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PDBsum entry 2nna

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Immune system PDB id
2nna
Jmol
Contents
Protein chains
182 a.a.
182 a.a.
13 a.a.
Waters ×311
HEADER    IMMUNE SYSTEM                           24-OCT-06   2NNA
TITLE     STRUCTURE OF THE MHC CLASS II MOLECULE HLA-DQ8 BOUND WITH A DEAMIDATED
TITLE    2 GLUTEN PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MHC CLASS II ANTIGEN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES IN DATABASE 24-207;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: MHC CLASS II ANTIGEN;
COMPND   8 CHAIN: B;
COMPND   9 FRAGMENT: RESIDUES IN DATABASE 33-224;
COMPND  10 ENGINEERED: YES;
COMPND  11 MOL_ID: 3;
COMPND  12 MOLECULE: GLUTEN PEPTIDE;
COMPND  13 CHAIN: C;
COMPND  14 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: SPODOPTERA FRUGIPERDA;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HI5 CELLS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBACDUAL;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: HI5 CELLS;
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBACDUAL;
SOURCE  21 MOL_ID: 3;
SOURCE  22 SYNTHETIC: YES;
SOURCE  23 OTHER_DETAILS: THE C TERMINUS OF CHAIN C WAS LINKED TO THE N
SOURCE  24 TERMINUS OF CHAIN B WITH A FLEXIBLE SERINE GLYCINE LINKER. THIS
SOURCE  25 FLEXIBLE LINKER WAS CLEAVED WITH TRYPSIN AT AN UNKNOWN POINT IN THE
SOURCE  26 SEQUENCE DURING THE PURIFICATION PROCESS.
KEYWDS    MAJOR HISTOCOMPATIBILITY COMPLEX HLA-DQ8, DEAMIDATED GLUTEN PEPTIDE,
KEYWDS   2 POST TRANSLATIONAL MODIFICATION, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.N.HENDERSON,J.A.TYE-DIN,J.ROSSJOHN,R.P.ANDERSON
REVDAT   4   13-JUL-11 2NNA    1       VERSN
REVDAT   3   18-AUG-09 2NNA    1       DBREF  SEQADV
REVDAT   2   24-FEB-09 2NNA    1       VERSN
REVDAT   1   04-SEP-07 2NNA    0
JRNL        AUTH   K.N.HENDERSON,J.A.TYE-DIN,H.H.REID,Z.CHEN,N.A.BORG,
JRNL        AUTH 2 T.BEISSBARTH,A.TATHAM,S.I.MANNERING,A.W.PURCELL,N.L.DUDEK,
JRNL        AUTH 3 D.A.VAN HEEL,J.MCCLUSKEY,J.ROSSJOHN,R.P.ANDERSON
JRNL        TITL   A STRUCTURAL AND IMMUNOLOGICAL BASIS FOR THE ROLE OF HUMAN
JRNL        TITL 2 LEUKOCYTE ANTIGEN DQ8 IN CELIAC DISEASE
JRNL        REF    IMMUNITY                      V.  27    23 2007
JRNL        REFN                   ISSN 1074-7613
JRNL        PMID   17629515
JRNL        DOI    10.1016/J.IMMUNI.2007.05.015
REMARK   2
REMARK   2 RESOLUTION.    2.10 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 : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.64
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 36603
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.217
REMARK   3   FREE R VALUE                     : 0.248
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1473
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            : 3071
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 311
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.85
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
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        : 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 2NNA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-06.
