spacer
spacer

PDBsum entry 2oje

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Immune system PDB id
2oje
Jmol
Contents
Protein chains
180 a.a.
190 a.a.
13 a.a.
214 a.a.
Ligands
PO4 ×4
Waters ×118
HEADER    IMMUNE SYSTEM                           12-JAN-07   2OJE
TITLE     MYCOPLASMA ARTHRITIDIS-DERIVED MITOGEN COMPLEXED WITH CLASS
TITLE    2 II MHC MOLECULE HLA-DR1/HA COMPLEX IN THE PRESENCE OF EDTA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR
COMPND   3 ALPHA CHAIN PRECURSOR;
COMPND   4 CHAIN: A, E;
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 27-206;
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 PRECURSOR;
COMPND  11 CHAIN: B, F;
COMPND  12 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 30-219;
COMPND  13 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: HAEMAGGLUTININ PEPTIDE 306-318;
COMPND  17 CHAIN: C, G;
COMPND  18 FRAGMENT: RESIDUES 306-318;
COMPND  19 ENGINEERED: YES;
COMPND  20 MOL_ID: 4;
COMPND  21 MOLECULE: SUPERANTIGEN;
COMPND  22 CHAIN: D, H;
COMPND  23 FRAGMENT: RESIDUES 25-238;
COMPND  24 SYNONYM: MYCOPLASMA ARTHRITIDIS-DERIVED MITOGEN;
COMPND  25 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: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  12 ORGANISM_COMMON: HUMAN;
SOURCE  13 ORGANISM_TAXID: 9606;
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PLM1;
SOURCE  19 MOL_ID: 3;
SOURCE  20 SYNTHETIC: YES;
SOURCE  21 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN INFLUENZA
SOURCE  22 VIRUS;
SOURCE  23 MOL_ID: 4;
SOURCE  24 ORGANISM_SCIENTIFIC: MYCOPLASMA ARTHRITIDIS;
SOURCE  25 ORGANISM_TAXID: 2111;
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS    SUPERANTIGEN, MHC, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.LI,Y.ZHAO,Y.GUO,Z.LI,L.EISELE,W.MOURAD
REVDAT   3   24-FEB-09 2OJE    1       VERSN
REVDAT   2   03-APR-07 2OJE    1       JRNL
REVDAT   1   23-JAN-07 2OJE    0
JRNL        AUTH   H.LI,Y.ZHAO,Y.GUO,Z.LI,L.EISELE,W.MOURAD
JRNL        TITL   ZINC INDUCES DIMERIZATION OF THE CLASS II MAJOR
JRNL        TITL 2 HISTOCOMPATIBILITY COMPLEX MOLECULE THAT LEADS TO
JRNL        TITL 3 COOPERATIVE BINDING TO A SUPERANTIGEN.
JRNL        REF    J.BIOL.CHEM.                  V. 282  5991 2007
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   17166841
JRNL        DOI    10.1074/JBC.M608482200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.00 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) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.22
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2671296.250
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.8
REMARK   3   NUMBER OF REFLECTIONS             : 40345
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) : 0.211
REMARK   3   FREE R VALUE                     : 0.261
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2850
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6318
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330
REMARK   3   BIN FREE R VALUE                    : 0.3980
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 443
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9872
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 118
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -6.73000
REMARK   3    B22 (A**2) : 13.74000
REMARK   3    B33 (A**2) : -7.01000
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) : 0.34
REMARK   3   ESD FROM SIGMAA              (A) : 0.49
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) : 0.43
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.58
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79
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) : 1.280 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.280 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.840 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.990 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.34
REMARK   3   BSOL        : 18.64
REMARK   3
REMARK   3  NCS MODEL : CONSTR
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  : ION.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : ION.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2OJE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-07.
