spacer
spacer

PDBsum entry 2xn9

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Immune system PDB id
2xn9
Jmol
Contents
Protein chains
199 a.a.
242 a.a.
215 a.a.
178 a.a.
188 a.a.
13 a.a.
Ligands
GOL ×4
Metals
_NA
Waters ×280
HEADER    IMMUNE SYSTEM                           31-JUL-10   2XN9
TITLE     CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN HUMAN T CELL
TITLE    2 RECEPTOR, STAPHYLOCOCCAL ENTEROTOXIN H AND HUMAN MAJOR
TITLE    3 HISTOCOMPATIBILITY COMPLEX CLASS II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: T CELL RECEPTOR ALPHA CHAIN C REGION;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 1-95;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES;
COMPND   7 OTHER_DETAILS: VARIABLE DOMAIN TRAV27 FUSED TO CONSTANT DOMAIN;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: T CELL RECEPTOR BETA-1 CHAIN C REGION;
COMPND  10 CHAIN: B;
COMPND  11 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 1-130;
COMPND  12 ENGINEERED: YES;
COMPND  13 MUTATION: YES;
COMPND  14 OTHER_DETAILS: VARIABLE DOMAIN TRBV19 FUSED TO CONSTANT DOMAIN;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: ENTEROTOXIN H;
COMPND  17 CHAIN: C;
COMPND  18 SYNONYM: SEH, STAPHYLOCOCCAL ENTEROTOXIN H;
COMPND  19 ENGINEERED: YES;
COMPND  20 MOL_ID: 4;
COMPND  21 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN,;
COMPND  22 CHAIN: D;
COMPND  23 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 26-207;
COMPND  24 SYNONYM: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS II ALPHA, MHC CLASS
COMPND  25  II ANTIGEN DRA CHAIN;
COMPND  26 ENGINEERED: YES;
COMPND  27 OTHER_DETAILS: CHAIN DR 0101;
COMPND  28 MOL_ID: 5;
COMPND  29 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS II BETA CHAIN;
COMPND  30 CHAIN: E;
COMPND  31 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 30-219;
COMPND  32 SYNONYM: MHC CLASS II ANTIGEN DRB1.1, DR-1, DR1;
COMPND  33 ENGINEERED: YES;
COMPND  34 OTHER_DETAILS: CHAIN DRB1 0101;
COMPND  35 MOL_ID: 6;
COMPND  36 MOLECULE: HEMAGGLUTININ;
COMPND  37 CHAIN: F;
COMPND  38 FRAGMENT: RESIDUES 59-71;
COMPND  39 SYNONYM: INFLUENZA HEMAGGLUTININ PEPTIDE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL: T LYMPHOCYTE;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGMT7;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  12 ORGANISM_COMMON: HUMAN;
SOURCE  13 ORGANISM_TAXID: 9606;
SOURCE  14 CELL: T LYMPHOCYTE;
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PGMT7;
SOURCE  19 MOL_ID: 3;
SOURCE  20 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE  21 ORGANISM_TAXID: 1280;
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE  24 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE  25 EXPRESSION_SYSTEM_VARIANT: UL635;
SOURCE  26 MOL_ID: 4;
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  28 ORGANISM_COMMON: HUMAN;
SOURCE  29 ORGANISM_TAXID: 9606;
SOURCE  30 CELL: ANTIGEN PRESENTING CELL;
SOURCE  31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  33 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE  34 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE  35 MOL_ID: 5;
SOURCE  36 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  37 ORGANISM_COMMON: HUMAN;
SOURCE  38 ORGANISM_TAXID: 9606;
SOURCE  39 CELL: ANTIGEN PRESENTING CELL;
SOURCE  40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  41 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  42 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  43 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE  44 MOL_ID: 6;
SOURCE  45 SYNTHETIC: YES;
SOURCE  46 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE  47 ORGANISM_TAXID: 11320
KEYWDS    IMMUNE SYSTEM, SUPERANTIGEN, IMMUNORECEPTORS, TERNARY COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.SALINE,K.E.J.RODSTROM,G.FISCHER,V.Y.OREKHOV,B.G.KARLSSON,
AUTHOR   2 K.LINDKVIST-PETERSSON
REVDAT   2   03-AUG-11 2XN9    1       JRNL   REMARK HETSYN VERSN
REVDAT   1   24-NOV-10 2XN9    0
JRNL        AUTH   M.SALINE,K.E.J.RODSTROM,G.FISCHER,V.Y.OREKHOV,B.G.KARLSSON,
JRNL        AUTH 2 K.LINDKVIST-PETERSSON
JRNL        TITL   THE STRUCTURE OF SUPERANTIGEN COMPLEXED WITH TCR AND MHC
JRNL        TITL 2 REVEALS NOVEL INSIGHTS INTO SUPERANTIGENIC T CELL
JRNL        TITL 3 ACTIVATION.
JRNL        REF    NAT.COMMUN.                   V.   1   119 2010
JRNL        REFN                   ISSN 2041-1723
JRNL        PMID   21081917
JRNL        DOI    10.1038/NCOMMS1117
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 152.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.17
REMARK   3   NUMBER OF REFLECTIONS             : 58700
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) : 0.22414
REMARK   3   R VALUE            (WORKING SET) : 0.22150
REMARK   3   FREE R VALUE                     : 0.27236
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1
REMARK   3   FREE R VALUE TEST SET COUNT      : 3148
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) : 2.300
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.360
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3577
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.97
REMARK   3   BIN R VALUE           (WORKING SET) : 0.293
REMARK   3   BIN FREE R VALUE SET COUNT          : 211
REMARK   3   BIN FREE R VALUE                    : 0.358
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8406
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 25
REMARK   3   SOLVENT ATOMS            : 280
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 49.17
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.997
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.75
REMARK   3    B22 (A**2) : 2.02
REMARK   3    B33 (A**2) : -0.56
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : -1.62
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.316
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.248
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.181
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.350
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8646 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11751 ; 1.443 ; 1.947
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1059 ; 6.671 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   439 ;36.530 ;24.579
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1435 ;18.278 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    51 ;19.710 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1259 ; 0.096 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6722 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  5250 ; 0.794 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8514 ; 1.488 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3396 ; 1.875 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3237 ; 3.061 ; 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   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS.
