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PDBsum entry 3it8

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Top Page protein ligands Protein-protein interface(s) links
Immune system PDB id
3it8
Jmol
Contents
Protein chains
(+ 0 more) 152 a.a.
(+ 0 more) 299 a.a.
Ligands
NAG ×18
Waters ×96
HEADER    IMMUNE SYSTEM                           27-AUG-09   3IT8
TITLE     CRYSTAL STRUCTURE OF TNF ALPHA COMPLEXED WITH A POXVIRUS MHC-RELATED
TITLE    2 TNF BINDING PROTEIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;
COMPND   3 CHAIN: A, B, C, G, H, I;
COMPND   4 FRAGMENT: TUMOR NECROSIS FACTOR, SOLUBLE FORM, UNP RESIDUES 82-233;
COMPND   5 SYNONYM: TNF-ALPHA, TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER
COMPND   6 2, TNF-A, CACHECTIN, TUMOR NECROSIS FACTOR, MEMBRANE FORM, TUMOR
COMPND   7 NECROSIS FACTOR, SOLUBLE FORM;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: 2L PROTEIN;
COMPND  11 CHAIN: D, E, F, J, K, L;
COMPND  12 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: TNF;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET23A;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: YABA-LIKE DISEASE VIRUS;
SOURCE  12 ORGANISM_COMMON: YLDV;
SOURCE  13 ORGANISM_TAXID: 132475;
SOURCE  14 STRAIN: ATCC VR-937;
SOURCE  15 GENE: 2L;
SOURCE  16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: CELL_LINE: BTI-TN-5B1-4;
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PACUW31
KEYWDS    MHC CLASS I HOMOLOG, CELL MEMBRANE, CYTOKINE, DISULFIDE BOND,
KEYWDS   2 GLYCOPROTEIN, LIPOPROTEIN, MEMBRANE, MYRISTATE, PHOSPHOPROTEIN,
KEYWDS   3 SECRETED, SIGNAL-ANCHOR, TRANSMEMBRANE, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Z.YANG,A.P.WEST JR.,P.J.BJORKMAN
REVDAT   2   13-JUL-11 3IT8    1       VERSN
REVDAT   1   20-OCT-09 3IT8    0
JRNL        AUTH   Z.YANG,A.P.WEST JR.,P.J.BJORKMAN
JRNL        TITL   CRYSTAL STRUCTURE OF TNFA COMPLEXED WITH A POXVIRUS
JRNL        TITL 2 MHC-RELATED TNF BINDING PROTEIN
JRNL        REF    NAT.STRUCT.MOL.BIOL.
JRNL        REFN                   ESSN 1545-9985
JRNL        DOI    10.1038/NSMB.1683
REMARK   2
REMARK   2 RESOLUTION.    2.80 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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.77
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)   (%) : 96.8
REMARK   3   NUMBER OF REFLECTIONS             : 98697
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) : 0.236
REMARK   3   FREE R VALUE                     : 0.266
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 4965
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3750
REMARK   3   BIN FREE R VALUE                    : 0.3521
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 76
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            : 21654
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 252
REMARK   3   SOLVENT ATOMS            : 96
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.42
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 28.90000
REMARK   3    B22 (A**2) : -12.36700
REMARK   3    B33 (A**2) : -16.53200
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -8.14100
REMARK   3    B23 (A**2) : 0.00000
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.48
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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        : 44.31
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 3IT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB054836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0047
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : RH COATED FLAT MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 99161
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.08100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.47200
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1TNF AND PDB ENTRY 1T7V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, SODIUM CITRATE, 0.2M NABR,
REMARK 280  PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       85.14750
REMARK 290   SMTRY3   2  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 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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
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     MET A    -3
REMARK 465     GLY A    -2
REMARK 465     SER A    -1
REMARK 465     HIS A     0
REMARK 465     HIS A     1
REMARK 465     HIS A     2
REMARK 465     HIS A     3
REMARK 465     HIS A     4
REMARK 465     HIS A     5
REMARK 465     MET B    -3
REMARK 465     GLY B    -2
REMARK 465     SER B    -1
REMARK 465     HIS B     0
REMARK 465     HIS B     1
REMARK 465     HIS B     2
REMARK 465     HIS B     3
REMARK 465     HIS B     4
REMARK 465     HIS B     5
REMARK 465     MET C    -3
REMARK 465     GLY C    -2
REMARK 465     SER C    -1
REMARK 465     HIS C     0
REMARK 465     HIS C     1
REMARK 465     HIS C     2
REMARK 465     HIS C     3
REMARK 465     HIS C     4
REMARK 465     HIS C     5
REMARK 465     ASN D   300
REMARK 465     GLY D   301
REMARK 465     GLU D   302
REMARK 465     LEU D   303
REMARK 465     TYR D   304
REMARK 465     ASP D   305
REMARK 465     HIS D   306
REMARK 465     LEU D   307
REMARK 465     TYR D   308
REMARK 465     ARG D   309
REMARK 465     LYS D   310
REMARK 465     THR D   311
REMARK 465     GLU D   312
REMARK 465     GLU D   313
REMARK 465     GLY D   314
REMARK 465     GLU D   315
REMARK 465     GLY D   316
REMARK 465     GLY D   317
REMARK 465     SER D   318
REMARK 465     HIS D   319
REMARK 465     HIS D   320
REMARK 465     HIS D   321
REMARK 465     HIS D   322
REMARK 465     HIS D   323
REMARK 465     HIS D   324
REMARK 465     ASN E   300
REMARK 465     GLY E   301
REMARK 465     GLU E   302
REMARK 465     LEU E   303
REMARK 465     TYR E   304
REMARK 465     ASP E   305
REMARK 465     HIS E   306
REMARK 465     LEU E   307
REMARK 465     TYR E   308
REMARK 465     ARG E   309
REMARK 465     LYS E   310
REMARK 465     THR E   311
REMARK 465     GLU E   312
REMARK 465     GLU E   313
REMARK 465     GLY E   314
REMARK 465     GLU E   315
REMARK 465     GLY E   316
REMARK 465     GLY E   317
REMARK 465     SER E   318
REMARK 465     HIS E   319
REMARK 465     HIS E   320
REMARK 465     HIS E   321
REMARK 465     HIS E   322
REMARK 465     HIS E   323
REMARK 465     HIS E   324
REMARK 465     ASN F   300
REMARK 465     GLY F   301
REMARK 465     GLU F   302
REMARK 465     LEU F   303
REMARK 465     TYR F   304
REMARK 465     ASP F   305
REMARK 465     HIS F   306
REMARK 465     LEU F   307
REMARK 465     TYR F   308
REMARK 465     ARG F   309
REMARK 465     LYS F   310
REMARK 465     THR F   311
REMARK 465     GLU F   312
REMARK 465     GLU F   313
REMARK 465     GLY F   314
REMARK 465     GLU F   315
REMARK 465     GLY F   316
REMARK 465     GLY F   317
REMARK 465     SER F   318
REMARK 465     HIS F   319
REMARK 465     HIS F   320
REMARK 465     HIS F   321
REMARK 465     HIS F   322
REMARK 465     HIS F   323
REMARK 465     HIS F   324
REMARK 465     MET G    -3