REMARK 100 THE RCSB ID CODE IS RCSB041209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
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) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40345
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.220
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.8
REMARK 200  DATA REDUNDANCY                : 5.200
REMARK 200  R MERGE                    (I) : 0.12400
REMARK 200  R SYM                      (I) : 12.40000
REMARK 200   FOR THE DATA SET  : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.19
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.56300
REMARK 200  R SYM FOR SHELL            (I) : 56.30000
REMARK 200   FOR SHELL         : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1R5I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7M POTASSIUM SODIUM PHOSPHATE,
REMARK 280  0.1M HEPES, 2 MM EDTA, PH 7.5, VAPOR DIFFUSION, TEMPERATURE
REMARK 280  298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
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+1/2
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        0.00000
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        0.00000
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       68.86750
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       89.77750
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       89.97600
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       68.86750
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       89.77750
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.97600
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       68.86750
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       89.77750
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.97600
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       68.86750
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       89.77750
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.97600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 49680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 103020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -267.0 KCAL/MOL
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 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, E, F, G
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       68.86750
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000       89.77750
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       89.97600
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000      -68.86750
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      -89.77750
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       89.97600
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH B 200  LIES ON A SPECIAL POSITION.
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     LYS G 307    CG   CD   CE   NZ
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    GLU A   179     N    ASP A   181              2.14
REMARK 500   O    LYS H   143     OH   TYR H   194              2.17
REMARK 500   O    HOH D   215     O    HOH D   233              2.19
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   NZ   LYS E     2     NZ   LYS E     2     3655     1.93
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    PHE A  51      -12.20   -141.48
REMARK 500    PRO A 102      135.86    -34.74
REMARK 500    PRO A 115       59.30    -69.92
REMARK 500    THR A 129      -61.82   -139.56
REMARK 500    GLU A 158       33.94   -142.80
REMARK 500    GLU A 179       64.85   -172.44
REMARK 500    PHE A 180      -32.47     49.29
REMARK 500    ASN B  33      -97.17     54.85
REMARK 500    THR B  90      -80.52   -115.99
REMARK 500    ASN B 113      -72.31    -58.70
REMARK 500    LYS B 139      -48.99   -138.14
REMARK 500    PRO B 165      106.11    -57.37
REMARK 500    LYS D  10      135.62    -32.41