REMARK   4
REMARK   4 2XN9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-AUG-10.
REMARK 100 THE PDBE ID CODE IS EBI-43900.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)
REMARK 200  OPTICS                         : TOROIDAL MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61858
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.30
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.72
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6
REMARK 200  DATA REDUNDANCY                : 3.2
REMARK 200  R MERGE                    (I) : 0.08
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.7
REMARK 200  R MERGE FOR SHELL          (I) : 0.45
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.10
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: PDB ENTRY 1OGA CHAINS D, E
REMARK 200                 AND PDB ENTRY 1HXY CHAINS A, B, D
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% W/V PEG 5000 MME, 0.1 M BIS-TRIS
REMARK 280  PH 7.0, 0.1 M NACL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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        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       95.59000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.44500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       95.59000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.44500
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR  49 TO CYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, SER  57 TO CYS
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     MET A     1
REMARK 465     PRO A   201
REMARK 465     GLU A   202
REMARK 465     SER A   203
REMARK 465     SER A   204
REMARK 465     MET B     1
REMARK 465     VAL B     2
REMARK 465     LYS C   216
REMARK 465     VAL C   217
REMARK 465     ILE D     1
REMARK 465     LYS D     2
REMARK 465     GLU D     3
REMARK 465     ALA D   182
REMARK 465     GLY E     1
REMARK 465     ALA E   190
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   2    CG   CD   OE1  NE2
REMARK 470     LEU A   3    CG   CD1  CD2
REMARK 470     GLN A  95    CG   CD   OE1  NE2
REMARK 470     GLN A 113    CG   CD   OE1  NE2
REMARK 470     ASP A 129    CG   OD1  OD2
REMARK 470     GLU B  17    CG   CD   OE1  OE2
REMARK 470     SER B 189    OG
REMARK 470     SER B 218    OG
REMARK 470     GLU B 219    CG   CD   OE1  OE2
REMARK 470     LYS C 131    CG   CD   CE   NZ
REMARK 470     LYS C 214    CG   CD   CE   NZ
REMARK 470     LYS D  38    CG   CD   CE   NZ
REMARK 470     LEU D  99    CG   CD1  CD2
REMARK 470     GLU D 172    CG   CD   OE1  OE2
REMARK 470     LYS E  98    CG   CD   CE   NZ
REMARK 470     LEU E 109    CG   CD1  CD2
REMARK 470     GLN E 110    CG   CD   OE1  NE2
REMARK 470     HIS E 111    CG   ND1  CD2  CE1  NE2
REMARK 470     GLU E 128    CG   CD   OE1  OE2
REMARK 470     ARG E 133    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS E 139    CG   CD   CE   NZ
REMARK 470     VAL E 164    CG1  CG2
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    LEU B 157   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    ARG B 193   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LYS A  59     -116.06     54.25
REMARK 500    ALA A  92      -64.75    -98.37
REMARK 500    GLN A  95      -68.29   -105.27
REMARK 500    ASN A  97      160.34     82.78
REMARK 500    SER A 127       -9.06    -49.24
REMARK 500    ASP A 129       30.37    -93.55
REMARK 500    ASP A 166       52.55     38.65
REMARK 500    ASN B  55       -7.43     84.27
REMARK 500    PHE B  76       69.95   -150.09
REMARK 500    ALA B 182       20.24    -78.86
REMARK 500    ASP B 185       44.18   -104.61
REMARK 500    ASN B 220      -32.24   -166.28
REMARK 500    GLN B 225      170.35    -58.60
REMARK 500    GLU C  38      -24.88     55.09
REMARK 500    ASN C  45       16.88     55.40
REMARK 500    ASN C  70       97.87    -69.43
REMARK 500    SER C  86     -164.24   -129.49
REMARK 500    LEU C  93      134.90   -172.77
REMARK 500    SER C 205      -72.11    -81.06
REMARK 500    ASP D  27       12.44     52.12
REMARK 500    PRO D  96      129.91    -33.09
REMARK 500    ASN D 124      -67.82     69.03
REMARK 500    HIS D 143       15.61     85.86
REMARK 500    GLU D 158       13.19    -68.19
REMARK 500    PRO D 173      129.50    -35.39
REMARK 500    THR E   3      -21.77     99.51
REMARK 500    ASN E  19       76.60     66.99
REMARK 500    ASN E  33       60.56     35.65
REMARK 500    GLN E  34       -7.06     69.53
REMARK 500    THR E  90      -68.56   -129.61
REMARK 500    THR E 106     -128.93   -155.04
REMARK 500    GLN E 107      137.85     89.09
REMARK 500    LEU E 109       66.59   -155.39
REMARK 500    GLN E 110      153.56     72.70
REMARK 500    ASP E 152       17.88      7.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASN A  97        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR E   3        23.4      L          L   OUTSIDE RANGE
REMARK 500    ASP E 152        24.1      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA C1216  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C  77   O
REMARK 620 2 HOH A2030   O    92.6
REMARK 620 3 HOH C2011   O    84.6  99.6
REMARK 620 4 HIS C  23   O   155.7 109.6  82.2
REMARK 620 5 SER C  77   OG   70.1 155.1  96.6  91.2
REMARK 620 6 HOH C2028   O    98.9  87.0 172.4  92.1  78.4
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1247
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D6E   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HLA-DR4 COMPLEX WITH PEPTIDOMIMETIC
REMARK 900 AND SEB
REMARK 900 RELATED ID: 1ENF   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H
REMARK 900 DETERMINED TO 1.69 A RESOLUTION
REMARK 900 RELATED ID: 2ESV   RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HLA-E-VMAPRTLIL/KK50.4 TCR COMPLEX
REMARK 900 RELATED ID: 1SEB   RELATED DB: PDB
REMARK 900 COMPLEX OF THE HUMAN MHC CLASS II GLYCOPROTEIN HLA-DR1
REMARK 900 ANDTHE BACTERIAL SUPERANTIGEN SEB
REMARK 900 RELATED ID: 1JWS   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF THE MHC CLASS
REMARK 900 IIMOLECULE HLA-DR1 (HA PEPTIDE 306-318) WITH
REMARK 900 THESUPERANTIGEN SEC3 VARIANT 3B1
REMARK 900 RELATED ID: 1H15   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DRA1*0101/ DRB5*0101
REMARK 900 COMPLEXED WITH A PEPTIDE FROM EPSTEIN BARR VIRUS DNA
REMARK 900 POLYMERASE.
