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PDBsum entry 1fyt

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Top Page protein ligands Protein-protein interface(s) links
Immune system PDB id
1fyt
Jmol
Contents
Protein chains
180 a.a. *
179 a.a. *
13 a.a. *
198 a.a. *
240 a.a. *
Ligands
NAG ×2
Waters ×100
* Residue conservation analysis
HEADER    IMMUNE SYSTEM                           03-OCT-00   1FYT
TITLE     CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR,
TITLE    2 INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND   5 SYNONYM: HLA-DR1, DRA;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1 BETA CHAIN;
COMPND   9 CHAIN: B;
COMPND  10 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND  11 SYNONYM: HLA-DR1, DRB1 0101;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: HEMAGGLUTININ HA1 PEPTIDE CHAIN;
COMPND  15 CHAIN: C;
COMPND  16 FRAGMENT: ANTIGEN PEPTIDE;
COMPND  17 ENGINEERED: YES;
COMPND  18 MOL_ID: 4;
COMPND  19 MOLECULE: T-CELL RECEPTOR ALPHA CHAIN;
COMPND  20 CHAIN: D;
COMPND  21 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND  22 SYNONYM: TCR HA1.7 ALPHA CHAIN;
COMPND  23 ENGINEERED: YES;
COMPND  24 MOL_ID: 5;
COMPND  25 MOLECULE: T-CELL RECEPTOR BETA CHAIN;
COMPND  26 CHAIN: E;
COMPND  27 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND  28 SYNONYM: TCR HA1.7 BETA CHAIN;
COMPND  29 ENGINEERED: YES;
COMPND  30 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE   8 MOL_ID: 2;
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  10 ORGANISM_COMMON: HUMAN;
SOURCE  11 ORGANISM_TAXID: 9606;
SOURCE  12 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE  13 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE  15 MOL_ID: 3;
SOURCE  16 ORGANISM_SCIENTIFIC: H3N2 SUBTYPE;
SOURCE  17 ORGANISM_TAXID: 119210;
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  20 MOL_ID: 4;
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  22 ORGANISM_COMMON: HUMAN;
SOURCE  23 ORGANISM_TAXID: 9606;
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  26 MOL_ID: 5;
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  28 ORGANISM_COMMON: HUMAN;
SOURCE  29 ORGANISM_TAXID: 9606;
SOURCE  30 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    PROTEIN-PROTEIN COMPLEX, IMMUNOGLOBULIN FOLD, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.HENNECKE,A.CARFI,D.C.WILEY
REVDAT   4   13-JUL-11 1FYT    1       VERSN
REVDAT   3   24-FEB-09 1FYT    1       VERSN
REVDAT   2   01-APR-03 1FYT    1       JRNL
REVDAT   1   08-NOV-00 1FYT    0
JRNL        AUTH   J.HENNECKE,A.CARFI,D.C.WILEY
JRNL        TITL   STRUCTURE OF A COVALENTLY STABILIZED COMPLEX OF A HUMAN
JRNL        TITL 2 ALPHABETA T-CELL RECEPTOR, INFLUENZA HA PEPTIDE AND MHC
JRNL        TITL 3 CLASS II MOLECULE, HLA-DR1.
