEQRES  16 D  240  PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS GLN VAL
SEQRES  17 D  240  GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP THR GLN
SEQRES  18 D  240  ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER ALA GLU
SEQRES  19 D  240  ALA TRP GLY ARG ALA ASP
FORMUL   6  HOH   *40(H2 O)
HELIX    1   1 LEU A   45  PHE A   51  1                                   7
HELIX    2   2 ALA A   56  SER A   77  1                                  22
HELIX    3   3 GLY B   54  ASN B   62  1                                   9
HELIX    4   4 GLN B   64  ARG B   72  1                                   9
HELIX    5   5 ALA B   73  TYR B   78  1                                   6
HELIX    6   6 TYR B   78  GLU B   87  1                                  10
HELIX    7   7 ALA C   64  GLU C   66  5                                   3
HELIX    8   8 GLN C   77  SER C   81  5                                   5
HELIX    9   9 ARG C  161  ASP C  164  5                                   4
HELIX   10  10 ALA D   82  THR D   86  5                                   5
HELIX   11  11 ASP D  112  VAL D  116  5                                   5
HELIX   12  12 SER D  127  GLN D  135  1                                   9
HELIX   13  13 ALA D  194  ASN D  199  1                                   6
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 GLU A  30  ASP A  35 -1  N  HIS A  33   O  VAL A  42
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  24   O  ILE A  31
SHEET    4   A 8 HIS A   5  LEU A  14 -1  N  ILE A   8   O  ASP A  25
SHEET    5   A 8 LEU B   8  PHE B  18 -1  O  PHE B  13   N  GLN A   9
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  LEU B  27   N  GLU B  14
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  PHE B  40   N  GLU B  28
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   B 2 ALA A  52  SER A  53  0
SHEET    2   B 2 GLU P  24  LEU P  25  1  O  GLU P  24   N  SER A  53
SHEET    1   C 4 GLU A  88  THR A  93  0
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  PHE A 153   N  ASN A 103
SHEET    4   C 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150
SHEET    1   D 4 GLU A  88  THR A  93  0
SHEET    2   D 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3   D 4 PHE A 145  PHE A 153 -1  O  PHE A 153   N  ASN A 103
SHEET    4   D 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146
SHEET    1   E 4 LYS A 126  PRO A 127  0
SHEET    2   E 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126
SHEET    3   E 4 TYR A 161  GLU A 166 -1  O  ARG A 164   N  THR A 120
SHEET    4   E 4 LEU A 174  TRP A 178 -1  O  TRP A 178   N  TYR A 161
SHEET    1   F 4 LYS B  98  PRO B 103  0
SHEET    2   F 4 LEU B 114  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3   F 4 PHE B 155  GLU B 162 -1  O  VAL B 159   N  CYS B 117
SHEET    4   F 4 VAL B 142  GLN B 149 -1  N  VAL B 143   O  MET B 160
SHEET    1   G 4 GLN B 136  GLU B 137  0
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136
SHEET    3   G 4 VAL B 170  GLU B 176 -1  O  THR B 172   N  PHE B 132
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  TRP B 188   N  TYR B 171
SHEET    1   H 5 VAL C   3  GLN C   5  0
SHEET    2   H 5 SER C  18  PHE C  24 -1  O  ASN C  23   N  GLU C   4
SHEET    3   H 5 TYR C  68  ILE C  73 -1  O  LEU C  71   N  LEU C  20
SHEET    4   H 5 LEU C  58  THR C  62 -1  N  SER C  59   O  TYR C  72
SHEET    5   H 5 GLY C  51  ASN C  55 -1  N  ASN C  55   O  LEU C  58
SHEET    1   I 5 ASP C   9  GLN C  13  0
SHEET    2   I 5 THR C 102  ASN C 107  1  O  THR C 105   N  LEU C  10