REMARK 465     GLY G    -2
REMARK 465     SER G    -1
REMARK 465     HIS G     0
REMARK 465     HIS G     1
REMARK 465     HIS G     2
REMARK 465     HIS G     3
REMARK 465     HIS G     4
REMARK 465     HIS G     5
REMARK 465     MET H    -3
REMARK 465     GLY H    -2
REMARK 465     SER H    -1
REMARK 465     HIS H     0
REMARK 465     HIS H     1
REMARK 465     HIS H     2
REMARK 465     HIS H     3
REMARK 465     HIS H     4
REMARK 465     HIS H     5
REMARK 465     MET I    -3
REMARK 465     GLY I    -2
REMARK 465     SER I    -1
REMARK 465     HIS I     0
REMARK 465     HIS I     1
REMARK 465     HIS I     2
REMARK 465     HIS I     3
REMARK 465     HIS I     4
REMARK 465     HIS I     5
REMARK 465     ASN J   300
REMARK 465     GLY J   301
REMARK 465     GLU J   302
REMARK 465     LEU J   303
REMARK 465     TYR J   304
REMARK 465     ASP J   305
REMARK 465     HIS J   306
REMARK 465     LEU J   307
REMARK 465     TYR J   308
REMARK 465     ARG J   309
REMARK 465     LYS J   310
REMARK 465     THR J   311
REMARK 465     GLU J   312
REMARK 465     GLU J   313
REMARK 465     GLY J   314
REMARK 465     GLU J   315
REMARK 465     GLY J   316
REMARK 465     GLY J   317
REMARK 465     SER J   318
REMARK 465     HIS J   319
REMARK 465     HIS J   320
REMARK 465     HIS J   321
REMARK 465     HIS J   322
REMARK 465     HIS J   323
REMARK 465     HIS J   324
REMARK 465     ASN K   300
REMARK 465     GLY K   301
REMARK 465     GLU K   302
REMARK 465     LEU K   303
REMARK 465     TYR K   304
REMARK 465     ASP K   305
REMARK 465     HIS K   306
REMARK 465     LEU K   307
REMARK 465     TYR K   308
REMARK 465     ARG K   309
REMARK 465     LYS K   310
REMARK 465     THR K   311
REMARK 465     GLU K   312
REMARK 465     GLU K   313
REMARK 465     GLY K   314
REMARK 465     GLU K   315
REMARK 465     GLY K   316
REMARK 465     GLY K   317
REMARK 465     SER K   318
REMARK 465     HIS K   319
REMARK 465     HIS K   320
REMARK 465     HIS K   321
REMARK 465     HIS K   322
REMARK 465     HIS K   323
REMARK 465     HIS K   324
REMARK 465     ASN L   300
REMARK 465     GLY L   301
REMARK 465     GLU L   302
REMARK 465     LEU L   303
REMARK 465     TYR L   304
REMARK 465     ASP L   305
REMARK 465     HIS L   306
REMARK 465     LEU L   307
REMARK 465     TYR L   308
REMARK 465     ARG L   309
REMARK 465     LYS L   310
REMARK 465     THR L   311
REMARK 465     GLU L   312
REMARK 465     GLU L   313
REMARK 465     GLY L   314
REMARK 465     GLU L   315
REMARK 465     GLY L   316
REMARK 465     GLY L   317
REMARK 465     SER L   318
REMARK 465     HIS L   319
REMARK 465     HIS L   320
REMARK 465     HIS L   321
REMARK 465     HIS L   322
REMARK 465     HIS L   323
REMARK 465     HIS L   324
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   O    ASP D    14     OD1  ASN J    62     2545     2.12
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    LEU D 288   CA  -  CB  -  CG  ANGL. DEV. =  20.5 DEGREES
REMARK 500    LEU E 288   CA  -  CB  -  CG  ANGL. DEV. =  20.6 DEGREES
REMARK 500    LEU F 288   CA  -  CB  -  CG  ANGL. DEV. =  19.7 DEGREES
REMARK 500    LEU J 288   CA  -  CB  -  CG  ANGL. DEV. =  20.7 DEGREES
REMARK 500    LEU K 288   CA  -  CB  -  CG  ANGL. DEV. =  20.7 DEGREES
REMARK 500    LEU L 288   CA  -  CB  -  CG  ANGL. DEV. =  20.1 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    SER A   9      -36.82    160.50
REMARK 500    ASP A  10      -20.59    111.42
REMARK 500    ALA A  22       63.12   -119.79
REMARK 500    ARG A  31       47.29    -88.21
REMARK 500    ALA A  33      -86.12    -27.84
REMARK 500    ASN A  34       61.52   -109.03
REMARK 500    LEU A  37       83.98   -164.38
REMARK 500    PRO A  70     -151.01    -73.03
REMARK 500    THR A  72     -100.79     30.11
REMARK 500    TYR A  87       73.04   -166.97
REMARK 500    GLN A  88       70.83    -52.76
REMARK 500    PRO A 100      -76.35    -63.37
REMARK 500    GLN A 102       43.66    -78.46
REMARK 500    ARG A 103       -0.11     73.34
REMARK 500    THR A 105      118.26     47.62
REMARK 500    GLU A 110     -121.98     99.10
REMARK 500    ALA A 111       81.19     87.42
REMARK 500    GLU A 146      -81.71    -71.75
REMARK 500    SER A 147      -75.50    177.95
REMARK 500    SER B   9      -36.30    160.40
REMARK 500    ASP B  10      -22.65    111.48
REMARK 500    ARG B  31       46.66    -87.38
REMARK 500    ALA B  33      -86.28    -28.69
REMARK 500    ASN B  34       60.06   -108.40
REMARK 500    LEU B  37       82.41   -164.98
REMARK 500    PRO B  70     -150.95    -72.79
REMARK 500    THR B  72     -100.81     29.88
REMARK 500    TYR B  87       73.12   -166.75
REMARK 500    GLN B  88       71.36    -53.38
REMARK 500    PRO B 100      -76.76    -63.44
REMARK 500    GLN B 102       43.62    -78.45
REMARK 500    ARG B 103       -0.05     73.34
REMARK 500    THR B 105      118.01     48.06
REMARK 500    GLU B 110     -122.25     98.91
REMARK 500    ALA B 111       81.10     87.31
REMARK 500    GLU B 146      -81.83    -71.49
REMARK 500    SER B 147      -75.81    177.99
REMARK 500    SER C   9      -36.56    160.00
REMARK 500    ASP C  10      -21.66    111.36
REMARK 500    ARG C  31       46.68    -87.61
REMARK 500    ALA C  33      -85.06    -27.91
REMARK 500    ASN C  34       59.64   -110.37
REMARK 500    LEU C  37       83.50   -164.97
REMARK 500    PRO C  70     -150.50    -72.37
REMARK 500    THR C  72     -100.56     29.96
REMARK 500    TYR C  87       72.74   -167.89
REMARK 500    GLN C  88       70.56    -52.96
REMARK 500    PRO C 100      -76.51    -64.29
REMARK 500    GLN C 102       43.84    -78.45
REMARK 500    THR C 105      118.07     48.00
REMARK 500
REMARK 500 THIS ENTRY HAS     299 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLU D 236        23.7      L          L   OUTSIDE RANGE
REMARK 500    GLU E 236        23.8      L          L   OUTSIDE RANGE
REMARK 500    GLU F 236        23.6      L          L   OUTSIDE RANGE
REMARK 500    GLU J 236        23.6      L          L   OUTSIDE RANGE
REMARK 500    GLU K 236        23.7      L          L   OUTSIDE RANGE
REMARK 500    GLU L 236        23.7      L          L   OUTSIDE RANGE
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 NAG D 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG J 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG K 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 327
DBREF  3IT8 A    6   157  UNP    P01375   TNFA_HUMAN      82    233
DBREF  3IT8 B    6   157  UNP    P01375   TNFA_HUMAN      82    233
DBREF  3IT8 C    6   157  UNP    P01375   TNFA_HUMAN      82    233
DBREF  3IT8 D    1   316  UNP    Q9DHW0   Q9DHW0_YLDV     17    332
DBREF  3IT8 E    1   316  UNP    Q9DHW0   Q9DHW0_YLDV     17    332
DBREF  3IT8 F    1   316  UNP    Q9DHW0   Q9DHW0_YLDV     17    332
DBREF  3IT8 G    6   157  UNP    P01375   TNFA_HUMAN      82    233
DBREF  3IT8 H    6   157  UNP    P01375   TNFA_HUMAN      82    233
DBREF  3IT8 I    6   157  UNP    P01375   TNFA_HUMAN      82    233
DBREF  3IT8 J    1   316  UNP    Q9DHW0   Q9DHW0_YLDV     17    332