REMARK 900 RELATED ID: 1F77   RELATED DB: PDB
REMARK 900 STAPHYLOCOCCAL ENTEROTOXIN H DETERMINED TO 2. 4 A RESOLUTION
REMARK 900 RELATED ID: 2SEB   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH A PEPTIDE
REMARK 900 FROM HUMAN COLLAGEN II
REMARK 900 RELATED ID: 2AK4   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SB27 TCR IN COMPLEX WITH HLA-B*3508-
REMARK 900 13MER PEPTIDE
REMARK 900 RELATED ID: 2GJ6   RELATED DB: PDB
REMARK 900 THE COMPLEX BETWEEN TCR A6 AND HUMAN CLASS I MHC HLA-A2WITH
REMARK 900 THE MODIFIED HTLV-1 TAX (Y5K-4-[3-INDOLYL]-BUTYRICACID)
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 2WBJ   RELATED DB: PDB
REMARK 900 TCR COMPLEX
REMARK 900 RELATED ID: 1KLU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HLA-DR1/TPI(23-37) COMPLEXED
REMARK 900 WITHSTAPHYLOCOCCAL ENTEROTOXIN C3 VARIANT 3B2 (SEC3-3B2)
REMARK 900 RELATED ID: 1FYT   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T
REMARK 900 CELLRECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS
REMARK 900 IIMOLECULE, HLA-DR1
REMARK 900 RELATED ID: 1PYW   RELATED DB: PDB
REMARK 900 HUMAN CLASS II MHC PROTEIN HLA-DR1 BOUND TO A
REMARK 900 DESIGNEDPEPTIDE RELATED TO INFLUENZA VIRUS HEMAGGLUTININ,
REMARK 900 FVKQNA(MAA)AL, IN COMPLEX WITH STAPHYLOCOCCAL ENTEROTOXINC3
REMARK 900 VARIANT 3B2 (SEC3-3B2)
REMARK 900 RELATED ID: 1J8H   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T
REMARK 900 CELLRECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS
REMARK 900 IIMOLECULE, HLA-DR4
REMARK 900 RELATED ID: 1KLG   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HLA-DR1/TPI(23-37, THR28-->ILE MUTANT)
REMARK 900 COMPLEXED WITH STAPHYLOCOCCAL ENTEROTOXIN C3 VARIANT
REMARK 900 3B2(SEC3 -3B2)
REMARK 900 RELATED ID: 2G9H   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN I (SEI)
REMARK 900 INCOMPLEX WITH A HUMAN MHC CLASS II MOLECULE
REMARK 900 RELATED ID: 1KTK   RELATED DB: PDB
REMARK 900 COMPLEX OF STREPTOCOCCAL PYROGENIC ENTEROTOXIN C (SPEC)WITH
REMARK 900 A HUMAN T CELL RECEPTOR BETA CHAIN (VBETA2.1)
REMARK 900 RELATED ID: 1DLH   RELATED DB: PDB
REMARK 900 RELATED ID: 2BNQ   RELATED DB: PDB
REMARK 900 STRUCTURAL AND KINETIC BASIS FOR HIGHTENED IMMUNOGENICITY
REMARK 900 OF T CELL VACCINES
REMARK 900 RELATED ID: 1D5Z   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH
REMARK 900 PEPTIDOMIMETIC
REMARK 900 RELATED ID: 2EYR   RELATED DB: PDB
REMARK 900 A STRUCTURAL BASIS FOR SELECTION AND CROSS-
REMARK 900 SPECIESREACTIVITY OF THE SEMI-INVARIANT NKT CELL RECEPTOR
REMARK 900 INCD1D/GLYCOLIPID RECOGNITION
REMARK 900 RELATED ID: 1T5X   RELATED DB: PDB
REMARK 900 HLA-DR1 IN COMPLEX WITH A SYNTHETIC PEPTIDE(AAYSDQATPLLLSPR)
REMARK 900 AND THE SUPERANTIGEN SEC3-3B2
REMARK 900 RELATED ID: 1A6A   RELATED DB: PDB
REMARK 900 THE STRUCTURE OF AN INTERMEDIATE IN CLASS II MHC MATURATION:
REMARK 900 CLIP BOUND TO HLA-DR3
REMARK 900 RELATED ID: 1KG0   RELATED DB: PDB
REMARK 900 STRUCTURE OF THE EPSTEIN-BARR VIRUS GP42 PROTEIN BOUND
REMARK 900 TOTHE MHC CLASS II RECEPTOR HLA-DR1
REMARK 900 RELATED ID: 1BX2   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HLA-DR2 (DRA*0101, DRB1*1501)
REMARK 900 COMPLEXEDWITH A PEPTIDE FROM HUMAN MYELIN BASIC PROTEIN
REMARK 900 RELATED ID: 1D5M   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH PEPTIDE
REMARK 900 RELATED ID: 1LO5   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE D227A VARIANT OF
REMARK 900 STAPHYLOCOCCALENTEROTOXIN A IN COMPLEX WITH HUMAN MHC CLASS
REMARK 900 II
REMARK 900 RELATED ID: 1HXY   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H INCOMPLEX
