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PDBsum entry 2fse

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Immune system, structural protein PDB id
2fse
Jmol
Contents
Protein chains
178 a.a.
186 a.a.
14 a.a.
Waters ×31
HEADER    IMMUNE SYSTEM, STRUCTURAL PROTEIN       22-JAN-06   2FSE
TITLE     CRYSTALLOGRAPHIC STRUCTURE OF A RHEUMATOID ARTHRITIS MHC
TITLE    2 SUSCEPTIBILITY ALLELE, HLA-DR1 (DRB1*0101), COMPLEXED WITH
TITLE    3 THE IMMUNODOMINANT DETERMINANT OF HUMAN TYPE II COLLAGEN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, E-K
COMPND   3 ALPHA CHAIN;
COMPND   4 CHAIN: A, C;
COMPND   5 ENGINEERED: YES;
COMPND   6 OTHER_DETAILS: CHAINS A AND C FORM A CHIMERA WITH CHAINS B
COMPND   7 AND D, RESPECTIVELY;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1
COMPND  10 BETA CHAIN;
COMPND  11 CHAIN: B, D;
COMPND  12 ENGINEERED: YES;
COMPND  13 OTHER_DETAILS: CHAINS B AND D FORM A CHIMERA WITH CHAINS A
COMPND  14 AND C, RESPECTIVELY;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: COLLAGEN ALPHA-1(II);
COMPND  17 CHAIN: E, F;
COMPND  18 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRMHA-3;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE  13 ORGANISM_TAXID: 10090;
SOURCE  14 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PRMHA-3;
SOURCE  19 MOL_ID: 3;
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  21 ORGANISM_COMMON: HUMAN;
SOURCE  22 ORGANISM_TAXID: 9606;
SOURCE  23 GENE: COL2A1;
SOURCE  24 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE  25 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  28 EXPRESSION_SYSTEM_PLASMID: PRMHA-3
KEYWDS    RHEUMATOID ARTHRITIS, HLA-DR1, COLLAGEN TYPE II, CRYSTAL
KEYWDS   2 STRUCTURE, ANTIGEN PRESENTATION, IMMUNE SYSTEM, STRUCTURAL
KEYWDS   3 PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.A.IVEY,E.F.ROSLONIEC,K.B.WHITTINGTON,A.H.KANG,H.W.PARK
REVDAT   2   24-FEB-09 2FSE    1       VERSN
REVDAT   1   19-SEP-06 2FSE    0
JRNL        AUTH   E.F.ROSLONIEC,R.A.IVEY,K.B.WHITTINGTON,A.H.KANG,
JRNL        AUTH 2 H.W.PARK
JRNL        TITL   CRYSTALLOGRAPHIC STRUCTURE OF A RHEUMATOID
JRNL        TITL 2 ARTHRITIS MHC SUSCEPTIBILITY ALLELE, HLA-DR1
JRNL        TITL 3 (DRB1*0101), COMPLEXED WITH THE IMMUNODOMINANT
JRNL        TITL 4 DETERMINANT OF HUMAN TYPE II COLLAGEN.
JRNL        REF    J.IMMUNOL.                    V. 177  3884 2006
JRNL        REFN                   ISSN 0022-1767
JRNL        PMID   16951351
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1936.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.4
REMARK   3   NUMBER OF REFLECTIONS             : 17458
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.222
REMARK   3   FREE R VALUE                     : 0.295
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1712
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6185
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 31
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.88
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -6.42300
REMARK   3    B22 (A**2) : 7.82700
REMARK   3    B33 (A**2) : -1.40400
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 15.01
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  : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2FSE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-06.