DBREF  3IT8 K    1   316  UNP    Q9DHW0   Q9DHW0_YLDV     17    332
DBREF  3IT8 L    1   316  UNP    Q9DHW0   Q9DHW0_YLDV     17    332
SEQADV 3IT8 MET A   -3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 GLY A   -2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 SER A   -1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS A    0  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS A    1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS A    2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS A    3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS A    4  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS A    5  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 LEU A  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 3IT8 MET B   -3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 GLY B   -2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 SER B   -1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS B    0  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS B    1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS B    2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS B    3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS B    4  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS B    5  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 LEU B  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 3IT8 MET C   -3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 GLY C   -2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 SER C   -1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS C    0  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS C    1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS C    2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS C    3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS C    4  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS C    5  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 LEU C  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 3IT8 GLY D  317  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 SER D  318  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS D  319  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS D  320  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS D  321  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS D  322  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS D  323  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS D  324  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 GLY E  317  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 SER E  318  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS E  319  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS E  320  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS E  321  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS E  322  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS E  323  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS E  324  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 GLY F  317  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 SER F  318  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS F  319  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS F  320  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS F  321  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS F  322  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS F  323  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS F  324  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 MET G   -3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 GLY G   -2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 SER G   -1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS G    0  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS G    1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS G    2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS G    3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS G    4  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS G    5  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 LEU G  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 3IT8 MET H   -3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 GLY H   -2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 SER H   -1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS H    0  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS H    1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS H    2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS H    3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS H    4  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS H    5  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 LEU H  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 3IT8 MET I   -3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 GLY I   -2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 SER I   -1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS I    0  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS I    1  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS I    2  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS I    3  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS I    4  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 HIS I    5  UNP  P01375              EXPRESSION TAG
SEQADV 3IT8 LEU I  143  UNP  P01375    ASP   219 CONFLICT
SEQADV 3IT8 GLY J  317  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 SER J  318  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS J  319  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS J  320  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS J  321  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS J  322  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS J  323  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS J  324  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 GLY K  317  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 SER K  318  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS K  319  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS K  320  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS K  321  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS K  322  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS K  323  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS K  324  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 GLY L  317  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 SER L  318  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS L  319  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS L  320  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS L  321  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS L  322  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS L  323  UNP  Q9DHW0              EXPRESSION TAG
SEQADV 3IT8 HIS L  324  UNP  Q9DHW0              EXPRESSION TAG
SEQRES   1 A  161  MET GLY SER HIS HIS HIS HIS HIS HIS ARG THR PRO SER