REMARK 900 WITH HUMAN MHC CLASS II
REMARK 900 RELATED ID: 1HQR   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-
REMARK 900 AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II
REMARK 900 RELATED ID: 1QRN   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2
REMARK 900 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A
REMARK 900 RELATED ID: 2BNR   RELATED DB: PDB
REMARK 900 STRUCTURAL AND KINETIC BASIS FOR HIGHTENED IMMUNOGENICITY
REMARK 900 OF T CELL VACCINES
REMARK 900 RELATED ID: 1KGC   RELATED DB: PDB
REMARK 900 IMMUNE RECEPTOR
REMARK 900 RELATED ID: 2CDG   RELATED DB: PDB
REMARK 900 STRUCTURE AND BINDING KINETICS OF THREE DIFFERENT HUMAN
REMARK 900 CD1D-ALPHA-GALACTOSYLCERAMIDE- SPECIFIC T CELL RECEPTORS
REMARK 900 (TCR 5B)
REMARK 900 RELATED ID: 1FV1   RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE BINDING OF AN
REMARK 900 IMMUNODOMINANTPEPTIDE FROM MYELIN BASIC PROTEIN IN
REMARK 900 DIFFERENT REGISTERS BYTWO HLA-DR2 ALLELES
REMARK 900 RELATED ID: 1SJH   RELATED DB: PDB
REMARK 900 HLA-DR1 COMPLEXED WITH A 13 RESIDUE HIV CAPSID PEPTIDE
REMARK 900 RELATED ID: 2EYS   RELATED DB: PDB
REMARK 900 A STRUCTURAL BASIS FOR SELECTION AND CROSS-
REMARK 900 SPECIESREACTIVITY OF THE SEMI-INVARIANT NKT CELL RECEPTOR
REMARK 900 INCD1D/GLYCOLIPID RECOGNITION
REMARK 900 RELATED ID: 2BNU   RELATED DB: PDB
REMARK 900 STRUCTURAL AND KINETIC BASIS FOR HIGHTENED IMMUNOGENICITY
REMARK 900 OF T CELL VACCINES
REMARK 900 RELATED ID: 1JWM   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF THE MHC CLASS
REMARK 900 IIMOLECULE HLA-DR1(HA PEPTIDE 306-318) WITH THE
REMARK 900 SUPERANTIGENSEC3
REMARK 900 RELATED ID: 2CDF   RELATED DB: PDB
REMARK 900 STRUCTURE AND BINDING KINETICS OF THREE DIFFERENT HUMAN
REMARK 900 CD1D-ALPHA-GALACTOSYLCERAMIDE- SPECIFIC T CELL RECEPTORS
REMARK 900 (TCR 5E)
REMARK 900 RELATED ID: 1MI5   RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF LC13 TCR IN COMPLEX WITH HLAB8-
REMARK 900 EBVPEPTIDE COMPLEX
REMARK 900 RELATED ID: 1YMM   RELATED DB: PDB
REMARK 900 TCR/HLA-DR2B/MBP-PEPTIDE COMPLEX
REMARK 900 RELATED ID: 1R5I   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MAM-MHC COMPLEX
REMARK 900 RELATED ID: 1ZGL   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3A6 TCR BOUND TO MBP /HLA-DR2A
REMARK 900 RELATED ID: 1EWC   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ZN2+ LOADED STAPHYLOCOCCAL ENTEROTOXIN
REMARK 900 H
REMARK 900 RELATED ID: 1T5W   RELATED DB: PDB
REMARK 900 HLA-DR1 IN COMPLEX WITH A SYNTHETIC PEPTIDE(AAYSDQATPLLLSPR)
REMARK 900 RELATED ID: 1D5X   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH DIPEPTIDE
REMARK 900 MIMETIC
REMARK 900 RELATED ID: 2AXH   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF T CELL RECEPTOR BETA CHAINS RELATEDTO
REMARK 900 RHEUMATOID ARTHRITIS
REMARK 900 RELATED ID: 1AQD   RELATED DB: PDB
REMARK 900 HLA-DR1 (DRA, DRB1 0101) HUMAN CLASS II
REMARK 900 HISTOCOMPATIBILITYPROTEIN (EXTRACELLULAR DOMAIN) COMPLEXED
REMARK 900 WITH ENDOGENOUSPEPTIDE
REMARK 900 RELATED ID: 2EYT   RELATED DB: PDB
REMARK 900 A STRUCTURAL BASIS FOR SELECTION AND CROSS-
REMARK 900 SPECIESREACTIVITY OF THE SEMI-INVARIANT NKT CELL RECEPTOR
REMARK 900 INCD1D/GLYCOLIPID RECOGNITION
REMARK 900 RELATED ID: 1SJE   RELATED DB: PDB
REMARK 900 HLA-DR1 COMPLEXED WITH A 16 RESIDUE HIV CAPSID PEPTIDEBOUND
REMARK 900 IN A HAIRPIN CONFORMATION
REMARK 900 RELATED ID: 1OGA   RELATED DB: PDB
REMARK 900 A STRUCTURAL BASIS FOR IMMUNODOMINANT HUMAN T-CELL RECEPTOR
REMARK 900 RECOGNITION.
