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PDBsum entry 1t5w

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Top Page protein Protein-protein interface(s) links
Immune system PDB id
1t5w
Jmol
Contents
Protein chains
180 a.a. *
190 a.a. *
13 a.a. *
Waters ×148
* Residue conservation analysis
HEADER    IMMUNE SYSTEM                           05-MAY-04   1T5W
TITLE     HLA-DR1 IN COMPLEX WITH A SYNTHETIC PEPTIDE
TITLE    2 (AAYSDQATPLLLSPR)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR
COMPND   3 ALPHA CHAIN;
COMPND   4 CHAIN: A, D;
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAIN;
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, E;
COMPND  12 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND  13 SYNONYM: MHC CLASS I ANTIGEN DRB1*1, DR-1, DR1;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: 15-MER PEPTIDE FRAGMENT OF REGULATORY PROTEIN
COMPND  17 MIG1;
COMPND  18 CHAIN: C, F;
COMPND  19 FRAGMENT: SYNTHETIC PEPTIDE;
COMPND  20 SYNONYM: REGULATORY PROTEIN CAT4;
COMPND  21 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DRA;
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: S2;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PRMAHA-3;
SOURCE  12 MOL_ID: 2;
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  14 ORGANISM_COMMON: HUMAN;
SOURCE  15 ORGANISM_TAXID: 9606;
SOURCE  16 GENE: HLA-DRB1;
SOURCE  17 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE  18 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: S2;
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PRMHA-3;
SOURCE  23 MOL_ID: 3;
SOURCE  24 SYNTHETIC: YES;
SOURCE  25 OTHER_DETAILS: SYNTHETIC PEPTIDE DESINGED TO STUDY THE P10
SOURCE  26 SIDE CHAIN SPECIFICITY OF HLA-DR1
KEYWDS    MHC CLASS II; NAJOR HISTOCOMPATIBILITY COMPLEX PROTEIN; HLA-
KEYWDS   2 DR1; ANTIGEN; PEPTIDE, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Z.ZAVALA-RUIZ,I.STRUG,M.W.ANDERSON,J.GORSKI,L.J.STERN
REVDAT   3   24-FEB-09 1T5W    1       VERSN
REVDAT   2   01-FEB-05 1T5W    1       JRNL   REMARK
REVDAT   1   17-AUG-04 1T5W    0
JRNL        AUTH   Z.ZAVALA-RUIZ,I.STRUG,M.W.ANDERSON,J.GORSKI,
JRNL        AUTH 2 L.J.STERN
JRNL        TITL   A POLYMORPHIC POCKET AT THE P10 POSITION
JRNL        TITL 2 CONTRIBUTES TO PEPTIDE BINDING SPECIFICITY IN
JRNL        TITL 3 CLASS II MHC PROTEINS
JRNL        REF    CHEM.BIOL.                    V.  11  1395 2004
JRNL        REFN                   ISSN 1074-5521
JRNL        PMID   15489166
JRNL        DOI    10.1016/J.CHEMBIOL.2004.08.007
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.90
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)   (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 44322
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) : 0.231
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 3143
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) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020
REMARK   3   BIN FREE R VALUE                    : 0.3440
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 532
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6259
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 148
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -10.81000
REMARK   3    B22 (A**2) : 20.61000
REMARK   3    B33 (A**2) : -9.80000
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) : 0.32
REMARK   3   ESD FROM SIGMAA              (A) : 0.31
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) : 0.36
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81
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 1T5W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-04.
REMARK 100 THE RCSB ID CODE IS RCSB022351.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X25
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1000
REMARK 200  MONOCHROMATOR                  : CYLINDRICAL PLATINUM-COATED
REMARK 200                                   SILICON MIRROR
REMARK 200  OPTICS                         : CYLINDRICAL PLATINUM-COATED
REMARK 200                                   SILICON MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44505
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.900
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 6.000
REMARK 200  R MERGE                    (I) : 0.05300
REMARK 200  R SYM                      (I) : 0.06500
REMARK 200   FOR THE DATA SET  : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.31200
REMARK 200  R SYM FOR SHELL            (I) : 0.37800
REMARK 200   FOR SHELL         : 3.500
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 1AQD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, PH 4.0, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.48800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.48800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       48.27700
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.32300
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       48.27700
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.32300
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      103.48800
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       48.27700
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.32300
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      103.48800
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       48.27700
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.32300