SEQRES   2 A  161  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA
SEQRES   3 A  161  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA
SEQRES   4 A  161  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU
SEQRES   5 A  161  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN
SEQRES   6 A  161  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL
SEQRES   7 A  161  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR
SEQRES   8 A  161  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO
SEQRES   9 A  161  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO
SEQRES  10 A  161  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU
SEQRES  11 A  161  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO
SEQRES  12 A  161  ASP TYR LEU LEU PHE ALA GLU SER GLY GLN VAL TYR PHE
SEQRES  13 A  161  GLY ILE ILE ALA LEU
SEQRES   1 B  161  MET GLY SER HIS HIS HIS HIS HIS HIS ARG THR PRO SER
SEQRES   2 B  161  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA
SEQRES   3 B  161  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA
SEQRES   4 B  161  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU
SEQRES   5 B  161  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN
SEQRES   6 B  161  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL
SEQRES   7 B  161  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR
SEQRES   8 B  161  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO
SEQRES   9 B  161  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO
SEQRES  10 B  161  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU
SEQRES  11 B  161  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO
SEQRES  12 B  161  ASP TYR LEU LEU PHE ALA GLU SER GLY GLN VAL TYR PHE
SEQRES  13 B  161  GLY ILE ILE ALA LEU
SEQRES   1 C  161  MET GLY SER HIS HIS HIS HIS HIS HIS ARG THR PRO SER
SEQRES   2 C  161  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA
SEQRES   3 C  161  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA
SEQRES   4 C  161  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU
SEQRES   5 C  161  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN
SEQRES   6 C  161  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL
SEQRES   7 C  161  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR
SEQRES   8 C  161  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO
SEQRES   9 C  161  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO
SEQRES  10 C  161  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU
SEQRES  11 C  161  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO
SEQRES  12 C  161  ASP TYR LEU LEU PHE ALA GLU SER GLY GLN VAL TYR PHE
SEQRES  13 C  161  GLY ILE ILE ALA LEU
SEQRES   1 D  324  ILE THR LEU LYS TYR ASN TYR THR VAL THR LEU LYS ASP
SEQRES   2 D  324  ASP GLY LEU TYR ASP GLY VAL PHE TYR ASP HIS TYR ASN
SEQRES   3 D  324  ASP GLN LEU VAL THR LYS ILE SER TYR ASN HIS GLU THR
SEQRES   4 D  324  ARG HIS GLY ASN VAL ASN PHE ARG ALA ASP TRP PHE ASN
SEQRES   5 D  324  ILE SER ARG SER PRO HIS THR PRO GLY ASN ASP TYR ASN
SEQRES   6 D  324  PHE ASN PHE TRP TYR SER LEU MET LYS GLU THR LEU GLU
SEQRES   7 D  324  GLU ILE ASN LYS ASN ASP SER THR LYS THR THR SER LEU
SEQRES   8 D  324  SER LEU ILE THR GLY CYS TYR GLU THR GLY LEU LEU PHE
SEQRES   9 D  324  GLY SER TYR GLY TYR VAL GLU THR ALA ASN GLY PRO LEU
SEQRES  10 D  324  ALA ARG TYR HIS THR GLY ASP LYS ARG PHE THR LYS MET
SEQRES  11 D  324  THR HIS LYS GLY PHE PRO LYS VAL GLY MET LEU THR VAL
SEQRES  12 D  324  LYS ASN THR LEU TRP LYS ASP VAL LYS ALA TYR LEU GLY
SEQRES  13 D  324  GLY PHE GLU TYR MET GLY CYS SER LEU ALA ILE LEU ASP
SEQRES  14 D  324  TYR GLN LYS MET ALA LYS GLY LYS ILE PRO LYS ASP THR
SEQRES  15 D  324  THR PRO THR VAL LYS VAL THR GLY ASN GLU LEU GLU ASP
SEQRES  16 D  324  GLY ASN MET THR LEU GLU CYS THR VAL ASN SER PHE TYR
SEQRES  17 D  324  PRO PRO ASP VAL ILE THR LYS TRP ILE GLU SER GLU HIS
SEQRES  18 D  324  PHE LYS GLY GLU TYR LYS TYR VAL ASN GLY ARG TYR TYR
SEQRES  19 D  324  PRO GLU TRP GLY ARG LYS SER ASN TYR GLU PRO GLY GLU
SEQRES  20 D  324  PRO GLY PHE PRO TRP ASN ILE LYS LYS ASP LYS ASP ALA
SEQRES  21 D  324  ASN THR TYR SER LEU THR ASP LEU VAL ARG THR THR SER
SEQRES  22 D  324  LYS MET SER SER GLN PRO VAL CYS VAL VAL PHE HIS ASP
SEQRES  23 D  324  THR LEU GLU ALA GLN VAL TYR THR CYS SER GLU GLY CYS
SEQRES  24 D  324  ASN GLY GLU LEU TYR ASP HIS LEU TYR ARG LYS THR GLU
SEQRES  25 D  324  GLU GLY GLU GLY GLY SER HIS HIS HIS HIS HIS HIS
SEQRES   1 E  324  ILE THR LEU LYS TYR ASN TYR THR VAL THR LEU LYS ASP
SEQRES   2 E  324  ASP GLY LEU TYR ASP GLY VAL PHE TYR ASP HIS TYR ASN
SEQRES   3 E  324  ASP GLN LEU VAL THR LYS ILE SER TYR ASN HIS GLU THR
SEQRES   4 E  324  ARG HIS GLY ASN VAL ASN PHE ARG ALA ASP TRP PHE ASN
SEQRES   5 E  324  ILE SER ARG SER PRO HIS THR PRO GLY ASN ASP TYR ASN
SEQRES   6 E  324  PHE ASN PHE TRP TYR SER LEU MET LYS GLU THR LEU GLU
SEQRES   7 E  324  GLU ILE ASN LYS ASN ASP SER THR LYS THR THR SER LEU
SEQRES   8 E  324  SER LEU ILE THR GLY CYS TYR GLU THR GLY LEU LEU PHE
SEQRES   9 E  324  GLY SER TYR GLY TYR VAL GLU THR ALA ASN GLY PRO LEU
SEQRES  10 E  324  ALA ARG TYR HIS THR GLY ASP LYS ARG PHE THR LYS MET
SEQRES  11 E  324  THR HIS LYS GLY PHE PRO LYS VAL GLY MET LEU THR VAL
SEQRES  12 E  324  LYS ASN THR LEU TRP LYS ASP VAL LYS ALA TYR LEU GLY
SEQRES  13 E  324  GLY PHE GLU TYR MET GLY CYS SER LEU ALA ILE LEU ASP
SEQRES  14 E  324  TYR GLN LYS MET ALA LYS GLY LYS ILE PRO LYS ASP THR
SEQRES  15 E  324  THR PRO THR VAL LYS VAL THR GLY ASN GLU LEU GLU ASP
SEQRES  16 E  324  GLY ASN MET THR LEU GLU CYS THR VAL ASN SER PHE TYR
SEQRES  17 E  324  PRO PRO ASP VAL ILE THR LYS TRP ILE GLU SER GLU HIS
SEQRES  18 E  324  PHE LYS GLY GLU TYR LYS TYR VAL ASN GLY ARG TYR TYR
SEQRES  19 E  324  PRO GLU TRP GLY ARG LYS SER ASN TYR GLU PRO GLY GLU
SEQRES  20 E  324  PRO GLY PHE PRO TRP ASN ILE LYS LYS ASP LYS ASP ALA
SEQRES  21 E  324  ASN THR TYR SER LEU THR ASP LEU VAL ARG THR THR SER
SEQRES  22 E  324  LYS MET SER SER GLN PRO VAL CYS VAL VAL PHE HIS ASP
SEQRES  23 E  324  THR LEU GLU ALA GLN VAL TYR THR CYS SER GLU GLY CYS
SEQRES  24 E  324  ASN GLY GLU LEU TYR ASP HIS LEU TYR ARG LYS THR GLU
SEQRES  25 E  324  GLU GLY GLU GLY GLY SER HIS HIS HIS HIS HIS HIS
SEQRES   1 F  324  ILE THR LEU LYS TYR ASN TYR THR VAL THR LEU LYS ASP
SEQRES   2 F  324  ASP GLY LEU TYR ASP GLY VAL PHE TYR ASP HIS TYR ASN
SEQRES   3 F  324  ASP GLN LEU VAL THR LYS ILE SER TYR ASN HIS GLU THR
SEQRES   4 F  324  ARG HIS GLY ASN VAL ASN PHE ARG ALA ASP TRP PHE ASN
SEQRES   5 F  324  ILE SER ARG SER PRO HIS THR PRO GLY ASN ASP TYR ASN
SEQRES   6 F  324  PHE ASN PHE TRP TYR SER LEU MET LYS GLU THR LEU GLU
SEQRES   7 F  324  GLU ILE ASN LYS ASN ASP SER THR LYS THR THR SER LEU
SEQRES   8 F  324  SER LEU ILE THR GLY CYS TYR GLU THR GLY LEU LEU PHE
SEQRES   9 F  324  GLY SER TYR GLY TYR VAL GLU THR ALA ASN GLY PRO LEU
SEQRES  10 F  324  ALA ARG TYR HIS THR GLY ASP LYS ARG PHE THR LYS MET
SEQRES  11 F  324  THR HIS LYS GLY PHE PRO LYS VAL GLY MET LEU THR VAL