JRNL        REF    EMBO J.                       V.  19  5611 2000
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   11060013
JRNL        DOI    10.1093/EMBOJ/19.21.5611
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.9
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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1407758.260
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 37122
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) : 0.221
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1871
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.69
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3488
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280
REMARK   3   BIN FREE R VALUE                    : 0.3770
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 184
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6516
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 100
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 59.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.13000
REMARK   3    B22 (A**2) : 6.74000
REMARK   3    B33 (A**2) : -6.88000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 3.42000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34
REMARK   3   ESD FROM SIGMAA              (A) : 0.31
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.600 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.690 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.630 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.950 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 24.68
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1FYT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB012026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-99
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               : APS
REMARK 200  BEAMLINE                       : 14-BM-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37159
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 6.000
REMARK 200  R MERGE                    (I) : 0.07600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.22100
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000,   1 M NACL,   100 MM
REMARK 280  HEPES, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 18K
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       71.45100
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.71950
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.45100
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.71950
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     GLY B     1
REMARK 465     ASP B     2
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     ASN B   113
REMARK 465     ARG B   191
REMARK 465     SER B   192
REMARK 465     ASP D   130
REMARK 465     SER D   131
REMARK 465     LYS D   132
REMARK 465     PHE D   204
REMARK 465     PRO D   205
REMARK 465     SER D   206
REMARK 465     PRO D   207
REMARK 465     GLU D   208
REMARK 465     SER D   209
REMARK 465     SER D   210
REMARK 465     CYS D   211
REMARK 465     ASP D   212
REMARK 465     VAL D   213
REMARK 465     LYS D   214
REMARK 465     ASP E   247
REMARK 465     CYS E   248
REMARK 465     GLY E   249
REMARK 465     PHE E   250
REMARK 465     THR E   251
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 D 152    CG   CD   OE1  NE2
REMARK 470     LYS D 154    CG   CD   CE   NZ
REMARK 470     ASP D 157    CG   OD1  OD2
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    ASN A  15   N   -  CA  -  C   ANGL. DEV. =  19.6 DEGREES
REMARK 500    PRO A  16   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES
REMARK 500    PRO B 103   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES
REMARK 500    PRO E 100   C   -  N   -  CA  ANGL. DEV. =   9.9 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      -55.64   -133.60
REMARK 500    ASN A  15      -79.21    -87.05
REMARK 500    ARG A 100       -4.06     72.36
REMARK 500    ASN B  19       73.43     61.50
REMARK 500    CYS B  79      -72.32    -59.24
REMARK 500    THR B  90      -79.88   -116.31
REMARK 500    PRO B 124     -165.31    -71.97
REMARK 500    SER D  51       -2.83     73.00
REMARK 500    ASN D  60       28.68     47.79
REMARK 500    PHE D  73       61.91   -156.96
REMARK 500    ALA D  86     -174.13    178.84
REMARK 500    ILE D 118      100.41    -59.08
REMARK 500    ASP D 122       78.21   -170.89
REMARK 500    PRO D 123      155.13    -45.92
REMARK 500    ASP D 143       16.71     58.73
