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PDBsum entry 1es0

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Top Page protein Protein-protein interface(s) links
Immune system PDB id
1es0
Jmol
Contents
Protein chains
182 a.a. *
190 a.a. *
Waters ×76
* Residue conservation analysis
HEADER    IMMUNE SYSTEM                           07-APR-00   1ES0
TITLE     CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH
TITLE    2 THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: ALPHA CHAIN;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: 65 KD GLUTAMIC ACID DECARBOXYLASE+H-2 CLASS II
COMPND   8 HISTOCOMPATIBILITY ANTIGEN;
COMPND   9 CHAIN: B;
COMPND  10 FRAGMENT: PEPTIDE (RESIDUES 222-235) + BETA CHAIN;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 EXPRESSION_SYSTEM_COMMON: INSECT;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   8 ORGANISM_COMMON: HUMAN;
SOURCE   9 ORGANISM_TAXID: 9606;
SOURCE  10 EXPRESSION_SYSTEM_COMMON: INSECT
KEYWDS    HISTOCOMPATIBILITY ANTIGEN, CLASS II MHC I-A(G7), IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.L.CORPER,L.TEYTON,I.A.WILSON
REVDAT   4   13-JUL-11 1ES0    1       VERSN
REVDAT   3   24-FEB-09 1ES0    1       VERSN
REVDAT   2   01-APR-03 1ES0    1       JRNL
REVDAT   1   28-JUN-00 1ES0    0
JRNL        AUTH   A.L.CORPER,T.STRATMANN,V.APOSTOLOPOULOS,C.A.SCOTT,
JRNL        AUTH 2 K.C.GARCIA,A.S.KANG,I.A.WILSON,L.TEYTON
JRNL        TITL   A STRUCTURAL FRAMEWORK FOR DECIPHERING THE LINK BETWEEN
JRNL        TITL 2 I-AG7 AND AUTOIMMUNE DIABETES.
JRNL        REF    SCIENCE                       V. 288   505 2000
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   10775108
JRNL        DOI    10.1126/SCIENCE.288.5465.505
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) : 39.96
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)   (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 15754
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) : 0.210
REMARK   3   FREE R VALUE                     : 0.258
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 1541
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007
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) (%) : 99.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1396
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760
REMARK   3   BIN FREE R VALUE                    : 0.3440
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 149
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            : 3012
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 76
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 51.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 8.00000
REMARK   3    B22 (A**2) : -3.51000
REMARK   3    B33 (A**2) : -4.50000
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) : 0.30
REMARK   3   ESD FROM SIGMAA              (A) : 0.28
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) : 0.39
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
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 : GROUP
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 : FLAT MODEL
REMARK   3   KSOL        : 0.35
REMARK   3   BSOL        : 32.63
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  : CIS_PEPTIDE.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   : CIS_PEPTIDE.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1ES0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-00.