REMARK 290   SMTRY3   8  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 300 REMARK: TOW MOLECULES IN THE ASYMTERIC UNIT ARE RELATED BY AN
REMARK 300 APPROXIMATE 2-FOLD AXIS
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: 7290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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: 7280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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    13
REMARK 465     ARG C    14
REMARK 465     LYS D     2
REMARK 465     PRO F    13
REMARK 465     ARG F    14
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475   M RES C SSEQI
REMARK 475     LYS A    2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     PRO B  108   CB    CG    CD
REMARK 480     LEU B  109   CB    CG    CD1   CD2
REMARK 480     GLN B  110   CB    CG    CD    OE1   NE2
REMARK 480     VAL B  170   CB    CG1   CG2
REMARK 480     ARG B  189   CB    CG    CD    NE    CZ    NH1   NH2
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              2.08
REMARK 500   O    LEU E     8     O    TYR E    32              2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NE2  GLN A    57     NE2  GLN A    57     4555     1.83
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    ARG B 166   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG B 166   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG E 166   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG E 166   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    ASN A  78       44.09     73.60
REMARK 500    THR A 113      146.62   -172.54
REMARK 500    TYR B  32      -92.10    -68.29
REMARK 500    ASN B  33      -76.59    -92.52
REMARK 500    THR B  90      -71.82   -119.53
REMARK 500    LYS B 105      132.10     66.46
REMARK 500    ASN D  78       42.43     72.99
REMARK 500    THR D 113      146.89   -173.24
REMARK 500    TYR E  32      -93.65    -68.61
REMARK 500    ASN E  33      -75.76    -91.07
REMARK 500    THR E  90      -74.61   -118.71
REMARK 500    LYS E 105      131.66     65.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DLH   RELATED DB: PDB
REMARK 900 HLA-DR1/HA, SIMILAR TO CURRENT ENTRY BUT WITH A DIFFERENT
REMARK 900 PEPTIDE BOUND TO HLA-DR1
REMARK 900 RELATED ID: 1AQD   RELATED DB: PDB
REMARK 900 HLA-DR1/A2, SIMILAR TO CURRENT ENTRY BUT WITH A DIFFERENT
REMARK 900 PEPTIDE BOUND TO HLA-DR1
REMARK 900 RELATED ID: 1T5X   RELATED DB: PDB
DBREF  1T5W A    2   181  UNP    P01903   2DRA_HUMAN      27    206
DBREF  1T5W D    2   181  UNP    P01903   2DRA_HUMAN      27    206
DBREF  1T5W B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  1T5W E    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  1T5W C    7    14  UNP    P27705   MIG1_YEAST     455    462
DBREF  1T5W F    7    14  UNP    P27705   MIG1_YEAST     455    462
SEQADV 1T5W ALA C    0  UNP  P27705              INSERTION
SEQADV 1T5W ALA C    1  UNP  P27705              INSERTION
SEQADV 1T5W TYR C    2  UNP  P27705              INSERTION
SEQADV 1T5W SER C    3  UNP  P27705              INSERTION
SEQADV 1T5W ASP C    4  UNP  P27705              INSERTION
SEQADV 1T5W GLN C    5  UNP  P27705              INSERTION
SEQADV 1T5W ALA C    6  UNP  P27705              INSERTION
SEQADV 1T5W ALA F    0  UNP  P27705              INSERTION
SEQADV 1T5W ALA F    1  UNP  P27705              INSERTION
SEQADV 1T5W TYR F    2  UNP  P27705              INSERTION
SEQADV 1T5W SER F    3  UNP  P27705              INSERTION
SEQADV 1T5W ASP F    4  UNP  P27705              INSERTION
SEQADV 1T5W GLN F    5  UNP  P27705              INSERTION
SEQADV 1T5W ALA F    6  UNP  P27705              INSERTION
SEQRES   1 A  180  LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU
SEQRES   2 A  180  ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP
SEQRES   3 A  180  GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU
SEQRES   4 A  180  THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER
SEQRES   5 A  180  PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP
SEQRES   6 A  180  LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR
SEQRES   7 A  180  THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU
SEQRES   8 A  180  THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU
SEQRES   9 A  180  ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN
SEQRES  10 A  180  VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY
SEQRES  11 A  180  VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU
SEQRES  12 A  180  PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR
SEQRES  13 A  180  GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU
SEQRES  14 A  180  ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
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   15  ALA ALA TYR SER ASP GLN ALA THR PRO LEU LEU LEU SER
SEQRES   2 C   15  PRO ARG
SEQRES   1 D  180  LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU
SEQRES   2 D  180  ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP
SEQRES   3 D  180  GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU
SEQRES   4 D  180  THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER
SEQRES   5 D  180  PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP
SEQRES   6 D  180  LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR
SEQRES   7 D  180  THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU
SEQRES   8 D  180  THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU
SEQRES   9 D  180  ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN
SEQRES  10 D  180  VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY
SEQRES  11 D  180  VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU
SEQRES  12 D  180  PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR
SEQRES  13 D  180  GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU
SEQRES  14 D  180  ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
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   15  ALA ALA TYR SER ASP GLN ALA THR PRO LEU LEU LEU SER
SEQRES   2 F   15  PRO ARG
FORMUL   7  HOH   *148(H2 O)
HELIX    1   1 LEU A   45  PHE A   51  5                                   7
HELIX    2   2 GLU A   55  SER A   77  1                                  23
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 LEU D   45  PHE D   51  5                                   7
HELIX    8   8 GLU D   55  SER D   77  1                                  23
HELIX    9   9 THR E   51  LEU E   53  5                                   3
HELIX   10  10 GLY E   54  ASN E   62  1                                   9
HELIX   11  11 GLN E   64  TYR E   78  1                                  15
HELIX   12  12 TYR E   78  GLU E   87  1                                  10
HELIX   13  13 SER E   88  THR E   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 HIS A   5  ASN A  15 -1  N  LEU A  14   O  SER A  19
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  CYS B  15   N  ILE A   7
SHEET    6   A 8 ARG B  23  ILE B  31 -1  O  LEU B  27   N  GLU B  14
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  HIS A 149   N  CYS A 107
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  HIS A 149   N  CYS A 107
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 TYR A 161  GLU A 166 -1  O  GLU A 166   N  ASN A 118
SHEET    4   D 4 LEU A 174  TRP A 178 -1  O  TRP A 178   N  TYR A 161
SHEET    1   E 4 LYS B  98  SER B 104  0
SHEET    2   E 4 ASN B 113  PHE B 122 -1  O  LEU B 114   N  SER B 104
SHEET    3   E 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113
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  SER B 104  0
SHEET    2   F 4 ASN B 113  PHE B 122 -1  O  LEU B 114   N  SER B 104
SHEET    3   F 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113
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  TRP B 188   N  TYR B 171
SHEET    1   H 8 GLU D  40  TRP D  43  0
SHEET    2   H 8 ASP D  29  ASP D  35 -1  N  HIS D  33   O  VAL D  42
SHEET    3   H 8 SER D  19  PHE D  26 -1  N  PHE D  26   O  ASP D  29
SHEET    4   H 8 HIS D   5  ASN D  15 -1  N  LEU D  14   O  SER D  19
SHEET    5   H 8 PHE E   7  PHE E  18 -1  O  CYS E  15   N  ILE D   7
SHEET    6   H 8 ARG E  23  ILE E  31 -1  O  ARG E  25   N  HIS E  16
SHEET    7   H 8 GLU E  36  ASP E  41 -1  O  PHE E  40   N  GLU E  28
SHEET    8   H 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39
SHEET    1   I 4 GLU D  88  THR D  93  0
SHEET    2   I 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   I 4 PHE D 145  PHE D 153 -1  O  HIS D 149   N  CYS D 107
SHEET    4   I 4 SER D 133  GLU D 134 -1  N  SER D 133   O  TYR D 150
SHEET    1   J 4 GLU D  88  THR D  93  0
SHEET    2   J 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   J 4 PHE D 145  PHE D 153 -1  O  HIS D 149   N  CYS D 107
SHEET    4   J 4 LEU D 138  PRO D 139 -1  N  LEU D 138   O  ARG D 146
SHEET    1   K 4 LYS D 126  VAL D 128  0
SHEET    2   K 4 ASN D 118  ARG D 123 -1  N  ARG D 123   O  LYS D 126
SHEET    3   K 4 TYR D 161  GLU D 166 -1  O  ARG D 164   N  THR D 120
SHEET    4   K 4 LEU D 174  TRP D 178 -1  O  TRP D 178   N  TYR D 161
SHEET    1   L 4 LYS E  98  SER E 104  0
SHEET    2   L 4 ASN E 113  PHE E 122 -1  O  LEU E 114   N  SER E 104
SHEET    3   L 4 PHE E 155  THR E 163 -1  O  THR E 163   N  ASN E 113
SHEET    4   L 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160
SHEET    1   M 4 LYS E  98  SER E 104  0
SHEET    2   M 4 ASN E 113  PHE E 122 -1  O  LEU E 114   N  SER E 104
SHEET    3   M 4 PHE E 155  THR E 163 -1  O  THR E 163   N  ASN E 113
SHEET    4   M 4 ILE E 148  GLN E 149 -1  N  ILE E 148   O  GLN E 156
SHEET    1   N 4 GLN E 136  GLU E 138  0
SHEET    2   N 4 GLU E 128  ARG E 133 -1  N  ARG E 133   O  GLN E 136
SHEET    3   N 4 VAL E 170  GLU E 176 -1  O  GLN E 174   N  ARG E 130
SHEET    4   N 4 LEU E 184  ARG E 189 -1  O  TRP E 188   N  TYR E 171
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04
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  107    CYS D  163                          1555   1555  2.04
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  2.04
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.03
CISPEP   1 ASN A   15    PRO A   16          0         0.34
CISPEP   2 THR A  113    PRO A  114          0         0.00
CISPEP   3 TYR B  123    PRO B  124          0         0.60
CISPEP   4 ASN D   15    PRO D   16          0         0.22
CISPEP   5 THR D  113    PRO D  114          0        -0.14
CISPEP   6 TYR E  123    PRO E  124          0         0.80
CRYST1   96.554  112.646  206.976  90.00  90.00  90.00 C 2 2 21     16
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      0.010357  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008877  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004831        0.00000
      
PROCHECK
Go to PROCHECK summary
 References