REMARK 100 THE RCSB ID CODE IS RCSB040069.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
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          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200  DATA SCALING SOFTWARE          : D*TREK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36603
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.640
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1JK8, WITH THE INSULIN PEPTIDE REMOVED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M MONO-POTTASIUM DIHYDROGEN
REMARK 280  PHOSPHATE, 19%(W/V) PEG 8000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 298K
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       29.41500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.53000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.26000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.53000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.41500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.26000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 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    -1
REMARK 465     GLU A   181
REMARK 465     GLY B   -14
REMARK 465     GLY B   -13
REMARK 465     GLY B   -12
REMARK 465     GLY B   -11
REMARK 465     SER B   -10
REMARK 465     ILE B    -9
REMARK 465     GLU B    -8
REMARK 465     GLY B    -7
REMARK 465     ARG B    -6
REMARK 465     GLY B    -5
REMARK 465     SER B    -4
REMARK 465     GLY B    -3
REMARK 465     GLY B    -2
REMARK 465     SER B   104
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     ASN B   113
REMARK 465     GLN B   191
REMARK 465     SER B   192
REMARK 465     GLN C    -3
REMARK 465     GLN C    -2
REMARK 465     TYR C    -1
REMARK 465     PRO C     0
REMARK 465     GLN C    14
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 B 165   CA  -  N   -  CD  ANGL. DEV. = -17.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    TYR A   9       54.58   -100.49
REMARK 500    ASN B  33     -106.43     66.51
REMARK 500    THR B  89      -87.30   -132.53
REMARK 500    ASP B 121       70.79     45.82
REMARK 500    PRO B 124     -170.39    -68.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 192        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH A 265        DISTANCE =  7.14 ANGSTROMS
REMARK 525    HOH A 269        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A 277        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A 341        DISTANCE =  6.16 ANGSTROMS
REMARK 525    HOH A 347        DISTANCE =  6.70 ANGSTROMS
REMARK 525    HOH A 349        DISTANCE =  8.04 ANGSTROMS
REMARK 525    HOH A 357        DISTANCE =  5.83 ANGSTROMS
REMARK 525    HOH B 197        DISTANCE =  7.58 ANGSTROMS
REMARK 525    HOH B 209        DISTANCE =  6.67 ANGSTROMS
REMARK 525    HOH B 211        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH B 267        DISTANCE =  6.34 ANGSTROMS
REMARK 525    HOH B 275        DISTANCE =  5.58 ANGSTROMS
REMARK 525    HOH B 305        DISTANCE =  5.07 ANGSTROMS
DBREF  2NNA A   -1   181  UNP    Q5Y7F5   Q5Y7F5_HUMAN    24    207
DBREF  2NNA B    1   192  UNP    Q5Y7F6   Q5Y7F6_HUMAN    33    224
DBREF  2NNA C   -3    14  UNP    P18573   GDA9_WHEAT     243    260
SEQADV 2NNA GLY B  -14  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B  -13  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B  -12  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B  -11  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA SER B  -10  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA ILE B   -9  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLU B   -8  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B   -7  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA ARG B   -6  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B   -5  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA SER B   -4  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B   -3  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B   -2  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLY B   -1  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA SER B    0  UNP  Q5Y7F6              EXPRESSION TAG
SEQADV 2NNA GLU C    3  UNP  P18573    GLN   249 CONFLICT
SEQADV 2NNA GLU C   11  UNP  P18573    GLN   257 CONFLICT
SEQRES   1 A  184  GLU ASP ILE VAL ALA ASP HIS VAL ALA SER TYR GLY VAL
SEQRES   2 A  184  ASN LEU TYR GLN SER TYR GLY PRO SER GLY GLN TYR SER
SEQRES   3 A  184  HIS GLU PHE ASP GLY ASP GLU GLU PHE TYR VAL ASP LEU