REMARK 100 THE RCSB ID CODE IS RCSB010843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-JAN-99
REMARK 200  TEMPERATURE           (KELVIN) : 96.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL7-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15754
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.960
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3
REMARK 200  DATA REDUNDANCY                : 4.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06800
REMARK 200   FOR THE DATA SET  : 15.7000
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     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.35300
REMARK 200   FOR SHELL         : 4.200
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: I-A(K) - PDB CODE 1IAK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-18% PEG 4000, 0.2 M LICL (PH 6.6),
REMARK 280  1% MPD, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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       48.04200
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       48.04200
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       47.57450
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.06150
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.57450
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.06150
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.04200
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.57450
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.06150
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.04200
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.57450
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.06150
REMARK 290   SMTRY3   8  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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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     GLU A     1D
REMARK 465     ASP A     1C
REMARK 465     ALA A   181
REMARK 465     ASP A   182
REMARK 465     LEU A   183
REMARK 465     VAL A   184
REMARK 465     PRO A   185
REMARK 465     ARG A   186
REMARK 465     GLY B   201P
REMARK 465     SER B   202P
REMARK 465     HIS B   203P
REMARK 465     SER B   204P
REMARK 465     ARG B   205P
REMARK 465     GLY B   206P
REMARK 465     GLY B    -5
REMARK 465     SER B    -4
REMARK 465     GLY B    -3
REMARK 465     SER B    -2
REMARK 465     GLY B    -1
REMARK 465     SER B     0
REMARK 465     GLY B     1
REMARK 465     ASP B     2
REMARK 465     SER B     3
REMARK 465     GLU B     4
REMARK 465     ARG B   105
REMARK 465     THR B   106
REMARK 465     GLU B   107
REMARK 465     ALA B   108
REMARK 465     LEU B   109
REMARK 465     ASN B   110
REMARK 465     HIS B   111
REMARK 465     HIS B   112
REMARK 465     SER B   190
REMARK 465     ALA B   191
REMARK 465     ASP B   192
REMARK 465     LEU B   193
REMARK 465     VAL B   194
REMARK 465     PRO B   195
REMARK 465     ARG B   196
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     ASP A   1B   CG   OD1  OD2
REMARK 470     LYS A  40    CG   CD   CE   NZ
REMARK 470     TYR B 207P   CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     TYR B 218P   CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     THR B 220P   OG1  CG2
REMARK 470     LYS B  63    CG   CD   CE   NZ
REMARK 470     GLU B  85    CG   CD   OE1  OE2
REMARK 470     ASN B 113    CG   OD1
REMARK 470     HIS B 166    CG   ND1  CD2  CE1  NE2
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    PHE A  48      -80.83    -29.26
REMARK 500    LEU A  51      -70.17   -108.38
REMARK 500    ASP A 158      -33.23     78.63
REMARK 500    ASN B  33      -97.94     66.04
REMARK 500    THR B  90      -98.02   -121.37
REMARK 500    PRO B 165       67.99    -57.95
REMARK 500    GLN B 167      137.21    -37.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS ENTRY CONTAINS COORDINATES FOR THE EXTRACELLULAR
REMARK 999 DOMAINS OF THE MURINE MHC CLASS II ALLELE I-A(G7) WITH A
REMARK 999 FRAGMENT FROM GAD65 (207 - 220) COVALENTLY ATTACHED TO THE
REMARK 999 FIRST RESIDUE OF THE AMINO TERMINUS OF THE MATURE BETA
REMARK 999 CHAIN. THE NUMBERING SCHEME FOR THE I-A(G7) RESIDUES IS AS
REMARK 999 DESCRIBED IN "SEQUENCES OF PROTEINS OF IMMUNOLOGICAL
REMARK 999 INTEREST" (1991), EDITED BY E.A. KABAT, T.T. WU, H.M.
REMARK 999 PERRY, K.S. GOTTESMAN AND C. FOELLER.
REMARK 999 DIMERIZATION OF THE I-A(G7) HETERODIMER WAS FACILITATED BY
REMARK 999 ADDING A LEUCINE ZIPPER TAIL TO THE CARBOXY TERMINUS OF
REMARK 999 EACH CHAIN. IN ADDITION, A HEXAHISTIDINE SEQUENCE WAS
REMARK 999 ENGINEERED TO THE CARBOXY TERMINAL END OF THE LEUCINE
REMARK 999 ZIPPER. THIS ALLOWED THE SECRETED PROTEIN TO BE PURIFIED
REMARK 999 BY NI-NTA CHROMATOGRAPHY. A THROMBIN CUT SITE WAS
REMARK 999 ENGINEERED IN A SPACER SEQUENCE BETWEEN THE CARBOXY
REMARK 999 TERMINAL RESIDUE OF EACH CHAIN AND THE LEUCINE ZIPPER-
REMARK 999 HEXAHISTIDINE SEQUENCE SO THAT MOST OF THE ENGINEERED
REMARK 999 RESIDUES COULD BE REMOVED FOR CRYSTALLIZATION. AFTER
REMARK 999 THROMBIN DIGESTION, EIGHT ENGINEERED RESIDUES (SSADLVPR)
REMARK 999 REMAINED ATTACHED TO THE CARBOXY TERMINAL END OF EACH
REMARK 999 I-A(G7) CHAIN.