REMARK 900 RELATED ID: 1JWU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF THE MHC CLASS
REMARK 900 IIMOLECULE HLA-DR1 (HA PEPTIDE 306-318) WITH
REMARK 900 THESUPERANTIGEN SEC3 VARIANT 3B2
REMARK 900 RELATED ID: 2CDE   RELATED DB: PDB
REMARK 900 STRUCTURE AND BINDING KINETICS OF THREE DIFFERENT HUMAN
REMARK 900 CD1D-ALPHA-GALACTOSYLCERAMIDE SPECIFIC T CELL RECEPTORS -
REMARK 900 INKT-TCR
REMARK 900 RELATED ID: 2XNA   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN HUMAN T
REMARK 900 CELL RECEPTOR AND STAPHYLOCOCCAL ENTEROTOXIN H
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN A RESIDUES 1-109 CONTAINS THE TCR VARIABLE DOMAIN TRAV27.
REMARK 999  ALPHA CHAIN RESIDUES 96-142 ARE EXCLUDED.
REMARK 999 CHAIN B RESIDUES 1-114 CONTAINS THE TCR VARIABLE DOMAIN TRBV19.
REMARK 999  BETA CHAIN RESIDUES 131-177 ARE EXCLUDED.
REMARK 999 SIGNAL SEQUENCES (RESIDUES B1-24, C1-25, D1-29) NOT IN CONSTRUCTS.
REMARK 999 SYNTHETIC PEPTIDE F OF 13 RESIDUES, 306-318 OF INFLUENZA
REMARK 999 HEMAGGLUTININ.
DBREF  2XN9 A    1   109  PDB    2XN9     2XN9             1    109
DBREF  2XN9 A  110   204  UNP    P01848   TCA_HUMAN        1     95
DBREF  2XN9 B    1   114  PDB    2XN9     2XN9             1    114
DBREF  2XN9 B  115   244  UNP    P01850   TRBC1_HUMAN      1    130
DBREF  2XN9 C    1   217  UNP    P0A0M0   ETXH_STAAU      25    241
DBREF  2XN9 D    1   182  UNP    P01903   DRA_HUMAN       26    207
DBREF  2XN9 E    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  2XN9 F    1    13  UNP    A8CDU0   A8CDU0_9INFA    59     71
SEQADV 2XN9 CYS A  158  UNP  P01848    THR    49 ENGINEERED MUTATION
SEQADV 2XN9 LYS B  118  UNP  P01850    ASN     4 CONFLICT
SEQADV 2XN9 ASN B  119  UNP  P01850    LYS     5 CONFLICT
SEQADV 2XN9 TYR B  151  UNP  P01850    PHE    37 CONFLICT
SEQADV 2XN9 CYS B  171  UNP  P01850    SER    57 ENGINEERED MUTATION
SEQADV 2XN9 SER B  189  UNP  P01850    CYS    75 CONFLICT
SEQRES   1 A  204  MET GLN LEU LEU GLU GLN SER PRO GLN PHE LEU SER ILE
SEQRES   2 A  204  GLN GLU GLY GLU ASN LEU THR VAL TYR CYS ASN SER SER
SEQRES   3 A  204  SER VAL PHE SER SER LEU GLN TRP TYR ARG GLN GLU PRO
SEQRES   4 A  204  GLY GLU GLY PRO VAL LEU LEU VAL THR VAL VAL THR GLY
SEQRES   5 A  204  GLY GLU VAL LYS LYS LEU LYS ARG LEU THR PHE GLN PHE
SEQRES   6 A  204  GLY ASP ALA ARG LYS ASP SER SER LEU HIS ILE THR ALA
SEQRES   7 A  204  ALA GLN PRO GLY ASP THR GLY LEU TYR LEU CYS ALA GLY
SEQRES   8 A  204  ALA GLY SER GLN GLY ASN LEU ILE PHE GLY LYS GLY THR
SEQRES   9 A  204  LYS LEU SER VAL LYS PRO ASN ILE GLN ASN PRO ASP PRO
SEQRES  10 A  204  ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS
SEQRES  11 A  204  SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN
SEQRES  12 A  204  VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP
SEQRES  13 A  204  LYS CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER
SEQRES  14 A  204  ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA
SEQRES  15 A  204  CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP
SEQRES  16 A  204  THR PHE PHE PRO SER PRO GLU SER SER
SEQRES   1 B  244  MET VAL ASP GLY GLY ILE THR GLN SER PRO LYS TYR LEU
SEQRES   2 B  244  PHE ARG LYS GLU GLY GLN ASN VAL THR LEU SER CYS GLU
SEQRES   3 B  244  GLN ASN LEU ASN HIS ASP ALA MET TYR TRP TYR ARG GLN
SEQRES   4 B  244  ASP PRO GLY GLN GLY LEU ARG LEU ILE TYR TYR SER GLN
SEQRES   5 B  244  ILE VAL ASN ASP PHE GLN LYS GLY ASP ILE ALA GLU GLY
SEQRES   6 B  244  TYR SER VAL SER ARG GLU LYS LYS GLU SER PHE PRO LEU
SEQRES   7 B  244  THR VAL THR SER ALA GLN LYS ASN PRO THR ALA PHE TYR
SEQRES   8 B  244  LEU CYS ALA SER SER SER ARG SER SER TYR GLU GLN TYR
SEQRES   9 B  244  PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU ASP LEU
SEQRES  10 B  244  LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO
SEQRES  11 B  244  SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU
SEQRES  12 B  244  VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU
SEQRES  13 B  244  LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY
SEQRES  14 B  244  VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA
SEQRES  15 B  244  LEU ASN ASP SER ARG TYR SER LEU SER SER ARG LEU ARG
SEQRES  16 B  244  VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE
SEQRES  17 B  244  ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP
SEQRES  18 B  244  GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE
SEQRES  19 B  244  VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES   1 C  217  GLU ASP LEU HIS ASP LYS SER GLU LEU THR ASP LEU ALA