REMARK 100 THE RCSB ID CODE IS RCSB036254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 77
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20446
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 91.287
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.4
REMARK 200  DATA REDUNDANCY                : 2.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.09900
REMARK 200   FOR THE DATA SET  : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.38200
REMARK 200   FOR SHELL         : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENE GLYCOL 3,350 AND
REMARK 280  200 MM AMMONIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.40500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.27500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.50000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.27500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.40500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.50000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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     ARG B     4
REMARK 465     GLU C   181
REMARK 465     ALA D   190
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   CG   GLN D   110     CG1  VAL D   164              1.74
REMARK 500   NE2  GLN D   110     CG   GLN D   166              2.03
REMARK 500   CH2  TRP C   168     NH1  ARG D     6              2.18
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 D   5   CA  -  N   -  CD  ANGL. DEV. = -11.5 DEGREES
REMARK 500    PRO D   5   C   -  N   -  CD  ANGL. DEV. = -21.6 DEGREES
REMARK 500    ARG D   6   CB  -  CA  -  C   ANGL. DEV. = -14.2 DEGREES
REMARK 500    PRO D 103   CA  -  N   -  CD  ANGL. DEV. = -19.1 DEGREES
REMARK 500    GLN D 107   N   -  CA  -  C   ANGL. DEV. =  17.9 DEGREES
REMARK 500    PRO D 108   CA  -  N   -  CD  ANGL. DEV. = -23.1 DEGREES
REMARK 500    PRO D 108   C   -  N   -  CD  ANGL. DEV. = -21.9 DEGREES
REMARK 500    LEU D 109   CA  -  C   -  N   ANGL. DEV. = -17.0 DEGREES
REMARK 500    GLN D 110   C   -  N   -  CA  ANGL. DEV. =  22.7 DEGREES
REMARK 500    GLN D 110   CA  -  C   -  N   ANGL. DEV. = -14.1 DEGREES
REMARK 500    GLY E1000   N   -  CA  -  C   ANGL. DEV. =  15.2 DEGREES
REMARK 500    PHE E1001   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES
REMARK 500    PHE F2001   CB  -  CG  -  CD2 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    PHE F2001   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    PHE F2001   C   -  N   -  CA  ANGL. DEV. =  22.7 DEGREES
REMARK 500    PHE F2001   CA  -  C   -  N   ANGL. DEV. = -24.6 DEGREES
REMARK 500    PHE F2001   O   -  C   -  N   ANGL. DEV. =  13.0 DEGREES
REMARK 500    LYS F2002   C   -  N   -  CA  ANGL. DEV. =  23.3 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    ASP A  17      -37.23    -33.44
REMARK 500    LYS A  75      -60.45    -91.78
REMARK 500    ARG A  76       22.87    -74.57
REMARK 500    SER A 113      145.47   -176.63
REMARK 500    VAL A 136     -177.87    -61.39
REMARK 500    PRO A 155      131.14    -26.42
REMARK 500    HIS A 167      134.42   -171.86
REMARK 500    PRO A 173      150.89    -38.73
REMARK 500    PHE A 180       98.30    -30.99
REMARK 500    ASN B  19       66.69     60.44
REMARK 500    THR B  21       34.50   -149.45
REMARK 500    TYR B  32     -144.30    -83.47
REMARK 500    GLN B  34        4.35   -158.07
REMARK 500    GLU B  46      149.13   -173.53
REMARK 500    TYR B  78      -74.14   -110.52
REMARK 500    CYS B  79      -75.31    -51.89
REMARK 500    THR B  90      -71.17   -113.12
REMARK 500    LEU B 109      154.74    -44.62
REMARK 500    HIS B 112       94.77     76.51
REMARK 500    PRO B 124     -174.54    -58.75
REMARK 500    GLU B 139      -40.71   -134.79
REMARK 500    TRP B 153       63.46     60.21
REMARK 500    THR B 163     -164.25   -163.52
REMARK 500    PRO B 165      113.56    -36.90
REMARK 500    ALA C  37      -74.00    -63.29
REMARK 500    ALA C  68      -71.57    -76.97
REMARK 500    LYS C  75      -62.92   -107.83
REMARK 500    SER C  77        3.62    -68.32
REMARK 500    SER C 113      148.80    172.78
REMARK 500    PRO C 114     -179.46    -67.80
REMARK 500    THR C 120      111.46   -170.18
REMARK 500    ASN C 124       62.56     61.25
REMARK 500    HIS C 143       27.17     49.65
REMARK 500    LEU C 144     -158.45   -111.66
REMARK 500    TRP C 168       -2.21    -59.37
REMARK 500    PRO C 173      151.76    -38.71
REMARK 500    ARG D   6       99.55     67.55
REMARK 500    TYR D  32      -91.23    -71.68
REMARK 500    ASN D  33      -91.17    -89.85
REMARK 500    ASP D  76      -74.69   -100.13
REMARK 500    THR D  77       -4.91    -54.34
REMARK 500    TYR D  78      -75.58   -125.82
REMARK 500    THR D  90      -73.72   -109.33
REMARK 500    PRO D 103     -173.56    -65.70
REMARK 500    THR D 104      -56.39   -135.72
REMARK 500    GLN D 107       48.47    -93.97
REMARK 500    GLN D 110       70.62     62.64
REMARK 500    ASP D 121       87.78     46.96
REMARK 500    GLN D 156      137.92    178.98
REMARK 500    PRO D 165       93.40    -53.21
REMARK 500    PHE E1001      125.82    -26.64
REMARK 500    PHE F2001       96.32     78.63
REMARK 500    PRO F2011      156.01    -45.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE WAS NO SEQUENCE DATABASE REFERENCE AT
REMARK 999 THE TIME OF PROCESSING FOR THE MHC CHAINS.