REMARK 999 NO ELECTRON DENSITY WAS VISIBLE FOR 1) THE FIRST 2 RESIDUES
REMARK 999 OF THE ALPHA CHAIN 2) THE LAST 6 RESIDUES OF THE SPACER
REMARK 999 SEQUENCE ATTACHED TO THE C-TERMINUS OF THE ALPHA CHAIN,
REMARK 999 3) THE 6 RESIDUE (GSGSGS) LINKER BETWEEN GAD65 AND THE BETA
REMARK 999 CHAIN, 4) THE FIRST 4 RESIDUES OF THE BETA CHAIN, AND 5)
REMARK 999 THE LAST 7 RESIDUES OF THE SPACER SEQUENCE ATTACHED TO THE
REMARK 999 C-TERMINUS OF THE BETA CHAIN. SIX ADDITIONAL RESIDUES
REMARK 999 (GSHSRG) FROM THE SIGNAL SEQUENCE REMAIN CONNECTED TO THE
REMARK 999 AMINO TERMINUS OF THE GAD65 PEPTIDE; NO DENSITY IS PRESENT
REMARK 999 FOR THESE RESIDUES.
REMARK 999
REMARK 999 THE RESIDUE NUMBERING FOR THE TWO PROTEIN CHAINS IS:
REMARK 999   A   1B - A 178  : MHC CLASS II ALPHA CHAIN
REMARK 999   A 179 -  A 186  : SPACER SEQUENCE
REMARK 999   B 207P - B 220P : RESIDUES 207-220 OF GAD65
REMARK 999   B   1  - B 188  : MHC CLASS II BETA CHAIN
REMARK 999   B 189  - B 196  : SPACER SEQUENCE
DBREF  1ES0 A    1   178  UNP    P04228   HA2D_MOUSE      24    205
DBREF  1ES0 B  207P  220P UNP    Q05329   DCE2_HUMAN     222    235
DBREF  1ES0 B    1   188  GB     387435   AAA39547        28    214
SEQADV 1ES0 SER A  179  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 SER A  180  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 ALA A  181  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 ASP A  182  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 LEU A  183  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 VAL A  184  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 PRO A  185  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 ARG A  186  UNP  P04228              SEE REMARK 999
SEQADV 1ES0 GLY B  201P UNP  Q05329              SEE REMARK 999
SEQADV 1ES0 SER B  202P UNP  Q05329              SEE REMARK 999
SEQADV 1ES0 HIS B  203P UNP  Q05329              SEE REMARK 999
SEQADV 1ES0 SER B  204P UNP  Q05329              SEE REMARK 999
SEQADV 1ES0 ARG B  205P UNP  Q05329              SEE REMARK 999
SEQADV 1ES0 GLY B  206P UNP  Q05329              SEE REMARK 999
SEQADV 1ES0 GLY B   -5  GB   387435              SEE REMARK 999
SEQADV 1ES0 SER B   -4  GB   387435              SEE REMARK 999
SEQADV 1ES0 GLY B   -3  GB   387435              SEE REMARK 999
SEQADV 1ES0 SER B   -2  GB   387435              SEE REMARK 999
SEQADV 1ES0 GLY B   -1  GB   387435              SEE REMARK 999
SEQADV 1ES0 SER B    0  GB   387435              SEE REMARK 999
SEQADV 1ES0 SER B  189  GB   387435              SEE REMARK 999
SEQADV 1ES0 SER B  190  GB   387435              SEE REMARK 999
SEQADV 1ES0 ALA B  191  GB   387435              SEE REMARK 999
SEQADV 1ES0 ASP B  192  GB   387435              SEE REMARK 999