SEQRES   2 C  217  LEU ALA ASN ALA TYR GLY GLN TYR ASN HIS PRO PHE ILE
SEQRES   3 C  217  LYS GLU ASN ILE LYS SER ASP GLU ILE SER GLY GLU LYS
SEQRES   4 C  217  ASP LEU ILE PHE ARG ASN GLN GLY ASP SER GLY ASN ASP
SEQRES   5 C  217  LEU ARG VAL LYS PHE ALA THR ALA ASP LEU ALA GLN LYS
SEQRES   6 C  217  PHE LYS ASN LYS ASN VAL ASP ILE TYR GLY ALA SER PHE
SEQRES   7 C  217  TYR TYR LYS CYS GLU LYS ILE SER GLU ASN ILE SER GLU
SEQRES   8 C  217  CYS LEU TYR GLY GLY THR THR LEU ASN SER GLU LYS LEU
SEQRES   9 C  217  ALA GLN GLU ARG VAL ILE GLY ALA ASN VAL TRP VAL ASP
SEQRES  10 C  217  GLY ILE GLN LYS GLU THR GLU LEU ILE ARG THR ASN LYS
SEQRES  11 C  217  LYS ASN VAL THR LEU GLN GLU LEU ASP ILE LYS ILE ARG
SEQRES  12 C  217  LYS ILE LEU SER ASP LYS TYR LYS ILE TYR TYR LYS ASP
SEQRES  13 C  217  SER GLU ILE SER LYS GLY LEU ILE GLU PHE ASP MET LYS
SEQRES  14 C  217  THR PRO ARG ASP TYR SER PHE ASP ILE TYR ASP LEU LYS
SEQRES  15 C  217  GLY GLU ASN ASP TYR GLU ILE ASP LYS ILE TYR GLU ASP
SEQRES  16 C  217  ASN LYS THR LEU LYS SER ASP ASP ILE SER HIS ILE ASP
SEQRES  17 C  217  VAL ASN LEU TYR THR LYS LYS LYS VAL
SEQRES   1 D  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 D  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 D  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 D  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 D  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 D  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 D  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 D  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 D  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 D  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 D  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 D  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 D  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 D  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES   1 E  190  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 E  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 E  190  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 E  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 E  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 E  190  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 E  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 E  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 E  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 E  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 E  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 E  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 E  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 E  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 E  190  PRO LEU THR VAL GLU TRP ARG ALA
SEQRES   1 F   13  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
HET    GOL  A1201       6
HET    GOL  B1245       6
HET    GOL  B1246       6
HET    GOL  B1247       6
HET     NA  C1216       1
HETNAM     GOL GLYCEROL
HETNAM      NA SODIUM ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   7  GOL    4(C3 H8 O3)
FORMUL   8   NA    NA 1+
FORMUL   9  HOH   *280(H2 O)
HELIX    1   1 GLN A   80  THR A   84  5                                   5
HELIX    2   2 ARG A  163  ASP A  166  5                                   4
HELIX    3   3 ALA A  182  PHE A  187  1                                   6
HELIX    4   4 ASP B  116  VAL B  120  5                                   5
HELIX    5   5 SER B  131  GLN B  139  1                                   9
HELIX    6   6 ALA B  198  GLN B  202  1                                   5
HELIX    7   7 ASP C    5  LEU C    9  5                                   5
HELIX    8   8 THR C   10  HIS C   23  1                                  14
HELIX    9   9 GLY C   47  ASN C   51  5                                   5
HELIX   10  10 THR C   59  LYS C   67  1                                   9
HELIX   11  11 LEU C  135  LYS C  151  1                                  17
HELIX   12  12 ASN C  185  ASP C  190  1                                   6
HELIX   13  13 LYS C  191  GLU C  194  5                                   4
HELIX   14  14 GLU D   47  ALA D   52  1                                   6
HELIX   15  15 GLU D   55  SER D   77  1                                  23
HELIX   16  16 THR E   51  LEU E   53  5                                   3
HELIX   17  17 GLY E   54  SER E   63  1                                  10
HELIX   18  18 GLN E   64  ALA E   73  1                                  10