REMARK 500    GLN D 152     -167.75    -65.53
REMARK 500    ASN D 195       93.93     90.71
REMARK 500    SER D 196       50.64     37.22
REMARK 500    GLU E  62      128.82    -38.63
REMARK 500    SER E  88     -177.81   -171.51
REMARK 500    PRO E 100        9.59    -62.83
REMARK 500    ASN E 121        2.28    -67.50
REMARK 500    HIS E 157       75.77   -116.15
REMARK 500    ASP E 188       67.46   -110.03
REMARK 500    THR E 227       19.80   -143.99
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  15        18.6      L          L   OUTSIDE RANGE
REMARK 500    SER D 196        25.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 511
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DLH   RELATED DB: PDB
REMARK 900 1DLH CONTAINS THE COMPLEX OF HLA-DR1 WITH THE HA306-318
REMARK 900 ANTIGEN PEPTIDE
DBREF  1FYT A    1   181  UNP    P01903   2DRA_HUMAN      26    206
DBREF  1FYT B    1   192  UNP    P04229   2B11_HUMAN      30    221
DBREF  1FYT C  306   318  UNP    P03437   HEMA_IAAIC     322    334
DBREF  1FYT D    1   214  PIR    RWHUAC   RWHUAC          21    232
DBREF  1FYT E    3   251  UNP    P01850   TCB_HUMAN       22    266
SEQADV 1FYT SER E  192  UNP  P01850    CYS   207 ENGINEERED
SEQRES   1 A  181  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 A  181  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 A  181  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 A  181  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 A  181  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 A  181  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 A  181  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 A  181  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 A  181  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 A  181  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 A  181  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 A  181  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 A  181  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 A  181  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES   1 B  192  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 B  192  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 B  192  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 B  192  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 B  192  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 B  192  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 B  192  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 B  192  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 B  192  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 B  192  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 B  192  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 B  192  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 B  192  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 B  192  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 B  192  PRO LEU THR VAL GLU TRP ARG ALA ARG SER
SEQRES   1 C   13  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES   1 D  212  GLN SER VAL THR GLN LEU GLY SER HIS VAL SER VAL SER
SEQRES   2 D  212  GLU GLY ALA LEU VAL LEU LEU ARG CYS ASN TYR SER SER
SEQRES   3 D  212  SER VAL PRO PRO TYR LEU PHE TRP TYR VAL GLN TYR PRO
SEQRES   4 D  212  ASN GLN GLY LEU GLN LEU LEU LEU LYS TYR THR SER ALA
SEQRES   5 D  212  ALA THR LEU VAL LYS GLY ILE ASN GLY PHE GLU ALA GLU
SEQRES   6 D  212  PHE LYS LYS SER GLU THR SER PHE HIS LEU THR LYS PRO
SEQRES   7 D  212  SER ALA HIS MET SER ASP ALA ALA GLU TYR PHE CYS ALA
SEQRES   8 D  212  VAL SER GLU SER PRO PHE GLY ASN GLU LYS LEU THR PHE
SEQRES   9 D  212  GLY THR GLY THR ARG LEU THR ILE ILE PRO ASN ILE GLN
SEQRES  10 D  212  ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS
SEQRES  11 D  212  SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP
SEQRES  12 D  212  SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL
SEQRES  13 D  212  TYR ILE THR ASP LYS THR VAL LEU ASP MET ARG SER MET
SEQRES  14 D  212  ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS
SEQRES  15 D  212  SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE
SEQRES  16 D  212  ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES  17 D  212  CYS ASP VAL LYS
SEQRES   1 E  245  LYS VAL THR GLN SER SER ARG TYR LEU VAL LYS ARG THR
SEQRES   2 E  245  GLY GLU LYS VAL PHE LEU GLU CYS VAL GLN ASP MET ASP
SEQRES   3 E  245  HIS GLU ASN MET PHE TRP TYR ARG GLN ASP PRO GLY LEU