SEQADV 1ES0 LEU B  193  GB   387435              SEE REMARK 999
SEQADV 1ES0 VAL B  194  GB   387435              SEE REMARK 999
SEQADV 1ES0 PRO B  195  GB   387435              SEE REMARK 999
SEQADV 1ES0 ARG B  196  GB   387435              SEE REMARK 999
SEQRES   1 A  190  GLU ASP ASP ILE GLU ALA ASP HIS VAL GLY PHE TYR GLY
SEQRES   2 A  190  THR THR VAL TYR GLN SER PRO GLY ASP ILE GLY GLN TYR
SEQRES   3 A  190  THR HIS GLU PHE ASP GLY ASP GLU LEU PHE TYR VAL ASP
SEQRES   4 A  190  LEU ASP LYS LYS LYS THR VAL TRP ARG LEU PRO GLU PHE
SEQRES   5 A  190  GLY GLN LEU ILE LEU PHE GLU PRO GLN GLY GLY LEU GLN
SEQRES   6 A  190  ASN ILE ALA ALA GLU LYS HIS ASN LEU GLY ILE LEU THR
SEQRES   7 A  190  LYS ARG SER ASN PHE THR PRO ALA THR ASN GLU ALA PRO
SEQRES   8 A  190  GLN ALA THR VAL PHE PRO LYS SER PRO VAL LEU LEU GLY
SEQRES   9 A  190  GLN PRO ASN THR LEU ILE CYS PHE VAL ASP ASN ILE PHE
SEQRES  10 A  190  PRO PRO VAL ILE ASN ILE THR TRP LEU ARG ASN SER LYS
SEQRES  11 A  190  SER VAL THR ASP GLY VAL TYR GLU THR SER PHE LEU VAL
SEQRES  12 A  190  ASN ARG ASP HIS SER PHE HIS LYS LEU SER TYR LEU THR
SEQRES  13 A  190  PHE ILE PRO SER ASP ASP ASP ILE TYR ASP CYS LYS VAL
SEQRES  14 A  190  GLU HIS TRP GLY LEU GLU GLU PRO VAL LEU LYS HIS TRP
SEQRES  15 A  190  SER SER ALA ASP LEU VAL PRO ARG
SEQRES   1 B  221  GLY SER HIS SER ARG GLY TYR GLU ILE ALA PRO VAL PHE
SEQRES   2 B  221  VAL LEU LEU GLU TYR VAL THR GLY SER GLY SER GLY SER
SEQRES   3 B  221  GLY ASP SER GLU ARG HIS PHE VAL HIS GLN PHE LYS GLY
SEQRES   4 B  221  GLU CYS TYR PHE THR ASN GLY THR GLN ARG ILE ARG LEU
SEQRES   5 B  221  VAL THR ARG TYR ILE TYR ASN ARG GLU GLU TYR LEU ARG
SEQRES   6 B  221  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   7 B  221  LEU GLY ARG HIS SER ALA GLU TYR TYR ASN LYS GLN TYR
SEQRES   8 B  221  LEU GLU ARG THR ARG ALA GLU LEU ASP THR ALA CYS ARG
SEQRES   9 B  221  HIS ASN TYR GLU GLU THR GLU VAL PRO THR SER LEU ARG
SEQRES  10 B  221  ARG LEU GLU GLN PRO ASN VAL ALA ILE SER LEU SER ARG
SEQRES  11 B  221  THR GLU ALA LEU ASN HIS HIS ASN THR LEU VAL CYS SER
SEQRES  12 B  221  VAL THR ASP PHE TYR PRO ALA LYS ILE LYS VAL ARG TRP
SEQRES  13 B  221  PHE ARG ASN GLY GLN GLU GLU THR VAL GLY VAL SER SER
SEQRES  14 B  221  THR GLN LEU ILE ARG ASN GLY ASP TRP THR PHE GLN VAL
SEQRES  15 B  221  LEU VAL MET LEU GLU MET THR PRO HIS GLN GLY GLU VAL
SEQRES  16 B  221  TYR THR CYS HIS VAL GLU HIS PRO SER LEU LYS SER PRO
SEQRES  17 B  221  ILE THR VAL GLU TRP SER SER ALA ASP LEU VAL PRO ARG
FORMUL   3  HOH   *76(H2 O)
HELIX    1   1 GLU A   47  LEU A   51  5                                   5
HELIX    2   2 GLU A   55  SER A   77  1                                  23
HELIX    3   3 GLY B   54  LEU B   68  1                                  13