SEQRES  12 F  324  LYS ASN THR LEU TRP LYS ASP VAL LYS ALA TYR LEU GLY
SEQRES  13 F  324  GLY PHE GLU TYR MET GLY CYS SER LEU ALA ILE LEU ASP
SEQRES  14 F  324  TYR GLN LYS MET ALA LYS GLY LYS ILE PRO LYS ASP THR
SEQRES  15 F  324  THR PRO THR VAL LYS VAL THR GLY ASN GLU LEU GLU ASP
SEQRES  16 F  324  GLY ASN MET THR LEU GLU CYS THR VAL ASN SER PHE TYR
SEQRES  17 F  324  PRO PRO ASP VAL ILE THR LYS TRP ILE GLU SER GLU HIS
SEQRES  18 F  324  PHE LYS GLY GLU TYR LYS TYR VAL ASN GLY ARG TYR TYR
SEQRES  19 F  324  PRO GLU TRP GLY ARG LYS SER ASN TYR GLU PRO GLY GLU
SEQRES  20 F  324  PRO GLY PHE PRO TRP ASN ILE LYS LYS ASP LYS ASP ALA
SEQRES  21 F  324  ASN THR TYR SER LEU THR ASP LEU VAL ARG THR THR SER
SEQRES  22 F  324  LYS MET SER SER GLN PRO VAL CYS VAL VAL PHE HIS ASP
SEQRES  23 F  324  THR LEU GLU ALA GLN VAL TYR THR CYS SER GLU GLY CYS
SEQRES  24 F  324  ASN GLY GLU LEU TYR ASP HIS LEU TYR ARG LYS THR GLU
SEQRES  25 F  324  GLU GLY GLU GLY GLY SER HIS HIS HIS HIS HIS HIS
SEQRES   1 G  161  MET GLY SER HIS HIS HIS HIS HIS HIS ARG THR PRO SER
SEQRES   2 G  161  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA
SEQRES   3 G  161  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA
SEQRES   4 G  161  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU
SEQRES   5 G  161  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN
SEQRES   6 G  161  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL
SEQRES   7 G  161  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR
SEQRES   8 G  161  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO
SEQRES   9 G  161  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO
SEQRES  10 G  161  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU
SEQRES  11 G  161  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO
SEQRES  12 G  161  ASP TYR LEU LEU PHE ALA GLU SER GLY GLN VAL TYR PHE
SEQRES  13 G  161  GLY ILE ILE ALA LEU
SEQRES   1 H  161  MET GLY SER HIS HIS HIS HIS HIS HIS ARG THR PRO SER
SEQRES   2 H  161  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA
SEQRES   3 H  161  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA
SEQRES   4 H  161  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU
SEQRES   5 H  161  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN
SEQRES   6 H  161  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL
SEQRES   7 H  161  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR
SEQRES   8 H  161  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO
SEQRES   9 H  161  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO
SEQRES  10 H  161  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU
SEQRES  11 H  161  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO
SEQRES  12 H  161  ASP TYR LEU LEU PHE ALA GLU SER GLY GLN VAL TYR PHE
SEQRES  13 H  161  GLY ILE ILE ALA LEU
SEQRES   1 I  161  MET GLY SER HIS HIS HIS HIS HIS HIS ARG THR PRO SER
SEQRES   2 I  161  ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO GLN ALA
SEQRES   3 I  161  GLU GLY GLN LEU GLN TRP LEU ASN ARG ARG ALA ASN ALA
SEQRES   4 I  161  LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN GLN LEU
SEQRES   5 I  161  VAL VAL PRO SER GLU GLY LEU TYR LEU ILE TYR SER GLN
SEQRES   6 I  161  VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR HIS VAL
SEQRES   7 I  161  LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL SER TYR
SEQRES   8 I  161  GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS SER PRO
SEQRES   9 I  161  CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA LYS PRO
SEQRES  10 I  161  TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE GLN LEU
SEQRES  11 I  161  GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN ARG PRO
SEQRES  12 I  161  ASP TYR LEU LEU PHE ALA GLU SER GLY GLN VAL TYR PHE
SEQRES  13 I  161  GLY ILE ILE ALA LEU
SEQRES   1 J  324  ILE THR LEU LYS TYR ASN TYR THR VAL THR LEU LYS ASP
SEQRES   2 J  324  ASP GLY LEU TYR ASP GLY VAL PHE TYR ASP HIS TYR ASN
SEQRES   3 J  324  ASP GLN LEU VAL THR LYS ILE SER TYR ASN HIS GLU THR
SEQRES   4 J  324  ARG HIS GLY ASN VAL ASN PHE ARG ALA ASP TRP PHE ASN
SEQRES   5 J  324  ILE SER ARG SER PRO HIS THR PRO GLY ASN ASP TYR ASN
SEQRES   6 J  324  PHE ASN PHE TRP TYR SER LEU MET LYS GLU THR LEU GLU
SEQRES   7 J  324  GLU ILE ASN LYS ASN ASP SER THR LYS THR THR SER LEU
SEQRES   8 J  324  SER LEU ILE THR GLY CYS TYR GLU THR GLY LEU LEU PHE
SEQRES   9 J  324  GLY SER TYR GLY TYR VAL GLU THR ALA ASN GLY PRO LEU
SEQRES  10 J  324  ALA ARG TYR HIS THR GLY ASP LYS ARG PHE THR LYS MET
SEQRES  11 J  324  THR HIS LYS GLY PHE PRO LYS VAL GLY MET LEU THR VAL
SEQRES  12 J  324  LYS ASN THR LEU TRP LYS ASP VAL LYS ALA TYR LEU GLY
SEQRES  13 J  324  GLY PHE GLU TYR MET GLY CYS SER LEU ALA ILE LEU ASP
SEQRES  14 J  324  TYR GLN LYS MET ALA LYS GLY LYS ILE PRO LYS ASP THR
SEQRES  15 J  324  THR PRO THR VAL LYS VAL THR GLY ASN GLU LEU GLU ASP
SEQRES  16 J  324  GLY ASN MET THR LEU GLU CYS THR VAL ASN SER PHE TYR
SEQRES  17 J  324  PRO PRO ASP VAL ILE THR LYS TRP ILE GLU SER GLU HIS
SEQRES  18 J  324  PHE LYS GLY GLU TYR LYS TYR VAL ASN GLY ARG TYR TYR
SEQRES  19 J  324  PRO GLU TRP GLY ARG LYS SER ASN TYR GLU PRO GLY GLU
SEQRES  20 J  324  PRO GLY PHE PRO TRP ASN ILE LYS LYS ASP LYS ASP ALA
SEQRES  21 J  324  ASN THR TYR SER LEU THR ASP LEU VAL ARG THR THR SER
SEQRES  22 J  324  LYS MET SER SER GLN PRO VAL CYS VAL VAL PHE HIS ASP
SEQRES  23 J  324  THR LEU GLU ALA GLN VAL TYR THR CYS SER GLU GLY CYS
SEQRES  24 J  324  ASN GLY GLU LEU TYR ASP HIS LEU TYR ARG LYS THR GLU
SEQRES  25 J  324  GLU GLY GLU GLY GLY SER HIS HIS HIS HIS HIS HIS
SEQRES   1 K  324  ILE THR LEU LYS TYR ASN TYR THR VAL THR LEU LYS ASP
SEQRES   2 K  324  ASP GLY LEU TYR ASP GLY VAL PHE TYR ASP HIS TYR ASN
SEQRES   3 K  324  ASP GLN LEU VAL THR LYS ILE SER TYR ASN HIS GLU THR
SEQRES   4 K  324  ARG HIS GLY ASN VAL ASN PHE ARG ALA ASP TRP PHE ASN
SEQRES   5 K  324  ILE SER ARG SER PRO HIS THR PRO GLY ASN ASP TYR ASN
SEQRES   6 K  324  PHE ASN PHE TRP TYR SER LEU MET LYS GLU THR LEU GLU
SEQRES   7 K  324  GLU ILE ASN LYS ASN ASP SER THR LYS THR THR SER LEU
SEQRES   8 K  324  SER LEU ILE THR GLY CYS TYR GLU THR GLY LEU LEU PHE
SEQRES   9 K  324  GLY SER TYR GLY TYR VAL GLU THR ALA ASN GLY PRO LEU
SEQRES  10 K  324  ALA ARG TYR HIS THR GLY ASP LYS ARG PHE THR LYS MET
SEQRES  11 K  324  THR HIS LYS GLY PHE PRO LYS VAL GLY MET LEU THR VAL
SEQRES  12 K  324  LYS ASN THR LEU TRP LYS ASP VAL LYS ALA TYR LEU GLY
SEQRES  13 K  324  GLY PHE GLU TYR MET GLY CYS SER LEU ALA ILE LEU ASP
SEQRES  14 K  324  TYR GLN LYS MET ALA LYS GLY LYS ILE PRO LYS ASP THR
SEQRES  15 K  324  THR PRO THR VAL LYS VAL THR GLY ASN GLU LEU GLU ASP
SEQRES  16 K  324  GLY ASN MET THR LEU GLU CYS THR VAL ASN SER PHE TYR
SEQRES  17 K  324  PRO PRO ASP VAL ILE THR LYS TRP ILE GLU SER GLU HIS
SEQRES  18 K  324  PHE LYS GLY GLU TYR LYS TYR VAL ASN GLY ARG TYR TYR
SEQRES  19 K  324  PRO GLU TRP GLY ARG LYS SER ASN TYR GLU PRO GLY GLU
SEQRES  20 K  324  PRO GLY PHE PRO TRP ASN ILE LYS LYS ASP LYS ASP ALA
