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PDBsum entry 1sje

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Top Page protein Protein-protein interface(s) links
Immune system PDB id
1sje
Jmol
Contents
Protein chains
180 a.a. *
190 a.a. *
15 a.a. *
232 a.a. *
Waters ×249
* Residue conservation analysis
HEADER    IMMUNE SYSTEM                           03-MAR-04   1SJE
TITLE     HLA-DR1 COMPLEXED WITH A 16 RESIDUE HIV CAPSID PEPTIDE
TITLE    2 BOUND IN A HAIRPIN CONFORMATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR
COMPND   3 ALPHA CHAIN;
COMPND   4 CHAIN: A;
COMPND   5 FRAGMENT: EXTRACELLUAR DOMAIN OF HLA-DRA*0101;
COMPND   6 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1
COMPND  10 BETA CHAIN;
COMPND  11 CHAIN: B;
COMPND  12 FRAGMENT: EXTRACELLUAR DOMAIN OF HLA-DRB*0101;
COMPND  13 SYNONYM: MHC CLASS I ANTIGEN DRB1*1, DR-1, DR1;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: GAG POLYPROTEIN;
COMPND  17 CHAIN: C;
COMPND  18 FRAGMENT: 16 RESIDUE PEPTIDE FROM HIV-1 GAG CAPSID PROTEIN;
COMPND  19 ENGINEERED: YES;
COMPND  20 MOL_ID: 4;
COMPND  21 MOLECULE: ENTEROTOXIN TYPE C-3;
COMPND  22 CHAIN: D;
COMPND  23 FRAGMENT: SEC3 VARIANT 3B2;
COMPND  24 SYNONYM: SEC3;
COMPND  25 ENGINEERED: YES;
COMPND  26 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DRA*0101;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 POLYMERASE/LAC;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 GENE: HLA-DRB*0101;
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 POLYMERASE/LAC;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE  21 MOL_ID: 3;
SOURCE  22 SYNTHETIC: YES;
SOURCE  23 OTHER_DETAILS: SYNTHESIZED PEPTIDE WITH SEQUENCE FROM
SOURCE  24 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1) GAG CAPSID
SOURCE  25 PROTEIN[166-181].;
SOURCE  26 MOL_ID: 4;
SOURCE  27 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE  28 ORGANISM_TAXID: 1280;
SOURCE  29 GENE: SEC3;
SOURCE  30 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  32 EXPRESSION_SYSTEM_STRAIN: HB2151;
SOURCE  33 EXPRESSION_SYSTEM_VECTOR_TYPE: LAC
KEYWDS    MHC CLASS II, MAJOR HISTOCOMPATIBILITY PROTEIN COMPLEX, HLA-
KEYWDS   2 DR1, HIV-1, CAPSID, SUPERANTIGEN, ANTIGEN, PEPTIDE, GAG,
KEYWDS   3 IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Z.ZAVALA-RUIZ,I.STRUG,B.D.WALKER,P.J.NORRIS,L.J.STERN
REVDAT   3   24-FEB-09 1SJE    1       VERSN
REVDAT   2   21-SEP-04 1SJE    1       JRNL
REVDAT   1   17-AUG-04 1SJE    0
JRNL        AUTH   Z.ZAVALA-RUIZ,I.STRUG,B.D.WALKER,P.J.NORRIS,
JRNL        AUTH 2 L.J.STERN
JRNL        TITL   A HAIRPIN TURN IN A CLASS II MHC-BOUND PEPTIDE
JRNL        TITL 2 ORIENTS RESIDUES OUTSIDE THE BINDING GROOVE FOR T
JRNL        TITL 3 CELL RECOGNITION.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101 13279 2004
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   15331779
JRNL        DOI    10.1073/PNAS.0403371101
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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) : 2.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 44573
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) : 0.196
REMARK   3   FREE R VALUE                     : 0.223
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 4984
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) : 2.45
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.60
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690
REMARK   3   BIN FREE R VALUE                    : 0.3050
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 804
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5042
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 249
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 40.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.90
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.98000
REMARK   3    B22 (A**2) : 2.58000
REMARK   3    B33 (A**2) : -4.56000
REMARK   3    B12 (A**2) : 4.77000
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) : 0.28
REMARK   3   ESD FROM SIGMAA              (A) : 0.27
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.34
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72
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) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : 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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1SJE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-04.