REMARK 500    ASN D  21       57.28   -145.53
REMARK 500    ALA D  94      -35.30    -33.09
REMARK 500    ASN D 125       74.24   -118.92
REMARK 500    LEU D 200      -52.26    -25.26
REMARK 500    PHE E  51      -12.39   -141.86
REMARK 500    LEU E  99      125.06    -37.60
REMARK 500    PRO E 102      137.77    -36.12
REMARK 500    THR E 129      -60.14   -141.09
REMARK 500    LEU E 144     -167.74   -108.80
REMARK 500    THR E 157       21.89    -74.92
REMARK 500    GLU E 158       32.21   -143.50
REMARK 500    GLU E 179       61.14   -172.71
REMARK 500    PHE E 180      -66.09     43.38
REMARK 500    ASN F  19       71.45     49.17
REMARK 500    ASN F  33      -98.41     55.14
REMARK 500    TYR F  78      -70.48   -111.22
REMARK 500    THR F  90      -80.77   -115.34
REMARK 500    ASN F 113      -74.17    -56.67
REMARK 500    LYS F 139      -50.44   -138.04
REMARK 500    PRO F 165      105.38    -55.88
REMARK 500    LYS H  10      135.39    -32.00
REMARK 500    ASN H  21       58.90   -145.31
REMARK 500    GLU H  71        1.57    -69.47
REMARK 500    ALA H  94      -37.13    -31.64
REMARK 500    ASN H 125       75.75   -117.22
REMARK 500    LEU H 200      -57.68    -17.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 214
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 202
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 214
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R5I   RELATED DB: PDB
REMARK 900 MYCOPLASMA ARTHRITIDIS-DERIVED MITOGEN COMPLEXED WITH CLASS
REMARK 900 II MHC MOLECULE HLA-DR1/HA COMPLEX IN THE PRESENCE OF ZINC
DBREF  2OJE A    2   181  UNP    P01903   2DRA_HUMAN      27    206
DBREF  2OJE E    2   181  UNP    P01903   2DRA_HUMAN      27    206
DBREF  2OJE B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  2OJE F    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  2OJE D    0   213  UNP    Q48898   Q48898_MYCAT    25    238
DBREF  2OJE H    0   213  UNP    Q48898   Q48898_MYCAT    25    238
DBREF  2OJE C  306   318  PDB    2OJE     2OJE           306    318
DBREF  2OJE G  306   318  PDB    2OJE     2OJE           306    318
SEQADV 2OJE MSE A   23  UNP  P01903    MET    48 MODIFIED RESIDUE
SEQADV 2OJE MSE A   36  UNP  P01903    MET    61 MODIFIED RESIDUE
SEQADV 2OJE MSE A   73  UNP  P01903    MET    98 MODIFIED RESIDUE
SEQADV 2OJE MSE E   23  UNP  P01903    MET    48 MODIFIED RESIDUE
SEQADV 2OJE MSE E   36  UNP  P01903    MET    61 MODIFIED RESIDUE
SEQADV 2OJE MSE E   73  UNP  P01903    MET    98 MODIFIED RESIDUE
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 MSE PHE ASP PHE ASP
SEQRES   3 A  180  GLY ASP GLU ILE PHE HIS VAL ASP MSE 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 MSE 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   13  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES   1 D  214  SER MET LYS LEU ARG VAL GLU ASN PRO LYS LYS ALA GLN
SEQRES   2 D  214  LYS HIS PHE VAL GLN ASN LEU ASN ASN VAL VAL PHE THR
SEQRES   3 D  214  ASN LYS GLU LEU GLU ASP ILE TYR ASN LEU SER ASN LYS
SEQRES   4 D  214  GLU GLU THR LYS GLU VAL LEU LYS LEU PHE LYS LEU LYS
SEQRES   5 D  214  VAL ASN GLN PHE TYR ARG HIS ALA PHE GLY ILE VAL ASN
SEQRES   6 D  214  ASP TYR ASN GLY LEU LEU GLU TYR LYS GLU ILE PHE ASN
SEQRES   7 D  214  MET MET PHE LEU LYS LEU SER VAL VAL PHE ASP THR GLN
SEQRES   8 D  214  ARG LYS GLU ALA ASN ASN VAL GLU GLN ILE LYS ARG ASN
SEQRES   9 D  214  ILE ALA ILE LEU ASP GLU ILE MET ALA LYS ALA ASP ASN
SEQRES  10 D  214  ASP LEU SER TYR PHE ILE SER GLN ASN LYS ASN PHE GLN
SEQRES  11 D  214  GLU LEU TRP ASP LYS ALA VAL LYS LEU THR LYS GLU MET
SEQRES  12 D  214  LYS ILE LYS LEU LYS GLY GLN LYS LEU ASP LEU ARG ASP
SEQRES  13 D  214  GLY GLU VAL ALA ILE ASN LYS VAL ARG GLU LEU PHE GLY
SEQRES  14 D  214  SER ASP LYS ASN VAL LYS GLU LEU TRP TRP PHE ARG SER
SEQRES  15 D  214  LEU LEU VAL LYS GLY VAL TYR LEU ILE LYS ARG TYR TYR