DBREF  2FSE A    4   180  UNP    P01903   2DRA_HUMAN      29    205
DBREF  2FSE B    4   190  UNP    P04229   2B11_HUMAN      33    219
DBREF  2FSE C    4   180  UNP    P01903   2DRA_HUMAN      29    205
DBREF  2FSE D    4   190  UNP    P04229   2B11_HUMAN      33    219
DBREF  2FSE E  999  1012  UNP    P02458   CO2A1_HUMAN    392    405
DBREF  2FSE F 1999  2012  UNP    P02458   CO2A1_HUMAN    392    405
SEQRES   1 A  178  GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO
SEQRES   2 A  178  ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP
SEQRES   3 A  178  GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL
SEQRES   4 A  178  TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU
SEQRES   5 A  178  ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA
SEQRES   6 A  178  ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO
SEQRES   7 A  178  ILE THR ASN VAL ALA PRO GLU VAL THR VAL LEU SER ARG
SEQRES   8 A  178  SER PRO VAL ASN LEU GLY GLU PRO ASN ILE LEU ILE CYS
SEQRES   9 A  178  PHE ILE ASP LYS PHE SER PRO PRO VAL VAL ASN VAL THR
SEQRES  10 A  178  TRP LEU ARG ASN GLY ARG PRO VAL THR GLU GLY VAL SER
SEQRES  11 A  178  GLU THR VAL PHE LEU PRO ARG ASP ASP HIS LEU PHE ARG
SEQRES  12 A  178  LYS PHE HIS TYR LEU THR PHE LEU PRO SER THR ASP ASP
SEQRES  13 A  178  PHE TYR ASP CYS GLU VAL ASP HIS TRP GLY LEU GLU GLU
SEQRES  14 A  178  PRO LEU ARG LYS HIS TRP GLU PHE GLU
SEQRES   1 B  187  ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE GLU CYS HIS
SEQRES   2 B  187  PHE PHE ASN GLY THR GLU ARG VAL ARG LEU LEU GLU ARG
SEQRES   3 B  187  CYS ILE TYR ASN GLN GLU GLU SER VAL ARG PHE ASP SER
SEQRES   4 B  187  ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY ARG
SEQRES   5 B  187  PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU LEU
SEQRES   6 B  187  GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS ARG HIS
SEQRES   7 B  187  ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN ARG ARG
SEQRES   8 B  187  VAL GLU PRO THR VAL THR VAL TYR PRO THR LYS THR GLN
SEQRES   9 B  187  PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL SER
SEQRES  10 B  187  ASP PHE TYR PRO GLY ASN ILE GLU VAL ARG TRP PHE ARG
SEQRES  11 B  187  ASN GLY LYS GLU GLU GLU THR GLY ILE VAL SER THR GLY
SEQRES  12 B  187  LEU VAL ARG ASN GLY ASP TRP THR PHE GLN THR LEU VAL
SEQRES  13 B  187  MET LEU GLU THR VAL PRO GLN SER GLY GLU VAL TYR THR
SEQRES  14 B  187  CYS GLN VAL GLU HIS PRO SER LEU THR ASP PRO VAL THR
SEQRES  15 B  187  VAL GLU TRP LYS ALA
SEQRES   1 C  178  GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO
SEQRES   2 C  178  ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP
SEQRES   3 C  178  GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL
SEQRES   4 C  178  TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU
SEQRES   5 C  178  ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA
SEQRES   6 C  178  ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO
SEQRES   7 C  178  ILE THR ASN VAL ALA PRO GLU VAL THR VAL LEU SER ARG
SEQRES   8 C  178  SER PRO VAL ASN LEU GLY GLU PRO ASN ILE LEU ILE CYS
SEQRES   9 C  178  PHE ILE ASP LYS PHE SER PRO PRO VAL VAL ASN VAL THR
SEQRES  10 C  178  TRP LEU ARG ASN GLY ARG PRO VAL THR GLU GLY VAL SER
SEQRES  11 C  178  GLU THR VAL PHE LEU PRO ARG ASP ASP HIS LEU PHE ARG
SEQRES  12 C  178  LYS PHE HIS TYR LEU THR PHE LEU PRO SER THR ASP ASP