REMARK 100 THE RCSB ID CODE IS RCSB021759.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : CU K-ALPHA
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : CONFOCAL MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 180 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49701
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 7.500
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : 0.08400
REMARK 200   FOR THE DATA SET  : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.41500
REMARK 200  R SYM FOR SHELL            (I) : 0.41300
REMARK 200   FOR SHELL         : 3.400
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: PDB ENTRY 1PYW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 73.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-MME 5000, ETHYLENE GLYCOL, PH
REMARK 280  5.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.37300
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.86747
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.46633
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       86.37300
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.86747
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.46633
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       86.37300
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.86747
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.46633
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.73495
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       80.93267
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       99.73495
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       80.93267
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       99.73495
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       80.93267
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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      172.74600
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       86.37300
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      149.60242
REMARK 350   BIOMT3   3  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     PRO C    49
REMARK 465     ASP D    99
REMARK 465     ASN D   100
REMARK 465     VAL D   101
REMARK 465     GLY D   102
REMARK 465     LYS D   103
REMARK 465     VAL D   104
REMARK 465     THR D   105
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   O    LEU B     8     O    TYR B    32              2.17
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    ARG A 100       11.32     52.07
REMARK 500    TYR B  32      -85.37    -71.10
REMARK 500    ASN B  33      -75.49    -98.78
REMARK 500    TYR B  78      -66.44   -107.37
REMARK 500    THR B  90      -74.71   -128.22
REMARK 500    THR B 106      -84.53    -79.40
REMARK 500    PRO B 108      -85.44    -61.51
REMARK 500    LEU B 109      108.34    -58.32
REMARK 500    GLN B 110     -104.60    -21.55
REMARK 500    HIS B 111       64.99    -52.11
REMARK 500    PRO B 124     -174.60    -69.65
REMARK 500    TYR D  32      157.32    178.51
REMARK 500    LYS D  37       73.30     53.92
REMARK 500    LYS D  57      -90.44    -57.63
REMARK 500    PHE D  95      147.34    164.85
REMARK 500    ASN D 125       66.05     71.70
REMARK 500    SER D 178      177.16     79.85
REMARK 500    ASN D 191       -5.44    -57.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KLU   RELATED DB: PDB
REMARK 900 HLA-DR1/TPI/SEC3-3B2, SIMILAR TO CURRENT ENTRY BUT WITH A
REMARK 900 DIFFERENT PEPTIDE BOUND TO HLA-DR1
REMARK 900 RELATED ID: 1PYW   RELATED DB: PDB
REMARK 900 HLA-DR1/FVKQNA*AAL/SEC3-3B2 (*A IS N-METHYL ALANINE),
REMARK 900 SIMILAR TO CURRENT ENTRY BUT WITH A DIFFERENT PEPTIDE BOUND
REMARK 900 TO HLA-DR1
REMARK 900 RELATED ID: 1SJH   RELATED DB: PDB
REMARK 900 HLA-DR1 COMPLEXED WITH A 13 RESIDUE HIV CAPSID PEPTIDE
DBREF  1SJE A    3   182  UNP    P01903   2DRA_HUMAN      28    207
DBREF  1SJE B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  1SJE C   34    49  UNP    P12495   GAG_HV1Z2      166    181
DBREF  1SJE D    1   239  UNP    P0A0L5   ENTC3_STAAU     28    266
SEQADV 1SJE SER D   43  UNP  P0A0L5    LYS    70 ENGINEERED
SEQADV 1SJE PHE D   45  UNP  P0A0L5    LEU    72 ENGINEERED
SEQADV 1SJE LYS D   46  UNP  P0A0L5    ALA    73 ENGINEERED
SEQADV 1SJE TRP D   47  UNP  P0A0L5    HIS    74 ENGINEERED
SEQRES   1 A  180  GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN
SEQRES   2 A  180  PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY
SEQRES   3 A  180  ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR
SEQRES   4 A  180  VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE
SEQRES   5 A  180  GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS
SEQRES   6 A  180  ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR THR
SEQRES   7 A  180  PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR
SEQRES   8 A  180  ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE
SEQRES   9 A  180  CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL
SEQRES  10 A  180  THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL
SEQRES  11 A  180  SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE
SEQRES  12 A  180  ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU
SEQRES  13 A  180  ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP
SEQRES  14 A  180  GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 B  190  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 B  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 B  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 B  190  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 B  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 B  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 B  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 B  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 B  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 B  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 B  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 B  190  PRO LEU THR VAL GLU TRP ARG ALA
SEQRES   1 C   16  PRO GLU VAL ILE PRO MET PHE SER ALA LEU SER GLU GLY
SEQRES   2 C   16  ALA THR PRO
SEQRES   1 D  239  GLU SER GLN PRO ASP PRO MET PRO ASP ASP LEU HIS LYS
SEQRES   2 D  239  SER SER GLU PHE THR GLY THR MET GLY ASN MET LYS TYR
SEQRES   3 D  239  LEU TYR ASP ASP HIS TYR VAL SER ALA THR LYS VAL LYS
SEQRES   4 D  239  SER VAL ASP SER PHE PHE LYS TRP ASP LEU ILE TYR ASN
SEQRES   5 D  239  ILE SER ASP LYS LYS LEU LYS ASN TYR ASP LYS VAL LYS
SEQRES   6 D  239  THR GLU LEU LEU ASN GLU ASP LEU ALA LYS LYS TYR LYS
SEQRES   7 D  239  ASP GLU VAL VAL ASP VAL TYR GLY SER ASN TYR TYR VAL
SEQRES   8 D  239  ASN CYS TYR PHE SER SER LYS ASP ASN VAL GLY LYS VAL
SEQRES   9 D  239  THR GLY GLY LYS THR CYS MET TYR GLY GLY ILE THR LYS
SEQRES  10 D  239  HIS GLU GLY ASN HIS PHE ASP ASN GLY ASN LEU GLN ASN
SEQRES  11 D  239  VAL LEU VAL ARG VAL TYR GLU ASN LYS ARG ASN THR ILE
SEQRES  12 D  239  SER PHE GLU VAL GLN THR ASP LYS LYS SER VAL THR ALA
SEQRES  13 D  239  GLN GLU LEU ASP ILE LYS ALA ARG ASN PHE LEU ILE ASN
SEQRES  14 D  239  LYS LYS ASN LEU TYR GLU PHE ASN SER SER PRO TYR GLU
SEQRES  15 D  239  THR GLY TYR ILE LYS PHE ILE GLU ASN ASN GLY ASN THR
SEQRES  16 D  239  PHE TRP TYR ASP MET MET PRO ALA PRO GLY ASP LYS PHE
SEQRES  17 D  239  ASP GLN SER LYS TYR LEU MET MET TYR ASN ASP ASN LYS
SEQRES  18 D  239  THR VAL ASP SER LYS SER VAL LYS ILE GLU VAL HIS LEU
SEQRES  19 D  239  THR THR LYS ASN GLY
FORMUL   5  HOH   *249(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  TYR B   78  1                                  15
HELIX    6   6 TYR B   78  GLU B   87  1                                  10
HELIX    7   7 SER B   88  THR B   90  5                                   3
HELIX    8   8 MET D    7  LEU D   11  5                                   5
HELIX    9   9 LYS D   13  PHE D   17  5                                   5
HELIX   10  10 MET D   21  ASP D   29  1                                   9
HELIX   11  11 ASN D   70  ASP D   79  1                                  10
HELIX   12  12 ALA D  156  ASN D  172  1                                  17
HELIX   13  13 ASP D  209  MET D  215  1                                   7
HELIX   14  14 MET D  216  ASN D  220  5                                   5
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  ASP A  35   O  GLU A  40
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  ALA A  10   O  MET A  23
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  PHE B  17   N  HIS A   5
SHEET    6   A 8 ARG B  23  ILE B  31 -1  O  ARG B  25   N  HIS B  16
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  THR 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  LEU A 151   N  LEU A 105
SHEET    4   B 4 SER A 133  GLU A 134 -1  N  SER A 133   O  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  O  ILE A 106   N  LEU A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105
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  N  ARG A 123   O  LYS A 126
SHEET    3   D 4 VAL A 160  GLU A 166 -1  O  ARG A 164   N  THR A 120
SHEET    4   D 4 LEU A 174  GLU A 179 -1  O  TRP A 178   N  TYR A 161
SHEET    1   E 4 LYS B  98  PRO B 103  0
SHEET    2   E 4 ASN B 113  PHE B 122 -1  O  SER B 120   N  LYS B  98
SHEET    3   E 4 PHE B 155  THR B 163 -1  O  LEU B 161   N  LEU B 115
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   F 4 LYS B  98  PRO B 103  0
SHEET    2   F 4 ASN B 113  PHE B 122 -1  O  SER B 120   N  LYS B  98
SHEET    3   F 4 PHE B 155  THR B 163 -1  O  LEU B 161   N  LEU B 115
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 137  0
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136
SHEET    3   G 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175
SHEET    1   H 3 VAL D  33  VAL D  38  0
SHEET    2   H 3 VAL D  82  GLY D  86 -1  O  VAL D  82   N  VAL D  38
SHEET    3   H 3 ILE D 115  LYS D 117 -1  O  THR D 116   N  ASP D  83
SHEET    1   I 3 ASP D  48  TYR D  51  0
SHEET    2   I 3 LYS D  63  GLU D  67 -1  O  THR D  66   N  LEU D  49
SHEET    3   I 3 LYS D 108  TYR D 112  1  O  MET D 111   N  GLU D  67
SHEET    1   J 5 ARG D 140  THR D 149  0
SHEET    2   J 5 GLN D 129  GLU D 137 -1  N  VAL D 133   O  PHE D 145
SHEET    3   J 5 LYS D 229  THR D 235  1  O  LEU D 234   N  TYR D 136
SHEET    4   J 5 THR D 183  ILE D 189 -1  N  LYS D 187   O  GLU D 231
SHEET    5   J 5 THR D 195  ASP D 199 -1  O  PHE D 196   N  PHE D 188
SHEET    1   K 2 SER D 153  THR D 155  0
SHEET    2   K 2 THR D 222  ASP D 224 -1  O  VAL D 223   N  VAL D 154
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.06
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03
SSBOND   4 CYS D   93    CYS D  110                          1555   1555  2.04
CISPEP   1 ASN A   15    PRO A   16          0        -0.14
CISPEP   2 THR A  113    PRO A  114          0         0.22
CISPEP   3 TYR B  123    PRO B  124          0         0.01
CRYST1  172.746  172.746  121.399  90.00  90.00 120.00 H 3           9
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      0.005789  0.003342  0.000000        0.00000
SCALE2      0.000000  0.006684  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008237        0.00000
      
PROCHECK
Go to PROCHECK summary
 References