SEQRES  16 D  214  GLU GLY ASP ILE GLU LEU LYS THR THR SER ASP PHE ALA
SEQRES  17 D  214  LYS ALA VAL PHE GLU ASP
SEQRES   1 E  180  LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU
SEQRES   2 E  180  ASN PRO ASP GLN SER GLY GLU PHE MSE PHE ASP PHE ASP
SEQRES   3 E  180  GLY ASP GLU ILE PHE HIS VAL ASP MSE ALA LYS LYS GLU
SEQRES   4 E  180  THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER
SEQRES   5 E  180  PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP
SEQRES   6 E  180  LYS ALA ASN LEU GLU ILE MSE THR LYS ARG SER ASN TYR
SEQRES   7 E  180  THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU
SEQRES   8 E  180  THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU
SEQRES   9 E  180  ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN
SEQRES  10 E  180  VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY
SEQRES  11 E  180  VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU
SEQRES  12 E  180  PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR
SEQRES  13 E  180  GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU
SEQRES  14 E  180  ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES   1 F  190  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 F  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 F  190  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 F  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 F  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 F  190  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 F  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 F  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 F  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 F  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 F  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 F  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 F  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 F  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 F  190  PRO LEU THR VAL GLU TRP ARG ALA
SEQRES   1 G   13  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES   1 H  214  SER MET LYS LEU ARG VAL GLU ASN PRO LYS LYS ALA GLN
SEQRES   2 H  214  LYS HIS PHE VAL GLN ASN LEU ASN ASN VAL VAL PHE THR
SEQRES   3 H  214  ASN LYS GLU LEU GLU ASP ILE TYR ASN LEU SER ASN LYS
SEQRES   4 H  214  GLU GLU THR LYS GLU VAL LEU LYS LEU PHE LYS LEU LYS
SEQRES   5 H  214  VAL ASN GLN PHE TYR ARG HIS ALA PHE GLY ILE VAL ASN
SEQRES   6 H  214  ASP TYR ASN GLY LEU LEU GLU TYR LYS GLU ILE PHE ASN
SEQRES   7 H  214  MET MET PHE LEU LYS LEU SER VAL VAL PHE ASP THR GLN
SEQRES   8 H  214  ARG LYS GLU ALA ASN ASN VAL GLU GLN ILE LYS ARG ASN
SEQRES   9 H  214  ILE ALA ILE LEU ASP GLU ILE MET ALA LYS ALA ASP ASN
SEQRES  10 H  214  ASP LEU SER TYR PHE ILE SER GLN ASN LYS ASN PHE GLN
SEQRES  11 H  214  GLU LEU TRP ASP LYS ALA VAL LYS LEU THR LYS GLU MET
SEQRES  12 H  214  LYS ILE LYS LEU LYS GLY GLN LYS LEU ASP LEU ARG ASP
SEQRES  13 H  214  GLY GLU VAL ALA ILE ASN LYS VAL ARG GLU LEU PHE GLY
SEQRES  14 H  214  SER ASP LYS ASN VAL LYS GLU LEU TRP TRP PHE ARG SER
SEQRES  15 H  214  LEU LEU VAL LYS GLY VAL TYR LEU ILE LYS ARG TYR TYR
SEQRES  16 H  214  GLU GLY ASP ILE GLU LEU LYS THR THR SER ASP PHE ALA
SEQRES  17 H  214  LYS ALA VAL PHE GLU ASP
MODRES 2OJE MSE A   23  MET  SELENOMETHIONINE
MODRES 2OJE MSE A   36  MET  SELENOMETHIONINE
MODRES 2OJE MSE A   73  MET  SELENOMETHIONINE
MODRES 2OJE MSE E   23  MET  SELENOMETHIONINE
MODRES 2OJE MSE E   36  MET  SELENOMETHIONINE
MODRES 2OJE MSE E   73  MET  SELENOMETHIONINE
HET    MSE  A  23       8
HET    MSE  A  36       8
HET    MSE  A  73       8
HET    MSE  E  23       8
HET    MSE  E  36       8
HET    MSE  E  73       8
HET    PO4  D 214       5
HET    PO4  C 202       5
HET    PO4  H 214       5
HET    PO4  E 204       5
HETNAM     MSE SELENOMETHIONINE
HETNAM     PO4 PHOSPHATE ION
FORMUL   1  MSE    6(C5 H11 N O2 SE)