SEQRES   4 E  245  GLY LEU ARG LEU ILE TYR PHE SER TYR ASP VAL LYS MET
SEQRES   5 E  245  LYS GLU LYS GLY ASP ILE PRO GLU GLY TYR SER VAL SER
SEQRES   6 E  245  ARG GLU LYS LYS GLU ARG PHE SER LEU ILE LEU GLU SER
SEQRES   7 E  245  ALA SER THR ASN GLN THR SER MET TYR LEU CYS ALA SER
SEQRES   8 E  245  SER SER THR GLY LEU PRO TYR GLY TYR THR PHE GLY SER
SEQRES   9 E  245  GLY THR ARG LEU THR VAL VAL GLU ASP LEU ASN LYS VAL
SEQRES  10 E  245  PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU ALA
SEQRES  11 E  245  GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS LEU
SEQRES  12 E  245  ALA THR GLY PHE PHE PRO ASP HIS VAL GLU LEU SER TRP
SEQRES  13 E  245  TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL SER THR
SEQRES  14 E  245  ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN ASP
SEQRES  15 E  245  SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER ALA
SEQRES  16 E  245  THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS GLN
SEQRES  17 E  245  VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP THR
SEQRES  18 E  245  GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER ALA
SEQRES  19 E  245  GLU ALA TRP GLY ARG ALA ASP CYS GLY PHE THR
MODRES 1FYT ASN A   78  ASN  GLYCOSYLATION SITE
MODRES 1FYT ASN A  118  ASN  GLYCOSYLATION SITE
HET    NAG  A 501      14
HET    NAG  A 511      14
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL   6  NAG    2(C8 H15 N O6)
FORMUL   8  HOH   *100(H2 O)
HELIX    1   1 GLU A   47  ALA A   52  1                                   6
HELIX    2   2 ALA A   56  SER A   77  1                                  22
HELIX    3   3 THR B   51  LEU B   53  5                                   3
HELIX    4   4 GLY B   54  SER B   63  1                                  10
HELIX    5   5 GLN B   64  ALA B   73  1                                  10
HELIX    6   6 ALA B   73  TYR B   78  1                                   6
HELIX    7   7 TYR B   78  GLU B   87  1                                  10
HELIX    8   8 ILE D   59  GLY D   61  5                                   3
HELIX    9   9 HIS D   81  ALA D   85  5                                   5
HELIX   10  10 ALA D  188  PHE D  193  1                                   6
HELIX   11  11 SER E   83  THR E   87  5                                   5
HELIX   12  12 ASP E  119  VAL E  123  5                                   5
HELIX   13  13 SER E  134  GLN E  142  1                                   9
HELIX   14  14 ALA E  201  GLN E  205  1                                   5
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  O  HIS A  33   N  VAL A  42
SHEET    3   A 8 SER A  19  PHE A  26 -1  O  PHE A  22   N  VAL A  34
SHEET    4   A 8 HIS A   5  LEU A  14 -1  O  ILE A   8   N  ASP A  25
SHEET    5   A 8 LEU B   8  PHE B  18 -1  N  TRP B   9   O  TYR A  13
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  ARG B  23   N  PHE B  18
SHEET    7   A 8 GLU B  35  ASP B  41 -1  N  GLU B  35   O  TYR B  32
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   B 4 GLU A  88  THR A  93  0
SHEET    2   B 4 ASN A 103  PHE A 112 -1  N  ILE A 106   O  LEU A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  N  PHE A 145   O  PHE A 112
SHEET    4   B 4 SER A 133  GLU A 134 -1  O  SER A 133   N  TYR A 150
SHEET    1   C 4 GLU A  88  THR A  93  0
SHEET    2   C 4 ASN A 103  PHE A 112 -1  N  ILE A 106   O  LEU A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  N  PHE A 145   O  PHE A 112
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146
SHEET    1   D 4 LYS A 126  VAL A 128  0
SHEET    2   D 4 ASN A 118  ARG A 123 -1  O  TRP A 121   N  VAL A 128
SHEET    3   D 4 TYR A 161  GLU A 166 -1  O  ASP A 162   N  LEU A 122
SHEET    4   D 4 LEU A 174  TRP A 178 -1  O  LEU A 174   N  VAL A 165
SHEET    1   E 4 LYS B  98  PRO B 103  0
SHEET    2   E 4 LEU B 115  PHE B 122 -1  N  VAL B 116   O  TYR B 102
SHEET    3   E 4 PHE B 155  LEU B 161 -1  N  PHE B 155   O  PHE B 122
SHEET    4   E 4 VAL B 142  SER B 144 -1  O  VAL B 143   N  MET B 160
SHEET    1   F 4 LYS B  98  PRO B 103  0
SHEET    2   F 4 LEU B 115  PHE B 122 -1  N  VAL B 116   O  TYR B 102
SHEET    3   F 4 PHE B 155  LEU B 161 -1  N  PHE B 155   O  PHE B 122
SHEET    4   F 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156
SHEET    1   G 4 GLN B 136  GLU B 138  0
SHEET    2   G 4 GLU B 128  ARG B 133 -1  O  TRP B 131   N  GLU B 138
SHEET    3   G 4 TYR B 171  GLU B 176 -1  N  THR B 172   O  PHE B 132