SHEET    3   I 5 GLY C  82  ILE C  90 -1  N  GLY C  82   O  LEU C 104
SHEET    4   I 5 VAL C  28  GLN C  36 -1  N  ASN C  29   O  LEU C  89
SHEET    5   I 5 LEU C  42  TYR C  47 -1  O  ILE C  43   N  HIS C  35
SHEET    1   J 4 ASP C   9  GLN C  13  0
SHEET    2   J 4 THR C 102  ASN C 107  1  O  THR C 105   N  LEU C  10
SHEET    3   J 4 GLY C  82  ILE C  90 -1  N  GLY C  82   O  LEU C 104
SHEET    4   J 4 LEU C  96  PHE C  98 -1  O  VAL C  97   N  ALA C  88
SHEET    1   K 8 TYR C 151  ILE C 152  0
SHEET    2   K 8 PHE C 165  TRP C 173 -1  O  TRP C 173   N  TYR C 151
SHEET    3   K 8 SER C 129  THR C 134 -1  N  CYS C 131   O  ALA C 172
SHEET    4   K 8 ALA C 116  ASP C 122 -1  N  ALA C 116   O  THR C 134
SHEET    5   K 8 GLU D 120  GLU D 125 -1  O  GLU D 125   N  ARG C 121
SHEET    6   K 8 LYS D 136  PHE D 146 -1  O  VAL D 140   N  PHE D 124
SHEET    7   K 8 TYR D 184  SER D 193 -1  O  LEU D 190   N  LEU D 139
SHEET    8   K 8 VAL D 166  THR D 168 -1  N  CYS D 167   O  ARG D 189
SHEET    1   L 8 CYS C 156  MET C 160  0
SHEET    2   L 8 PHE C 165  TRP C 173 -1  O  PHE C 165   N  MET C 160
SHEET    3   L 8 SER C 129  THR C 134 -1  N  CYS C 131   O  ALA C 172
SHEET    4   L 8 ALA C 116  ASP C 122 -1  N  ALA C 116   O  THR C 134
SHEET    5   L 8 GLU D 120  GLU D 125 -1  O  GLU D 125   N  ARG C 121
SHEET    6   L 8 LYS D 136  PHE D 146 -1  O  VAL D 140   N  PHE D 124
SHEET    7   L 8 TYR D 184  SER D 193 -1  O  LEU D 190   N  LEU D 139
SHEET    8   L 8 LEU D 173  LYS D 174 -1  N  LEU D 173   O  ALA D 185
SHEET    1   M 4 VAL D   4  THR D   7  0
SHEET    2   M 4 MET D  19  GLN D  25 -1  O  THR D  24   N  THR D   5
SHEET    3   M 4 LEU D  76  LEU D  78 -1  O  LEU D  76   N  LEU D  21
SHEET    4   M 4 TYR D  64  VAL D  66 -1  N  ASN D  65   O  ARG D  77
SHEET    1   N 6 PHE D  10  LYS D  14  0
SHEET    2   N 6 SER D 105  VAL D 110  1  O  THR D 108   N  ARG D  11
SHEET    3   N 6 SER D  87  THR D  94 -1  N  TYR D  89   O  SER D 105
SHEET    4   N 6 TYR D  31  GLN D  37 -1  N  TYR D  33   O  ALA D  92
SHEET    5   N 6 LEU D  43  GLY D  51 -1  O  LYS D  44   N  ARG D  36
SHEET    6   N 6 ILE D  54  LYS D  57 -1  O  ASP D  56   N  TYR D  48
SHEET    1   O 4 PHE D  10  LYS D  14  0
SHEET    2   O 4 SER D 105  VAL D 110  1  O  THR D 108   N  ARG D  11
SHEET    3   O 4 SER D  87  THR D  94 -1  N  TYR D  89   O  SER D 105
SHEET    4   O 4 TYR D 100  PHE D 101 -1  O  TYR D 100   N  SER D  93
SHEET    1   P 4 LYS D 160  GLU D 161  0
SHEET    2   P 4 VAL D 151  VAL D 157 -1  N  VAL D 157   O  LYS D 160
SHEET    3   P 4 HIS D 203  PHE D 210 -1  O  GLN D 207   N  SER D 154
SHEET    4   P 4 GLN D 229  TRP D 236 -1  O  GLN D 229   N  PHE D 210
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.07
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.04
SSBOND   4 CYS C   22    CYS C   86                          1555   1555  2.08
SSBOND   5 CYS C  131    CYS C  181                          1555   1555  2.10
SSBOND   6 CYS C  156    CYS D  167                          1555   1555  2.05
SSBOND   7 CYS D   23    CYS D   91                          1555   1555  1.99
SSBOND   8 CYS D  141    CYS D  206                          1555   1555  2.00
CRYST1   86.391  270.542   97.396  90.00  90.00  90.00 C 2 2 2       8
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      0.011575  0.000000  0.000000        0.00000
SCALE2      0.000000  0.003696  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010267        0.00000
      
PROCHECK
Go to PROCHECK summary
 References