SEQRES  13 C  178  PHE TYR ASP CYS GLU VAL ASP HIS TRP GLY LEU GLU GLU
SEQRES  14 C  178  PRO LEU ARG LYS HIS TRP GLU PHE GLU
SEQRES   1 D  187  ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE GLU CYS HIS
SEQRES   2 D  187  PHE PHE ASN GLY THR GLU ARG VAL ARG LEU LEU GLU ARG
SEQRES   3 D  187  CYS ILE TYR ASN GLN GLU GLU SER VAL ARG PHE ASP SER
SEQRES   4 D  187  ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU GLY ARG
SEQRES   5 D  187  PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU LEU
SEQRES   6 D  187  GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS ARG HIS
SEQRES   7 D  187  ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN ARG ARG
SEQRES   8 D  187  VAL GLU PRO THR VAL THR VAL TYR PRO THR LYS THR GLN
SEQRES   9 D  187  PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL SER
SEQRES  10 D  187  ASP PHE TYR PRO GLY ASN ILE GLU VAL ARG TRP PHE ARG
SEQRES  11 D  187  ASN GLY LYS GLU GLU GLU THR GLY ILE VAL SER THR GLY
SEQRES  12 D  187  LEU VAL ARG ASN GLY ASP TRP THR PHE GLN THR LEU VAL
SEQRES  13 D  187  MET LEU GLU THR VAL PRO GLN SER GLY GLU VAL TYR THR
SEQRES  14 D  187  CYS GLN VAL GLU HIS PRO SER LEU THR ASP PRO VAL THR
SEQRES  15 D  187  VAL GLU TRP LYS ALA
SEQRES   1 E   14  ALA GLY PHE LYS GLY GLU GLN GLY PRO LYS GLY GLU PRO
SEQRES   2 E   14  GLY
SEQRES   1 F   14  ALA GLY PHE LYS GLY GLU GLN GLY PRO LYS GLY GLU PRO
SEQRES   2 F   14  GLY
FORMUL   7  HOH   *31(H2 O)
HELIX    1   1 LEU A   45  ALA A   52  1                                   8
HELIX    2   2 ALA A   56  ARG A   76  1                                  21
HELIX    3   3 GLY B   54  GLN B   64  1                                  11
HELIX    4   4 GLN B   64  TYR B   78  1                                  15
HELIX    5   5 TYR B   78  GLU B   87  1                                  10
HELIX    6   6 SER B   88  THR B   90  5                                   3
HELIX    7   7 LEU C   45  ARG C   50  1                                   6
HELIX    8   8 GLU C   55  SER C   77  1                                  23
HELIX    9   9 THR D   51  LEU D   53  5                                   3
HELIX   10  10 GLY D   54  GLN D   64  1                                  11
HELIX   11  11 GLN D   64  TYR D   78  1                                  15
HELIX   12  12 TYR D   78  GLU D   87  1                                  10
HELIX   13  13 SER D   88  THR D   90  5                                   3
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  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  26   O  ASP A  29
SHEET    4   A 8 VAL A   6  ASN A  15 -1  N  ILE A   8   O  ASP A  25
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  LEU B  11   N  GLU A  11
SHEET    6   A 8 ARG B  23  ILE B  31 -1  O  ARG B  29   N  LYS B  12
SHEET    7   A 8 GLU B  36  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 4 GLU A  88  SER A  93  0
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  LYS A 147   N  ILE A 109
SHEET    4   B 4 VAL A 132  GLU A 134 -1  N  SER A 133   O  TYR A 150
SHEET    1   C 4 GLU A  88  SER 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  LYS A 147   N  ILE A 109
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146
SHEET    1   D 4 ARG A 126  PRO A 127  0
SHEET    2   D 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  ARG A 126