SEQRES   4 A  184  GLU ARG LYS GLU THR VAL TRP GLN LEU PRO LEU PHE ARG
SEQRES   5 A  184  ARG PHE ARG ARG PHE ASP PRO GLN PHE ALA LEU THR ASN
SEQRES   6 A  184  ILE ALA VAL LEU LYS HIS ASN LEU ASN ILE VAL ILE LYS
SEQRES   7 A  184  ARG SER ASN SER THR ALA ALA THR ASN GLU VAL PRO GLU
SEQRES   8 A  184  VAL THR VAL PHE SER LYS SER PRO VAL THR LEU GLY GLN
SEQRES   9 A  184  PRO ASN THR LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO
SEQRES  10 A  184  PRO VAL VAL ASN ILE THR TRP LEU SER ASN GLY HIS SER
SEQRES  11 A  184  VAL THR GLU GLY VAL SER GLU THR SER PHE LEU SER LYS
SEQRES  12 A  184  SER ASP HIS SER PHE PHE LYS ILE SER TYR LEU THR PHE
SEQRES  13 A  184  LEU PRO SER ALA ASP GLU ILE TYR ASP CYS LYS VAL GLU
SEQRES  14 A  184  HIS TRP GLY LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU
SEQRES  15 A  184  PRO GLU
SEQRES   1 B  207  GLY GLY GLY GLY SER ILE GLU GLY ARG GLY SER GLY GLY
SEQRES   2 B  207  GLY SER ARG ASP SER PRO GLU ASP PHE VAL TYR GLN PHE
SEQRES   3 B  207  LYS GLY MET CYS TYR PHE THR ASN GLY THR GLU ARG VAL
SEQRES   4 B  207  ARG LEU VAL THR ARG TYR ILE TYR ASN ARG GLU GLU TYR
SEQRES   5 B  207  ALA ARG PHE ASP SER ASP VAL GLY VAL TYR ARG ALA VAL
SEQRES   6 B  207  THR PRO LEU GLY PRO PRO ALA ALA GLU TYR TRP ASN SER
SEQRES   7 B  207  GLN LYS GLU VAL LEU GLU ARG THR ARG ALA GLU LEU ASP
SEQRES   8 B  207  THR VAL CYS ARG HIS ASN TYR GLN LEU GLU LEU ARG THR
SEQRES   9 B  207  THR LEU GLN ARG ARG VAL GLU PRO THR VAL THR ILE SER
SEQRES  10 B  207  PRO SER ARG THR GLU ALA LEU ASN HIS HIS ASN LEU LEU
SEQRES  11 B  207  VAL CYS SER VAL THR ASP PHE TYR PRO ALA GLN ILE LYS
SEQRES  12 B  207  VAL ARG TRP PHE ARG ASN ASP GLN GLU GLU THR THR GLY
SEQRES  13 B  207  VAL VAL SER THR PRO LEU ILE ARG ASN GLY ASP TRP THR
SEQRES  14 B  207  PHE GLN ILE LEU VAL MET LEU GLU MET THR PRO GLN ARG
SEQRES  15 B  207  GLY ASP VAL TYR THR CYS HIS VAL GLU HIS PRO SER LEU
SEQRES  16 B  207  GLN ASN PRO ILE ILE VAL GLU TRP ARG ALA GLN SER
SEQRES   1 C   18  GLN GLN TYR PRO SER GLY GLU GLY SER PHE GLN PRO SER
SEQRES   2 C   18  GLN GLU ASN PRO GLN
FORMUL   4  HOH   *311(H2 O)
HELIX    1   1 LEU A   45  ARG A   52  1                                   8
HELIX    2   2 ASP A   55  SER A   77  1                                  23
HELIX    3   3 GLY B   -1  SER B    3  5                                   5
HELIX    4   4 GLY B   54  SER B   63  1                                  10
HELIX    5   5 GLN B   64  VAL B   78  1                                  15
HELIX    6   6 VAL B   78  ARG B   88  1                                  11
HELIX    7   7 THR B   89  ARG B   93  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  HIS A  24   O  GLU A  31
SHEET    4   A 8 HIS A   5  GLN A  14 -1  N  SER A   8   O  GLU A  25
SHEET    5   A 8 VAL B   8  THR B  18 -1  O  TYR B   9   N  TYR A  13
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  ARG B  25   N  TYR B  16
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  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  ILE A 112 -1  O  ILE A 106   N  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  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  ILE A 112 -1  O  ILE A 106   N  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  SER A 139 -1  N  LEU A 138   O  PHE A 146
SHEET    1   D 4 HIS A 126  VAL A 128  0
SHEET    2   D 4 ASN A 118  SER A 123 -1  N  SER A 123   O  HIS A 126
SHEET    3   D 4 TYR A 161  GLU A 166 -1  O  LYS A 164   N  THR A 120
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  SER B 102  0
SHEET    2   E 4 LEU B 115  PHE B 122 -1  O  SER B 118   N  THR B 100
SHEET    3   E 4 PHE B 155  LEU B 161 -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 THR B  98  SER B 102  0
SHEET    2   F 4 LEU B 115  PHE B 122 -1  O  SER B 118   N  THR B 100
SHEET    3   F 4 PHE B 155  LEU B 161 -1  O  LEU B 161   N  LEU B 115
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  O  HIS B 174   N  ARG B 130
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 GLY A   17    PRO A   18          0        -0.05
CISPEP   2 PHE A  113    PRO A  114          0        -0.19
CISPEP   3 TYR B  123    PRO B  124          0         0.10
CRYST1   58.830   92.520  113.060  90.00  90.00  90.00 P 21 21 21    4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.016998  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010808  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008845        0.00000
      
PROCHECK
Go to PROCHECK summary
 References