SEQRES  21 K  324  ASN THR TYR SER LEU THR ASP LEU VAL ARG THR THR SER
SEQRES  22 K  324  LYS MET SER SER GLN PRO VAL CYS VAL VAL PHE HIS ASP
SEQRES  23 K  324  THR LEU GLU ALA GLN VAL TYR THR CYS SER GLU GLY CYS
SEQRES  24 K  324  ASN GLY GLU LEU TYR ASP HIS LEU TYR ARG LYS THR GLU
SEQRES  25 K  324  GLU GLY GLU GLY GLY SER HIS HIS HIS HIS HIS HIS
SEQRES   1 L  324  ILE THR LEU LYS TYR ASN TYR THR VAL THR LEU LYS ASP
SEQRES   2 L  324  ASP GLY LEU TYR ASP GLY VAL PHE TYR ASP HIS TYR ASN
SEQRES   3 L  324  ASP GLN LEU VAL THR LYS ILE SER TYR ASN HIS GLU THR
SEQRES   4 L  324  ARG HIS GLY ASN VAL ASN PHE ARG ALA ASP TRP PHE ASN
SEQRES   5 L  324  ILE SER ARG SER PRO HIS THR PRO GLY ASN ASP TYR ASN
SEQRES   6 L  324  PHE ASN PHE TRP TYR SER LEU MET LYS GLU THR LEU GLU
SEQRES   7 L  324  GLU ILE ASN LYS ASN ASP SER THR LYS THR THR SER LEU
SEQRES   8 L  324  SER LEU ILE THR GLY CYS TYR GLU THR GLY LEU LEU PHE
SEQRES   9 L  324  GLY SER TYR GLY TYR VAL GLU THR ALA ASN GLY PRO LEU
SEQRES  10 L  324  ALA ARG TYR HIS THR GLY ASP LYS ARG PHE THR LYS MET
SEQRES  11 L  324  THR HIS LYS GLY PHE PRO LYS VAL GLY MET LEU THR VAL
SEQRES  12 L  324  LYS ASN THR LEU TRP LYS ASP VAL LYS ALA TYR LEU GLY
SEQRES  13 L  324  GLY PHE GLU TYR MET GLY CYS SER LEU ALA ILE LEU ASP
SEQRES  14 L  324  TYR GLN LYS MET ALA LYS GLY LYS ILE PRO LYS ASP THR
SEQRES  15 L  324  THR PRO THR VAL LYS VAL THR GLY ASN GLU LEU GLU ASP
SEQRES  16 L  324  GLY ASN MET THR LEU GLU CYS THR VAL ASN SER PHE TYR
SEQRES  17 L  324  PRO PRO ASP VAL ILE THR LYS TRP ILE GLU SER GLU HIS
SEQRES  18 L  324  PHE LYS GLY GLU TYR LYS TYR VAL ASN GLY ARG TYR TYR
SEQRES  19 L  324  PRO GLU TRP GLY ARG LYS SER ASN TYR GLU PRO GLY GLU
SEQRES  20 L  324  PRO GLY PHE PRO TRP ASN ILE LYS LYS ASP LYS ASP ALA
SEQRES  21 L  324  ASN THR TYR SER LEU THR ASP LEU VAL ARG THR THR SER
SEQRES  22 L  324  LYS MET SER SER GLN PRO VAL CYS VAL VAL PHE HIS ASP
SEQRES  23 L  324  THR LEU GLU ALA GLN VAL TYR THR CYS SER GLU GLY CYS
SEQRES  24 L  324  ASN GLY GLU LEU TYR ASP HIS LEU TYR ARG LYS THR GLU
SEQRES  25 L  324  GLU GLY GLU GLY GLY SER HIS HIS HIS HIS HIS HIS
MODRES 3IT8 ASN D    6  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN D   52  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN D   83  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN E    6  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN E   52  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN E   83  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN F    6  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN F   52  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN F   83  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN J    6  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN J   52  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN J   83  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN K    6  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN K   52  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN K   83  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN L    6  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN L   52  ASN  GLYCOSYLATION SITE
MODRES 3IT8 ASN L   83  ASN  GLYCOSYLATION SITE
HET    NAG  D 325      14
HET    NAG  D 326      14
HET    NAG  D 327      14
HET    NAG  E 325      14
HET    NAG  E 326      14
HET    NAG  E 327      14
HET    NAG  F 325      14
HET    NAG  F 326      14
HET    NAG  F 327      14
HET    NAG  J 325      14
HET    NAG  J 326      14
HET    NAG  J 327      14
HET    NAG  K 325      14
HET    NAG  K 326      14
HET    NAG  K 327      14
HET    NAG  L 325      14
HET    NAG  L 326      14
HET    NAG  L 327      14
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL  13  NAG    18(C8 H15 N O6)
FORMUL  31  HOH   *96(H2 O)
HELIX    1   1 ARG A  138  LEU A  142  5                                   5
HELIX    2   2 ARG B  138  LEU B  142  5                                   5
HELIX    3   3 ARG C  138  LEU C  142  5                                   5
HELIX    4   4 ASN D   52  SER D   56  5                                   5
HELIX    5   5 PRO D   60  ASN D   83  1                                  24
HELIX    6   6 VAL D  138  THR D  142  5                                   5
HELIX    7   7 LEU D  147  MET D  161  1                                  15
HELIX    8   8 MET D  161  LYS D  175  1                                  15
HELIX    9   9 GLU D  220  LYS D  223  5                                   4
HELIX   10  10 ASN E   52  SER E   56  5                                   5
HELIX   11  11 PRO E   60  ASN E   83  1                                  24
HELIX   12  12 VAL E  138  THR E  142  5                                   5
HELIX   13  13 LEU E  147  MET E  161  1                                  15
HELIX   14  14 MET E  161  LYS E  175  1                                  15
HELIX   15  15 GLU E  220  LYS E  223  5                                   4
HELIX   16  16 ASN F   52  SER F   56  5                                   5
HELIX   17  17 PRO F   60  ASN F   83  1                                  24
HELIX   18  18 VAL F  138  THR F  142  5                                   5
HELIX   19  19 LEU F  147  MET F  161  1                                  15
HELIX   20  20 MET F  161  LYS F  175  1                                  15
HELIX   21  21 GLU F  220  LYS F  223  5                                   4
HELIX   22  22 ARG G  138  LEU G  142  5                                   5
HELIX   23  23 ARG H  138  LEU H  142  5                                   5
HELIX   24  24 ARG I  138  LEU I  142  5                                   5
HELIX   25  25 ASN J   52  SER J   56  5                                   5
HELIX   26  26 PRO J   60  ASN J   83  1                                  24
HELIX   27  27 VAL J  138  THR J  142  5                                   5
HELIX   28  28 LEU J  147  MET J  161  1                                  15
HELIX   29  29 MET J  161  LYS J  175  1                                  15
HELIX   30  30 GLU J  220  LYS J  223  5                                   4
HELIX   31  31 ASN K   52  SER K   56  5                                   5
HELIX   32  32 PRO K   60  ASN K   83  1                                  24
HELIX   33  33 VAL K  138  THR K  142  5                                   5
HELIX   34  34 LEU K  147  MET K  161  1                                  15
HELIX   35  35 MET K  161  LYS K  175  1                                  15
HELIX   36  36 GLU K  220  LYS K  223  5                                   4
HELIX   37  37 ASN L   52  SER L   56  5                                   5
HELIX   38  38 PRO L   60  ASN L   83  1                                  24
HELIX   39  39 VAL L  138  THR L  142  5                                   5
HELIX   40  40 LEU L  147  MET L  161  1                                  15
HELIX   41  41 MET L  161  LYS L  175  1                                  15
HELIX   42  42 GLU L  220  LYS L  223  5                                   4
SHEET    1   A 3 TRP A  28  LEU A  29  0