HELIX   19  19 ALA E   73  TYR E   78  1                                   6
HELIX   20  20 TYR E   78  GLY E   86  1                                   9
HELIX   21  21 GLU E   87  GLN E   92  1                                   6
SHEET    1  AA 5 GLU A   5  SER A   7  0
SHEET    2  AA 5 LEU A  19  ASN A  24 -1  O  TYR A  22   N  SER A   7
SHEET    3  AA 5 ASP A  71  ILE A  76 -1  O  SER A  72   N  CYS A  23
SHEET    4  AA 5 LEU A  61  PHE A  65 -1  O  THR A  62   N  HIS A  75
SHEET    5  AA 5 VAL A  55  LEU A  58 -1  O  LYS A  56   N  PHE A  63
SHEET    1  AB 4 PHE A  10  GLN A  14  0
SHEET    2  AB 4 THR A 104  LYS A 109  1  O  LYS A 105   N  LEU A  11
SHEET    3  AB 4 GLY A  85  GLY A  91 -1  O  GLY A  85   N  LEU A 106
SHEET    4  AB 4 ILE A  99  PHE A 100  1  O  ILE A  99   N  GLY A  91
SHEET    1  AC 5 PHE A  10  GLN A  14  0
SHEET    2  AC 5 THR A 104  LYS A 109  1  O  LYS A 105   N  LEU A  11
SHEET    3  AC 5 GLY A  85  GLY A  91 -1  O  GLY A  85   N  LEU A 106
SHEET    4  AC 5 LEU A  32  GLN A  37 -1  O  GLN A  33   N  ALA A  90
SHEET    5  AC 5 VAL A  44  VAL A  49 -1  O  VAL A  44   N  ARG A  36
SHEET    1  AD 2 ILE A  99  PHE A 100  0
SHEET    2  AD 2 GLY A  85  GLY A  91  1  O  GLY A  91   N  ILE A  99
SHEET    1  AE 2 VAL A 152  ILE A 154  0
SHEET    2  AE 2 PHE A 167  SER A 176 -1  O  TRP A 175   N  TYR A 153
SHEET    1  AF 2 CYS A 158  MET A 162  0
SHEET    2  AF 2 PHE A 167  SER A 176 -1  O  PHE A 167   N  MET A 162
SHEET    1  BA 2 VAL B 170  THR B 172  0
SHEET    2  BA 2 TYR B 188  SER B 197 -1  O  ARG B 193   N  CYS B 171
SHEET    1  BB 2 LEU B 177  LYS B 178  0
SHEET    2  BB 2 TYR B 188  SER B 197  1  O  SER B 189   N  LEU B 177
SHEET    1  BC 4 ILE B   6  SER B   9  0
SHEET    2  BC 4 VAL B  21  GLN B  27 -1  O  SER B  24   N  SER B   9
SHEET    3  BC 4 LEU B  78  VAL B  80 -1  O  LEU B  78   N  LEU B  23
SHEET    4  BC 4 TYR B  66  VAL B  68 -1  O  SER B  67   N  THR B  79
SHEET    1  BD 4 TYR B  12  LYS B  16  0
SHEET    2  BD 4 THR B 109  THR B 114  1  O  ARG B 110   N  LEU B  13
SHEET    3  BD 4 ALA B  89  SER B  96 -1  O  ALA B  89   N  LEU B 111
SHEET    4  BD 4 TYR B 104  PHE B 105 -1  O  TYR B 104   N  SER B  95
SHEET    1  BE 6 TYR B  12  LYS B  16  0
SHEET    2  BE 6 THR B 109  THR B 114  1  O  ARG B 110   N  LEU B  13
SHEET    3  BE 6 ALA B  89  SER B  96 -1  O  ALA B  89   N  LEU B 111
SHEET    4  BE 6 ALA B  33  ASP B  40 -1  O  ALA B  33   N  SER B  96
SHEET    5  BE 6 GLY B  44  ILE B  53 -1  O  GLY B  44   N  ASP B  40
SHEET    6  BE 6 ASP B  56  LYS B  59 -1  O  ASP B  56   N  ILE B  53
SHEET    1  BF 2 TYR B 104  PHE B 105  0
SHEET    2  BF 2 ALA B  89  SER B  96 -1  O  SER B  95   N  TYR B 104
SHEET    1  BG 4 LYS B 164  VAL B 166  0
SHEET    2  BG 4 VAL B 155  VAL B 161 -1  O  TRP B 159   N  VAL B 166
SHEET    3  BG 4 HIS B 207  PHE B 214 -1  O  ARG B 209   N  TRP B 160
SHEET    4  BG 4 GLN B 233  TRP B 240 -1  O  GLN B 233   N  PHE B 214
SHEET    1  CA 3 PHE C  25  ILE C  30  0
SHEET    2  CA 3 VAL C  71  GLY C  75 -1  O  VAL C  71   N  ILE C  30
SHEET    3  CA 3 THR C  97  LEU C  99 -1  O  THR C  98   N  ASP C  72
SHEET    1  CB 5 ILE C  35  SER C  36  0
SHEET    2  CB 5 ASP C  40  PHE C  43 -1  O  ASP C  40   N  SER C  36
SHEET    3  CB 5 ASP C  52  LYS C  56 -1  O  LEU C  53   N  PHE C  43
SHEET    4  CB 5 SER C  90  TYR C  94  1  O  GLU C  91   N  ARG C  54
SHEET    5  CB 5 SER C  77  PHE C  78 -1  O  PHE C  78   N  CYS C  92
SHEET    1  CC 2 ILE C 119  GLN C 120  0
SHEET    2  CC 2 LYS C 103  VAL C 116 -1  O  VAL C 116   N  ILE C 119
SHEET    1  CD 2 GLU C 124  LYS C 130  0
SHEET    2  CD 2 LYS C 103  VAL C 116 -1  N  LEU C 104   O  ASN C 129
SHEET    1  CE 5 TYR C 174  ASP C 177  0
SHEET    2  CE 5 LYS C 161  MET C 168 -1  O  ILE C 164   N  PHE C 176
SHEET    3  CE 5 ILE C 204  TYR C 212 -1  N  SER C 205   O  ASP C 167
SHEET    4  CE 5 LYS C 103  VAL C 116  1  O  GLY C 111   N  ILE C 207
SHEET    5  CE 5 ILE C 119  GLN C 120 -1  O  ILE C 119   N  VAL C 116
SHEET    1  CF 5 TYR C 174  ASP C 177  0
SHEET    2  CF 5 LYS C 161  MET C 168 -1  O  ILE C 164   N  PHE C 176
SHEET    3  CF 5 ILE C 204  TYR C 212 -1  N  SER C 205   O  ASP C 167
SHEET    4  CF 5 LYS C 103  VAL C 116  1  O  GLY C 111   N  ILE C 207
SHEET    5  CF 5 GLU C 124  LYS C 130 -1  O  GLU C 124   N  ALA C 112
SHEET    1  CG 2 ASN C 132  THR C 134  0
SHEET    2  CG 2 THR C 198  LYS C 200 -1  O  LEU C 199   N  VAL C 133
SHEET    1  DA 8 GLU D  40  TRP D  43  0
SHEET    2  DA 8 ASP D  29  ASP D  35 -1  O  HIS D  33   N  VAL D  42
SHEET    3  DA 8 SER D  19  PHE D  26 -1  O  PHE D  22   N  VAL D  34