HELIX    4   4 TYR B   66  ALA B   78  1                                  12
HELIX    5   5 ALA B   78  THR B   86  1                                   9
HELIX    6   6 THR B   90  ARG B   94  5                                   5
SHEET    1   A 8 LYS A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  O  TYR A  33   N  VAL A  42
SHEET    3   A 8 ILE A  19  PHE A  26 -1  O  TYR A  22   N  VAL A  34
SHEET    4   A 8 HIS A   4  SER A  15 -1  N  PHE A   7   O  GLU A  25
SHEET    5   A 8 PHE B   7  THR B  18 -1  N  PHE B   7   O  SER A  15
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  ARG B  23   N  THR B  18
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32
SHEET    8   A 8 TYR B  47  ALA B  49 -1  N  ARG B  48   O  ARG B  39
SHEET    1   B 4 GLN A  88  PRO A  93  0
SHEET    2   B 4 ASN A 103  ILE A 112 -1  N  ILE A 106   O  PHE A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  PHE A 145   N  ILE A 112
SHEET    4   B 4 VAL A 132  GLU A 134 -1  O  TYR A 133   N  TYR A 150
SHEET    1   C 4 GLN A  88  PRO A  93  0
SHEET    2   C 4 ASN A 103  ILE A 112 -1  N  ILE A 106   O  PHE A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  PHE A 145   N  ILE A 112
SHEET    4   C 4 LEU A 138  VAL A 139 -1  N  LEU A 138   O  HIS 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 ILE A 160  GLU A 166 -1  N  ASP A 162   O  LEU A 122
SHEET    4   D 4 VAL A 174  SER A 179 -1  O  VAL A 174   N  VAL A 165
SHEET    1   E 4 ASN B  98  LEU B 103  0
SHEET    2   E 4 THR B 114  PHE B 122 -1  N  VAL B 116   O  SER B 102
SHEET    3   E 4 PHE B 155  GLU B 162 -1  N  PHE B 155   O  PHE B 122
SHEET    4   E 4 VAL B 142  SER B 144 -1  O  SER B 143   N  MET B 160
SHEET    1   F 4 ASN B  98  LEU B 103  0
SHEET    2   F 4 THR B 114  PHE B 122 -1  N  VAL B 116   O  SER B 102
SHEET    3   F 4 PHE B 155  GLU B 162 -1  N  PHE B 155   O  PHE B 122
SHEET    4   F 4 ILE B 148  ARG 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 LYS B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136
SHEET    3   G 4 TYR B 171  GLU B 176 -1  N  THR B 172   O  PHE B 132
SHEET    4   G 4 ILE B 184  TRP B 188 -1  O  ILE B 184   N  VAL B 175
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.04
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03
CISPEP   1 SER A   15    PRO A   16          0         0.67
CISPEP   2 PHE A  113    PRO A  114          0        -0.74
CISPEP   3 TYR B  123    PRO B  124          0        -0.08
CRYST1   95.149  110.123   96.084  90.00  90.00  90.00 C 2 2 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      0.010510  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009081  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010408        0.00000
      
PROCHECK
Go to PROCHECK summary
 References