SHEET    4   G 4 LEU B 184  TRP B 188 -1  O  LEU B 184   N  VAL B 175
SHEET    1   H 2 SER D   2  THR D   4  0
SHEET    2   H 2 ASN D  23  SER D  25 -1  O  ASN D  23   N  THR D   4
SHEET    1   I 4 GLN D  44  TYR D  49  0
SHEET    2   I 4 TYR D  31  GLN D  37 -1  O  LEU D  32   N  TYR D  49
SHEET    3   I 4 ALA D  86  SER D  93 -1  O  GLU D  87   N  GLN D  37
SHEET    4   I 4 LEU D 104  PHE D 106 -1  N  THR D 105   O  VAL D  92
SHEET    1   J 5 GLN D  44  TYR D  49  0
SHEET    2   J 5 TYR D  31  GLN D  37 -1  O  LEU D  32   N  TYR D  49
SHEET    3   J 5 ALA D  86  SER D  93 -1  O  GLU D  87   N  GLN D  37
SHEET    4   J 5 THR D 110  ILE D 115 -1  O  THR D 110   N  TYR D  88
SHEET    5   J 5 HIS D   9  SER D  13  1  N  VAL D  10   O  ARG D 111
SHEET    1   K 4 VAL D  18  LEU D  20  0
SHEET    2   K 4 SER D  72  LYS D  77 -1  O  LEU D  75   N  LEU D  20
SHEET    3   K 4 GLU D  63  LYS D  67 -1  O  GLU D  63   N  THR D  76
SHEET    4   K 4 LEU D  55  LYS D  57 -1  N  VAL D  56   O  ALA D  64
SHEET    1   L 4 ALA D 124  LEU D 128  0
SHEET    2   L 4 SER D 137  THR D 142 -1  O  VAL D 138   N  LEU D 128
SHEET    3   L 4 PHE D 173  SER D 182 -1  O  ALA D 178   N  PHE D 141
SHEET    4   L 4 TYR D 159  ILE D 160 -1  N  TYR D 159   O  TRP D 181
SHEET    1   M 4 ALA D 124  LEU D 128  0
SHEET    2   M 4 SER D 137  THR D 142 -1  O  VAL D 138   N  LEU D 128
SHEET    3   M 4 PHE D 173  SER D 182 -1  O  ALA D 178   N  PHE D 141
SHEET    4   M 4 THR D 164  MET D 168 -1  N  THR D 164   O  SER D 177
SHEET    1   N 2 VAL E   4  THR E   5  0
SHEET    2   N 2 VAL E  24  GLN E  25 -1  N  VAL E  24   O  THR E   5
SHEET    1   O 5 GLU E  56  LYS E  57  0
SHEET    2   O 5 GLY E  42  SER E  49 -1  O  PHE E  48   N  GLU E  56
SHEET    3   O 5 ASN E  31  ASP E  38 -1  O  MET E  32   N  SER E  49
SHEET    4   O 5 SER E  88  SER E  95 -1  O  MET E  89   N  GLN E  37
SHEET    5   O 5 THR E 107  PHE E 108 -1  O  THR E 107   N  SER E  94
SHEET    1   P 6 GLU E  56  LYS E  57  0
SHEET    2   P 6 GLY E  42  SER E  49 -1  O  PHE E  48   N  GLU E  56
SHEET    3   P 6 ASN E  31  ASP E  38 -1  O  MET E  32   N  SER E  49
SHEET    4   P 6 SER E  88  SER E  95 -1  O  MET E  89   N  GLN E  37
SHEET    5   P 6 THR E 112  VAL E 117 -1  O  THR E 112   N  TYR E  90
SHEET    6   P 6 TYR E  10  ARG E  14  1  O  LEU E  11   N  THR E 115
SHEET    1   Q 3 VAL E  19  LEU E  21  0
SHEET    2   Q 3 SER E  76  LEU E  79 -1  N  LEU E  77   O  LEU E  21
SHEET    3   Q 3 TYR E  65  SER E  68 -1  O  SER E  66   N  ILE E  78
SHEET    1   R 4 GLU E 127  PHE E 131  0
SHEET    2   R 4 LYS E 143  PHE E 153 -1  O  VAL E 147   N  PHE E 131
SHEET    3   R 4 TYR E 191  SER E 200 -1  N  TYR E 191   O  PHE E 153
SHEET    4   R 4 VAL E 173  THR E 175 -1  O  SER E 174   N  ARG E 196
SHEET    1   S 4 GLU E 127  PHE E 131  0
SHEET    2   S 4 LYS E 143  PHE E 153 -1  O  VAL E 147   N  PHE E 131
SHEET    3   S 4 TYR E 191  SER E 200 -1  N  TYR E 191   O  PHE E 153
SHEET    4   S 4 LEU E 180  LYS E 181 -1  N  LEU E 180   O  SER E 192
SHEET    1   T 4 LYS E 167  VAL E 169  0
SHEET    2   T 4 VAL E 158  VAL E 164 -1  O  TRP E 162   N  VAL E 169
SHEET    3   T 4 HIS E 210  PHE E 217 -1  O  ARG E 212   N  TRP E 163
SHEET    4   T 4 GLN E 236  TRP E 243 -1  O  GLN E 236   N  PHE E 217
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.05
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.06
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.04
SSBOND   4 CYS D   22    CYS D   90                          1555   1555  2.03
SSBOND   5 CYS D  139    CYS D  189                          1555   1555  2.05
SSBOND   6 CYS E   23    CYS E   92                          1555   1555  2.03
SSBOND   7 CYS E  148    CYS E  213                          1555   1555  2.03
LINK         ND2 ASN A  78                 C1  NAG A 501     1555   1555  1.45
LINK         ND2 ASN A 118                 C1  NAG A 511     1555   1555  1.46
CISPEP   1 THR A  113    PRO A  114          0        -1.74
CISPEP   2 TYR B  123    PRO B  124          0         0.49
CISPEP   3 PHE E  154    PRO E  155          0         0.58
SITE     1 AC1  3 ARG A  76  SER A  77  ASN A  78
SITE     1 AC2  3 ASN A 118  GLU A 166  TRP A 168
CRYST1  142.902   73.439  122.428  90.00 108.23  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      0.006998  0.000000  0.002304        0.00000
SCALE2      0.000000  0.013617  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008599        0.00000
      
PROCHECK
Go to PROCHECK summary
 References