SHEET    4  DA 8 HIS D   5  ASN D  15 -1  O  ILE D   8   N  ASP D  25
SHEET    5  DA 8 PHE E   7  PHE E  18 -1  O  PHE E   7   N  ASN D  15
SHEET    6  DA 8 ARG E  23  TYR E  32 -1  O  ARG E  23   N  PHE E  18
SHEET    7  DA 8 GLU E  35  ASP E  41 -1  O  GLU E  35   N  TYR E  32
SHEET    8  DA 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39
SHEET    1  DB 4 GLU D  88  THR D  93  0
SHEET    2  DB 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3  DB 4 PHE D 145  PHE D 153 -1  O  PHE D 145   N  PHE D 112
SHEET    4  DB 4 LEU D 138  PRO D 139  1  O  LEU D 138   N  ARG D 146
SHEET    1  DC 4 GLU D  88  THR D  93  0
SHEET    2  DC 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3  DC 4 PHE D 145  PHE D 153 -1  O  PHE D 145   N  PHE D 112
SHEET    4  DC 4 SER D 133  GLU D 134 -1  O  SER D 133   N  TYR D 150
SHEET    1  DD 2 LEU D 138  PRO D 139  0
SHEET    2  DD 2 PHE D 145  PHE D 153  1  O  ARG D 146   N  LEU D 138
SHEET    1  DE 4 LYS D 126  VAL D 128  0
SHEET    2  DE 4 ASN D 118  ARG D 123 -1  O  TRP D 121   N  VAL D 128
SHEET    3  DE 4 VAL D 160  GLU D 166 -1  O  ASP D 162   N  LEU D 122
SHEET    4  DE 4 LEU D 174  GLU D 179 -1  O  LEU D 174   N  VAL D 165
SHEET    1  EA 4 LYS E  98  PRO E 103  0
SHEET    2  EA 4 ASN E 113  PHE E 122 -1  O  VAL E 116   N  TYR E 102
SHEET    3  EA 4 PHE E 155  THR E 163 -1  O  PHE E 155   N  PHE E 122
SHEET    4  EA 4 ILE E 148  GLN E 149  1  O  ILE E 148   N  GLN E 156
SHEET    1  EB 4 LYS E  98  PRO E 103  0
SHEET    2  EB 4 ASN E 113  PHE E 122 -1  O  VAL E 116   N  TYR E 102
SHEET    3  EB 4 PHE E 155  THR E 163 -1  O  PHE E 155   N  PHE E 122
SHEET    4  EB 4 VAL E 142  SER E 144 -1  O  VAL E 143   N  MET E 160
SHEET    1  EC 2 ILE E 148  GLN E 149  0
SHEET    2  EC 2 PHE E 155  THR E 163  1  O  GLN E 156   N  ILE E 148
SHEET    1  ED 4 GLN E 136  GLU E 138  0
SHEET    2  ED 4 GLU E 128  ARG E 133 -1  O  TRP E 131   N  GLU E 138
SHEET    3  ED 4 TYR E 171  GLU E 176 -1  O  THR E 172   N  PHE E 132
SHEET    4  ED 4 LEU E 184  TRP E 188 -1  O  LEU E 184   N  VAL E 175
SSBOND   1 CYS A   23    CYS A   89                          1555   1555  2.04
SSBOND   2 CYS A  133    CYS A  183                          1555   1555  2.03
SSBOND   3 CYS A  158    CYS B  171                          1555   1555  2.05
SSBOND   4 CYS B   25    CYS B   93                          1555   1555  2.00
SSBOND   5 CYS B  145    CYS B  210                          1555   1555  2.03
SSBOND   6 CYS C   82    CYS C   92                          1555   1555  2.06
SSBOND   7 CYS D  107    CYS D  163                          1555   1555  2.06
SSBOND   8 CYS E   15    CYS E   79                          1555   1555  2.08
SSBOND   9 CYS E  117    CYS E  173                          1555   1555  2.01
LINK        NA    NA C1216                 O   SER C  77     1555   1555  2.47
LINK        NA    NA C1216                 O   HOH A2030     1555   1555  2.18
LINK        NA    NA C1216                 O   HOH C2011     1555   1555  2.47
LINK        NA    NA C1216                 O   HIS C  23     1555   1555  2.22
LINK        NA    NA C1216                 OG  SER C  77     1555   1555  2.50
LINK        NA    NA C1216                 O   HOH C2028     1555   1555  2.71
CISPEP   1 SER A    7    PRO A    8          0        -6.37
CISPEP   2 SER B    9    PRO B   10          0        -5.29
CISPEP   3 TYR B  151    PRO B  152          0         0.75
CISPEP   4 ALA B  243    ASP B  244          0         4.26
CISPEP   5 ASN D   15    PRO D   16          0         0.22
CISPEP   6 THR D  113    PRO D  114          0         0.06
CISPEP   7 PRO E  108    LEU E  109          0         0.84
CISPEP   8 TYR E  123    PRO E  124          0         4.01
SITE     1 AC1  5 HOH A2030  HIS C  23  SER C  77  HOH C2011
SITE     2 AC1  5 HOH C2028
SITE     1 AC2  7 GLU A  17  ARG A 163  SER A 164  HOH A2092
SITE     2 AC2  7 SER B 168  ARG B 195  GOL B1245
SITE     1 AC3  5 GLU A  17  GOL A1201  HOH A2092  VAL B 196
SITE     2 AC3  5 SER B 197
SITE     1 AC4  5 ARG B 110  ASP B 153  GLN B 175  PRO B 176
SITE     2 AC4  5 TYR B 188
SITE     1 AC5  5 ASN B  30  HIS B  31  ASP B  32  SER B  97
SITE     2 AC5  5 ARG B  98
CRYST1  191.180   48.890  166.720  90.00 113.55  90.00 C 1 2 1       4
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      0.005231  0.000000  0.002280        0.00000
SCALE2      0.000000  0.020454  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006543        0.00000
      
PROCHECK
Go to PROCHECK summary
 References