SHEET    2   A 3 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29
SHEET    3   A 3 LEU A  36  ALA A  38 -1  O  LEU A  36   N  HIS A  15
SHEET    1   B 5 TRP A  28  LEU A  29  0
SHEET    2   B 5 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29
SHEET    3   B 5 TYR A 151  ALA A 156 -1  O  PHE A 152   N  VAL A  16
SHEET    4   B 5 GLY A  54  GLN A  67 -1  N  LEU A  57   O  ILE A 155
SHEET    5   B 5 PRO A 113  LEU A 126 -1  O  LEU A 126   N  GLY A  54
SHEET    1   C 5 GLU A  42  ARG A  44  0
SHEET    2   C 5 GLN A  47  VAL A  49 -1  O  GLN A  47   N  ARG A  44
SHEET    3   C 5 ARG A 131  ILE A 136 -1  O  LEU A 132   N  LEU A  48
SHEET    4   C 5 LEU A  76  ALA A  84 -1  N  THR A  79   O  GLU A 135
SHEET    5   C 5 TYR A  87  LYS A  98 -1  O  LEU A  93   N  ILE A  80
SHEET    1   D 3 TRP B  28  LEU B  29  0
SHEET    2   D 3 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29
SHEET    3   D 3 LEU B  36  ALA B  38 -1  O  LEU B  36   N  HIS B  15
SHEET    1   E 5 TRP B  28  LEU B  29  0
SHEET    2   E 5 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29
SHEET    3   E 5 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16
SHEET    4   E 5 GLY B  54  GLN B  67 -1  N  TYR B  59   O  GLY B 153
SHEET    5   E 5 PRO B 113  LEU B 126 -1  O  LEU B 126   N  GLY B  54
SHEET    1   F 5 GLU B  42  ARG B  44  0
SHEET    2   F 5 GLN B  47  VAL B  49 -1  O  GLN B  47   N  ARG B  44
SHEET    3   F 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48
SHEET    4   F 5 LEU B  76  ALA B  84 -1  N  THR B  79   O  GLU B 135
SHEET    5   F 5 TYR B  87  LYS B  98 -1  O  LEU B  93   N  ILE B  80
SHEET    1   G 3 TRP C  28  LEU C  29  0
SHEET    2   G 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29
SHEET    3   G 3 LEU C  36  ALA C  38 -1  O  LEU C  36   N  HIS C  15
SHEET    1   H 5 TRP C  28  LEU C  29  0
SHEET    2   H 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29
SHEET    3   H 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16
SHEET    4   H 5 GLY C  54  GLN C  67 -1  N  LEU C  57   O  ILE C 155
SHEET    5   H 5 PRO C 113  LEU C 126 -1  O  LEU C 126   N  GLY C  54
SHEET    1   I 5 GLU C  42  ARG C  44  0
SHEET    2   I 5 GLN C  47  VAL C  49 -1  O  GLN C  47   N  ARG C  44
SHEET    3   I 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48
SHEET    4   I 5 LEU C  76  ALA C  84 -1  N  SER C  81   O  SER C 133
SHEET    5   I 5 TYR C  87  LYS C  98 -1  O  LEU C  93   N  ILE C  80
SHEET    1   J 8 HIS D  41  ARG D  47  0
SHEET    2   J 8 GLN D  28  ASN D  36 -1  N  ASN D  36   O  HIS D  41
SHEET    3   J 8 ASP D  18  TYR D  25 -1  N  ASP D  23   O  VAL D  30
SHEET    4   J 8 THR D   2  THR D  10 -1  N  THR D   8   O  VAL D  20
SHEET    5   J 8 SER D  90  THR D 100 -1  O  THR D  95   N  TYR D   5
SHEET    6   J 8 LEU D 103  THR D 112 -1  O  TYR D 109   N  ILE D  94
SHEET    7   J 8 GLY D 115  HIS D 121 -1  O  ALA D 118   N  VAL D 110
SHEET    8   J 8 ARG D 126  LYS D 129 -1  O  THR D 128   N  ARG D 119
SHEET    1   K 4 THR D 185  THR D 189  0
SHEET    2   K 4 MET D 198  PHE D 207 -1  O  ASN D 205   N  THR D 185
SHEET    3   K 4 TYR D 263  THR D 271 -1  O  ASP D 267   N  CYS D 202
SHEET    4   K 4 ILE D 254  LYS D 255 -1  N  LYS D 255   O  SER D 264
SHEET    1   L 3 ILE D 213  GLU D 218  0
SHEET    2   L 3 PRO D 279  PHE D 284 -1  O  PHE D 284   N  ILE D 213
SHEET    3   L 3 GLN D 291  TYR D 293 -1  O  TYR D 293   N  CYS D 281
SHEET    1   M 8 HIS E  41  ARG E  47  0
SHEET    2   M 8 GLN E  28  ASN E  36 -1  N  LYS E  32   O  ASN E  45
SHEET    3   M 8 ASP E  18  TYR E  25 -1  N  ASP E  23   O  VAL E  30
SHEET    4   M 8 THR E   2  THR E  10 -1  N  THR E   8   O  VAL E  20
SHEET    5   M 8 SER E  90  THR E 100 -1  O  THR E  95   N  TYR E   5
SHEET    6   M 8 LEU E 103  THR E 112 -1  O  TYR E 109   N  ILE E  94
SHEET    7   M 8 GLY E 115  HIS E 121 -1  O  ALA E 118   N  VAL E 110
SHEET    8   M 8 ARG E 126  LYS E 129 -1  O  THR E 128   N  ARG E 119
SHEET    1   N 4 THR E 185  THR E 189  0
SHEET    2   N 4 MET E 198  PHE E 207 -1  O  ASN E 205   N  THR E 185
SHEET    3   N 4 TYR E 263  THR E 271 -1  O  ASP E 267   N  CYS E 202
SHEET    4   N 4 ILE E 254  LYS E 255 -1  N  LYS E 255   O  SER E 264
SHEET    1   O 3 ILE E 213  GLU E 218  0
SHEET    2   O 3 PRO E 279  PHE E 284 -1  O  PHE E 284   N  ILE E 213
SHEET    3   O 3 GLN E 291  TYR E 293 -1  O  TYR E 293   N  CYS E 281
SHEET    1   P 8 HIS F  41  ARG F  47  0
SHEET    2   P 8 GLN F  28  ASN F  36 -1  N  ASN F  36   O  HIS F  41
SHEET    3   P 8 ASP F  18  TYR F  25 -1  N  ASP F  23   O  VAL F  30
SHEET    4   P 8 THR F   2  THR F  10 -1  N  THR F   8   O  VAL F  20
SHEET    5   P 8 SER F  90  THR F 100 -1  O  THR F  95   N  TYR F   5
SHEET    6   P 8 LEU F 103  THR F 112 -1  O  TYR F 109   N  ILE F  94
SHEET    7   P 8 GLY F 115  HIS F 121 -1  O  ALA F 118   N  VAL F 110
SHEET    8   P 8 ARG F 126  LYS F 129 -1  O  THR F 128   N  ARG F 119
SHEET    1   Q 4 THR F 185  THR F 189  0
SHEET    2   Q 4 MET F 198  PHE F 207 -1  O  ASN F 205   N  THR F 185
SHEET    3   Q 4 TYR F 263  THR F 271 -1  O  ASP F 267   N  CYS F 202
SHEET    4   Q 4 ILE F 254  LYS F 255 -1  N  LYS F 255   O  SER F 264
SHEET    1   R 3 ILE F 213  GLU F 218  0
SHEET    2   R 3 PRO F 279  PHE F 284 -1  O  PHE F 284   N  ILE F 213
SHEET    3   R 3 GLN F 291  TYR F 293 -1  O  TYR F 293   N  CYS F 281
SHEET    1   S 3 TRP G  28  LEU G  29  0
SHEET    2   S 3 VAL G  13  ALA G  18 -1  N  VAL G  17   O  LEU G  29
SHEET    3   S 3 LEU G  36  ALA G  38 -1  O  LEU G  36   N  HIS G  15
SHEET    1   T 5 TRP G  28  LEU G  29  0
SHEET    2   T 5 VAL G  13  ALA G  18 -1  N  VAL G  17   O  LEU G  29
SHEET    3   T 5 TYR G 151  ALA G 156 -1  O  PHE G 152   N  VAL G  16
SHEET    4   T 5 GLY G  54  GLN G  67 -1  N  TYR G  59   O  GLY G 153
SHEET    5   T 5 PRO G 113  LEU G 126 -1  O  LEU G 126   N  GLY G  54
SHEET    1   U 5 GLU G  42  ARG G  44  0
SHEET    2   U 5 GLN G  47  VAL G  49 -1  O  GLN G  47   N  ARG G  44
SHEET    3   U 5 ARG G 131  ILE G 136 -1  O  LEU G 132   N  LEU G  48
SHEET    4   U 5 LEU G  76  ALA G  84 -1  N  THR G  79   O  GLU G 135
SHEET    5   U 5 TYR G  87  LYS G  98 -1  O  LEU G  93   N  ILE G  80
SHEET    1   V 3 TRP H  28  LEU H  29  0
SHEET    2   V 3 VAL H  13  ALA H  18 -1  N  VAL H  17   O  LEU H  29
SHEET    3   V 3 LEU H  36  ALA H  38 -1  O  LEU H  36   N  HIS H  15
SHEET    1   W 5 TRP H  28  LEU H  29  0
SHEET    2   W 5 VAL H  13  ALA H  18 -1  N  VAL H  17   O  LEU H  29
SHEET    3   W 5 TYR H 151  ALA H 156 -1  O  PHE H 152   N  VAL H  16
SHEET    4   W 5 GLY H  54  GLN H  67 -1  N  TYR H  59   O  GLY H 153
SHEET    5   W 5 PRO H 113  LEU H 126 -1  O  LEU H 126   N  GLY H  54
SHEET    1   X 5 GLU H  42  ARG H  44  0
SHEET    2   X 5 GLN H  47  VAL H  49 -1  O  GLN H  47   N  ARG H  44
SHEET    3   X 5 ARG H 131  ILE H 136 -1  O  LEU H 132   N  LEU H  48
SHEET    4   X 5 LEU H  76  ALA H  84 -1  N  THR H  79   O  GLU H 135
SHEET    5   X 5 TYR H  87  LYS H  98 -1  O  LEU H  93   N  ILE H  80
SHEET    1   Y 3 TRP I  28  LEU I  29  0