SHEET    3   D 4 TYR A 161  ASP 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 THR B  98  PRO B 103  0
SHEET    2   E 4 ASN B 113  PHE B 122 -1  O  SER B 118   N  THR B 100
SHEET    3   E 4 PHE B 155  THR B 163 -1  O  PHE B 155   N  PHE B 122
SHEET    4   E 4 ILE B 142  ARG B 149 -1  N  THR B 145   O  LEU B 158
SHEET    1   F 4 LYS B 136  GLU B 137  0
SHEET    2   F 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  LYS B 136
SHEET    3   F 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130
SHEET    4   F 4 VAL B 184  LYS B 189 -1  O  VAL B 186   N  CYS B 173
SHEET    1   G 7 GLU C  40  TRP C  43  0
SHEET    2   G 7 ASP C  29  ASP C  35 -1  N  ASP C  35   O  GLU C  40
SHEET    3   G 7 SER C  19  PHE C  26 -1  N  PHE C  26   O  ASP C  29
SHEET    4   G 7 HIS C   5  ASN C  15 -1  N  ILE C   8   O  ASP C  25
SHEET    5   G 7 PHE D   7  PHE D  18 -1  O  CYS D  15   N  ILE C   7
SHEET    6   G 7 ARG D  23  ILE D  31 -1  O  ILE D  31   N  GLN D  10
SHEET    7   G 7 GLU D  36  ASP D  41 -1  O  PHE D  40   N  GLU D  28
SHEET    1   H 4 GLU C  88  SER C  93  0
SHEET    2   H 4 ASN C 103  PHE C 112 -1  O  ASP C 110   N  GLU C  88
SHEET    3   H 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105
SHEET    4   H 4 VAL C 132  GLU C 134 -1  N  SER C 133   O  TYR C 150
SHEET    1   I 4 GLU C  88  SER C  93  0
SHEET    2   I 4 ASN C 103  PHE C 112 -1  O  ASP C 110   N  GLU C  88
SHEET    3   I 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105
SHEET    4   I 4 LEU C 138  PRO C 139 -1  N  LEU C 138   O  ARG C 146
SHEET    1   J 4 ARG C 126  PRO C 127  0
SHEET    2   J 4 ASN C 118  ARG C 123 -1  N  ARG C 123   O  ARG C 126
SHEET    3   J 4 TYR C 161  ASP C 166 -1  O  ASP C 162   N  LEU C 122
SHEET    4   J 4 LEU C 174  TRP C 178 -1  O  LEU C 174   N  VAL C 165
SHEET    1   K 4 THR D  98  TYR D 102  0
SHEET    2   K 4 ASN D 113  PHE D 122 -1  O  SER D 120   N  THR D  98
SHEET    3   K 4 PHE D 155  THR D 163 -1  O  LEU D 161   N  LEU D 115
SHEET    4   K 4 VAL D 143  ARG D 149 -1  N  THR D 145   O  LEU D 158
SHEET    1   L 4 LYS D 136  GLU D 137  0
SHEET    2   L 4 GLU D 128  ARG D 133 -1  N  ARG D 133   O  LYS D 136
SHEET    3   L 4 TYR D 171  GLU D 176 -1  O  GLN D 174   N  ARG D 130
SHEET    4   L 4 VAL D 184  TRP D 188 -1  O  VAL D 186   N  CYS D 173
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.04
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.04
SSBOND   4 CYS C  107    CYS C  163                          1555   1555  2.04
SSBOND   5 CYS D   15    CYS D   79                          1555   1555  2.03
SSBOND   6 CYS D  117    CYS D  173                          1555   1555  2.04
CISPEP   1 ASN A   15    PRO A   16          0         0.30
CISPEP   2 SER A  113    PRO A  114          0         0.07
CISPEP   3 TYR B  123    PRO B  124          0        -0.72
CISPEP   4 ASN C   15    PRO C   16          0         0.19
CISPEP   5 SER C  113    PRO C  114          0        -0.26
CISPEP   6 TYR D  123    PRO D  124          0         0.28
CRYST1   60.810  109.000  170.550  90.00  90.00  90.00 P 21 21 21    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      0.016445  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009174  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005863        0.00000
      
PROCHECK
Go to PROCHECK summary
 References