FORMUL   9  PO4    4(O4 P 3-)
FORMUL  13  HOH   *118(H2 O)
HELIX    1   1 LEU A   45  ARG A   50  1                                   6
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 SER B   88  THR B   90  5                                   3
HELIX    8   8 THR D   25  ASN D   34  1                                  10
HELIX    9   9 GLU D   43  ASN D   67  1                                  25
HELIX   10  10 GLU D   71  GLU D   93  1                                  23
HELIX   11  11 ASN D   96  GLN D  124  1                                  29
HELIX   12  12 ASN D  125  LEU D  146  1                                  22
HELIX   13  13 GLU D  157  GLY D  168  1                                  12
HELIX   14  14 ASP D  170  LEU D  176  1                                   7
HELIX   15  15 LEU D  176  GLU D  195  1                                  20
HELIX   16  16 GLU D  199  SER D  204  1                                   6
HELIX   17  17 SER D  204  PHE D  211  1                                   8
HELIX   18  18 LEU E   45  ARG E   50  1                                   6
HELIX   19  19 GLU E   55  SER E   77  1                                  23
HELIX   20  20 THR F   51  LEU F   53  5                                   3
HELIX   21  21 GLY F   54  SER F   63  1                                  10
HELIX   22  22 GLN F   64  TYR F   78  1                                  15
HELIX   23  23 TYR F   78  GLU F   87  1                                  10
HELIX   24  24 SER F   88  THR F   90  5                                   3
HELIX   25  25 THR H   25  ASN H   34  1                                  10
HELIX   26  26 GLU H   43  ASN H   67  1                                  25
HELIX   27  27 GLU H   71  GLU H   93  1                                  23
HELIX   28  28 ASN H   96  GLN H  124  1                                  29
HELIX   29  29 ASN H  125  LEU H  146  1                                  22
HELIX   30  30 GLU H  157  GLY H  168  1                                  12
HELIX   31  31 ASP H  170  LEU H  176  1                                   7
HELIX   32  32 LEU H  176  GLU H  195  1                                  20
HELIX   33  33 GLU H  199  THR H  203  5                                   5
HELIX   34  34 SER H  204  PHE H  211  1                                   8
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  ILE A   8   O  ASP A  25
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  PHE B   7   N  ASN A  15
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  ILE B  31   N  GLN B  10
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  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  PHE A 153   N  ASN A 103
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  PHE A 153   N  ASN A 103
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  ARG A 164   N  THR A 120
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 LEU B 114  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3   E 4 PHE B 155  GLU B 162 -1  O  PHE B 155   N  PHE B 122
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 LEU B 114  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3   F 4 PHE B 155  GLU B 162 -1  O  PHE B 155   N  PHE B 122
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 138  0
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  TRP B 131   O  GLU B 138
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 8 GLU E  40  TRP E  43  0
SHEET    2   H 8 ASP E  29  ASP E  35 -1  N  HIS E  33   O  VAL E  42
SHEET    3   H 8 SER E  19  PHE E  26 -1  N  PHE E  26   O  ASP E  29
SHEET    4   H 8 HIS E   5  ASN E  15 -1  N  ILE E   8   O  ASP E  25
SHEET    5   H 8 PHE F   7  PHE F  18 -1  O  PHE F   7   N  ASN E  15
SHEET    6   H 8 ARG F  23  TYR F  32 -1  O  ILE F  31   N  GLN F  10
SHEET    7   H 8 GLU F  35  ASP F  41 -1  O  GLU F  35   N  TYR F  32
SHEET    8   H 8 TYR F  47  ALA F  49 -1  O  ARG F  48   N  ARG F  39
SHEET    1   I 4 GLU E  88  THR E  93  0
SHEET    2   I 4 ASN E 103  PHE E 112 -1  O  ILE E 106   N  LEU E  92
SHEET    3   I 4 PHE E 145  PHE E 153 -1  O  PHE E 153   N  ASN E 103
SHEET    4   I 4 SER E 133  GLU E 134 -1  N  SER E 133   O  TYR E 150
SHEET    1   J 4 GLU E  88  THR E  93  0
SHEET    2   J 4 ASN E 103  PHE E 112 -1  O  ILE E 106   N  LEU E  92
SHEET    3   J 4 PHE E 145  PHE E 153 -1  O  PHE E 153   N  ASN E 103
SHEET    4   J 4 LEU E 138  PRO E 139 -1  N  LEU E 138   O  ARG E 146
SHEET    1   K 4 LYS E 126  VAL E 128  0
SHEET    2   K 4 ASN E 118  ARG E 123 -1  N  ARG E 123   O  LYS E 126
SHEET    3   K 4 TYR E 161  GLU E 166 -1  O  ARG E 164   N  THR E 120
SHEET    4   K 4 LEU E 174  TRP E 178 -1  O  TRP E 178   N  TYR E 161
SHEET    1   L 4 LYS F  98  SER F 104  0
SHEET    2   L 4 LEU F 114  PHE F 122 -1  O  VAL F 116   N  TYR F 102
SHEET    3   L 4 PHE F 155  GLU F 162 -1  O  PHE F 155   N  PHE F 122
SHEET    4   L 4 VAL F 142  SER F 144 -1  N  VAL F 143   O  MET F 160
SHEET    1   M 4 LYS F  98  SER F 104  0
SHEET    2   M 4 LEU F 114  PHE F 122 -1  O  VAL F 116   N  TYR F 102
SHEET    3   M 4 PHE F 155  GLU F 162 -1  O  PHE F 155   N  PHE F 122
SHEET    4   M 4 ILE F 148  GLN F 149 -1  N  ILE F 148   O  GLN F 156
SHEET    1   N 4 GLN F 136  GLU F 138  0
SHEET    2   N 4 GLU F 128  ARG F 133 -1  N  TRP F 131   O  GLU F 138
SHEET    3   N 4 VAL F 170  GLU F 176 -1  O  GLN F 174   N  ARG F 130
SHEET    4   N 4 LEU F 184  ARG F 189 -1  O  LEU F 184   N  VAL F 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
SSBOND   4 CYS E  107    CYS E  163                          1555   1555  2.04
SSBOND   5 CYS F   15    CYS F   79                          1555   1555  2.04
SSBOND   6 CYS F  117    CYS F  173                          1555   1555  2.03
LINK         C   PHE A  22                 N   MSE A  23     1555   1555  1.33
LINK         C   MSE A  23                 N   PHE A  24     1555   1555  1.33
LINK         C   ASP A  35                 N   MSE A  36     1555   1555  1.33
LINK         C   MSE A  36                 N   ALA A  37     1555   1555  1.33
LINK         C   ILE A  72                 N   MSE A  73     1555   1555  1.33
LINK         C   MSE A  73                 N   THR A  74     1555   1555  1.33
LINK         C   PHE E  22                 N   MSE E  23     1555   1555  1.33
LINK         C   MSE E  23                 N   PHE E  24     1555   1555  1.33
LINK         C   ASP E  35                 N   MSE E  36     1555   1555  1.33
LINK         C   MSE E  36                 N   ALA E  37     1555   1555  1.33
LINK         C   ILE E  72                 N   MSE E  73     1555   1555  1.33
LINK         C   MSE E  73                 N   THR E  74     1555   1555  1.33
CISPEP   1 ASN A   15    PRO A   16          0        -0.27
CISPEP   2 THR A  113    PRO A  114          0        -0.26
CISPEP   3 TYR B  123    PRO B  124          0        -0.27
CISPEP   4 ASN E   15    PRO E   16          0         0.28
CISPEP   5 THR E  113    PRO E  114          0        -0.10
CISPEP   6 TYR F  123    PRO F  124          0         0.30
SITE     1 AC1  8 ALA A  61  PO4 C 202  LYS C 310  ALA D  11
SITE     2 AC1  8 GLN D  12  HIS D  14  LYS D 113  ASP D 117
SITE     1 AC2  6 GLY A  58  LYS C 307  LYS C 310  LYS D  10
SITE     2 AC2  6 LYS D 113  PO4 D 214
SITE     1 AC3  7 PO4 E 204  LYS G 310  ALA H  11  GLN H  12
SITE     2 AC3  7 HIS H  14  LYS H 113  ASP H 117
SITE     1 AC4  4 GLU E  55  GLY E  58  LYS G 310  PO4 H 214
CRYST1  137.735  179.555  179.952  90.00  90.00  90.00 I 2 2 2      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      0.007260  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005569  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005557        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

spacer

spacer