SHEET    2   Y 3 VAL I  13  ALA I  18 -1  N  VAL I  17   O  LEU I  29
SHEET    3   Y 3 LEU I  36  ALA I  38 -1  O  LEU I  36   N  HIS I  15
SHEET    1   Z 5 TRP I  28  LEU I  29  0
SHEET    2   Z 5 VAL I  13  ALA I  18 -1  N  VAL I  17   O  LEU I  29
SHEET    3   Z 5 TYR I 151  ALA I 156 -1  O  PHE I 152   N  VAL I  16
SHEET    4   Z 5 GLY I  54  GLN I  67 -1  N  LEU I  57   O  ILE I 155
SHEET    5   Z 5 PRO I 113  LEU I 126 -1  O  LEU I 126   N  GLY I  54
SHEET    1  AA 5 GLU I  42  ARG I  44  0
SHEET    2  AA 5 GLN I  47  VAL I  49 -1  O  GLN I  47   N  ARG I  44
SHEET    3  AA 5 ARG I 131  ILE I 136 -1  O  LEU I 132   N  LEU I  48
SHEET    4  AA 5 LEU I  76  ALA I  84 -1  N  SER I  81   O  SER I 133
SHEET    5  AA 5 TYR I  87  LYS I  98 -1  O  LEU I  93   N  ILE I  80
SHEET    1  AB 8 HIS J  41  ARG J  47  0
SHEET    2  AB 8 GLN J  28  ASN J  36 -1  N  LYS J  32   O  ASN J  45
SHEET    3  AB 8 ASP J  18  TYR J  25 -1  N  ASP J  23   O  VAL J  30
SHEET    4  AB 8 THR J   2  THR J  10 -1  N  THR J   8   O  VAL J  20
SHEET    5  AB 8 SER J  90  THR J 100 -1  O  THR J  95   N  TYR J   5
SHEET    6  AB 8 LEU J 103  THR J 112 -1  O  TYR J 109   N  ILE J  94
SHEET    7  AB 8 GLY J 115  HIS J 121 -1  O  ALA J 118   N  VAL J 110
SHEET    8  AB 8 ARG J 126  LYS J 129 -1  O  THR J 128   N  ARG J 119
SHEET    1  AC 4 THR J 185  THR J 189  0
SHEET    2  AC 4 MET J 198  PHE J 207 -1  O  ASN J 205   N  THR J 185
SHEET    3  AC 4 TYR J 263  THR J 271 -1  O  ASP J 267   N  CYS J 202
SHEET    4  AC 4 ILE J 254  LYS J 256 -1  N  LYS J 255   O  SER J 264
SHEET    1  AD 3 ILE J 213  GLU J 218  0
SHEET    2  AD 3 PRO J 279  PHE J 284 -1  O  PHE J 284   N  ILE J 213
SHEET    3  AD 3 GLN J 291  TYR J 293 -1  O  TYR J 293   N  CYS J 281
SHEET    1  AE 8 HIS K  41  ARG K  47  0
SHEET    2  AE 8 GLN K  28  ASN K  36 -1  N  ASN K  36   O  HIS K  41
SHEET    3  AE 8 ASP K  18  TYR K  25 -1  N  ASP K  23   O  VAL K  30
SHEET    4  AE 8 THR K   2  THR K  10 -1  N  THR K   8   O  VAL K  20
SHEET    5  AE 8 SER K  90  THR K 100 -1  O  THR K  95   N  TYR K   5
SHEET    6  AE 8 LEU K 103  THR K 112 -1  O  TYR K 109   N  ILE K  94
SHEET    7  AE 8 GLY K 115  HIS K 121 -1  O  ALA K 118   N  VAL K 110
SHEET    8  AE 8 ARG K 126  LYS K 129 -1  O  THR K 128   N  ARG K 119
SHEET    1  AF 4 THR K 185  THR K 189  0
SHEET    2  AF 4 MET K 198  PHE K 207 -1  O  ASN K 205   N  THR K 185
SHEET    3  AF 4 TYR K 263  THR K 271 -1  O  ASP K 267   N  CYS K 202
SHEET    4  AF 4 ILE K 254  LYS K 255 -1  N  LYS K 255   O  SER K 264
SHEET    1  AG 3 ILE K 213  GLU K 218  0
SHEET    2  AG 3 PRO K 279  PHE K 284 -1  O  PHE K 284   N  ILE K 213
SHEET    3  AG 3 GLN K 291  TYR K 293 -1  O  TYR K 293   N  CYS K 281
SHEET    1  AH 8 HIS L  41  ARG L  47  0
SHEET    2  AH 8 GLN L  28  ASN L  36 -1  N  LYS L  32   O  ASN L  45
SHEET    3  AH 8 ASP L  18  TYR L  25 -1  N  ASP L  23   O  VAL L  30
SHEET    4  AH 8 THR L   2  THR L  10 -1  N  THR L   8   O  VAL L  20
SHEET    5  AH 8 SER L  90  THR L 100 -1  O  THR L  95   N  TYR L   5
SHEET    6  AH 8 LEU L 103  THR L 112 -1  O  TYR L 109   N  ILE L  94
SHEET    7  AH 8 GLY L 115  HIS L 121 -1  O  ALA L 118   N  VAL L 110
SHEET    8  AH 8 ARG L 126  LYS L 129 -1  O  THR L 128   N  ARG L 119
SHEET    1  AI 4 THR L 185  THR L 189  0
SHEET    2  AI 4 MET L 198  PHE L 207 -1  O  ASN L 205   N  THR L 185
SHEET    3  AI 4 TYR L 263  THR L 271 -1  O  ASP L 267   N  CYS L 202
SHEET    4  AI 4 ILE L 254  LYS L 255 -1  N  LYS L 255   O  SER L 264
SHEET    1  AJ 3 ILE L 213  GLU L 218  0
SHEET    2  AJ 3 PRO L 279  PHE L 284 -1  O  PHE L 284   N  ILE L 213
SHEET    3  AJ 3 GLN L 291  TYR L 293 -1  O  TYR L 293   N  CYS L 281
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.03
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.03
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.03
SSBOND   4 CYS D  202    CYS D  281                          1555   1555  2.04
SSBOND   5 CYS D  295    CYS D  299                          1555   1555  2.02
SSBOND   6 CYS E  202    CYS E  281                          1555   1555  2.04
SSBOND   7 CYS E  295    CYS E  299                          1555   1555  2.02
SSBOND   8 CYS F  202    CYS F  281                          1555   1555  2.04
SSBOND   9 CYS F  295    CYS F  299                          1555   1555  2.03
SSBOND  10 CYS G   69    CYS G  101                          1555   1555  2.03
SSBOND  11 CYS H   69    CYS H  101                          1555   1555  2.03
SSBOND  12 CYS I   69    CYS I  101                          1555   1555  2.03
SSBOND  13 CYS J  202    CYS J  281                          1555   1555  2.05
SSBOND  14 CYS J  295    CYS J  299                          1555   1555  2.01
SSBOND  15 CYS K  202    CYS K  281                          1555   1555  2.05
SSBOND  16 CYS K  295    CYS K  299                          1555   1555  2.02
SSBOND  17 CYS L  202    CYS L  281                          1555   1555  2.04
SSBOND  18 CYS L  295    CYS L  299                          1555   1555  2.03
LINK         ND2 ASN D   6                 C1  NAG D 325     1555   1555  1.46
LINK         ND2 ASN D  52                 C1  NAG D 326     1555   1555  1.46
LINK         ND2 ASN D  83                 C1  NAG D 327     1555   1555  1.46
LINK         ND2 ASN E   6                 C1  NAG E 325     1555   1555  1.45
LINK         ND2 ASN E  52                 C1  NAG E 326     1555   1555  1.46
LINK         ND2 ASN E  83                 C1  NAG E 327     1555   1555  1.46
LINK         ND2 ASN F   6                 C1  NAG F 325     1555   1555  1.46
LINK         ND2 ASN F  52                 C1  NAG F 326     1555   1555  1.46
LINK         ND2 ASN F  83                 C1  NAG F 327     1555   1555  1.46
LINK         ND2 ASN J   6                 C1  NAG J 325     1555   1555  1.45
LINK         ND2 ASN J  52                 C1  NAG J 326     1555   1555  1.45
LINK         ND2 ASN J  83                 C1  NAG J 327     1555   1555  1.45
LINK         ND2 ASN K   6                 C1  NAG K 325     1555   1555  1.46
LINK         ND2 ASN K  52                 C1  NAG K 326     1555   1555  1.45
LINK         ND2 ASN K  83                 C1  NAG K 327     1555   1555  1.46
LINK         ND2 ASN L   6                 C1  NAG L 325     1555   1555  1.45
LINK         ND2 ASN L  52                 C1  NAG L 326     1555   1555  1.46
LINK         ND2 ASN L  83                 C1  NAG L 327     1555   1555  1.46
SITE     1 AC1  5 LYS D   4  ASN D   6  THR D   8  TYR D  22
SITE     2 AC1  5 HOH D 328
SITE     1 AC2  3 ASN D  52  SER D  54  ARG D  55
SITE     1 AC3  1 ASN D  83
SITE     1 AC4  5 LYS E   4  ASN E   6  THR E   8  TYR E  22
SITE     2 AC4  5 ILE E  94
SITE     1 AC5  2 ASN E  52  ARG E  55
SITE     1 AC6  2 ASN E  83  SER E  85
SITE     1 AC7  6 LYS F   4  ASN F   6  THR F   8  TYR F  22
SITE     2 AC7  6 ILE F  94  GLU F 111
SITE     1 AC8  3 ASN F  52  SER F  54  ARG F  55
SITE     1 AC9  1 ASN F  83
SITE     1 BC1  5 LYS J   4  ASN J   6  THR J   8  TYR J  22
SITE     2 BC1  5 ILE J  94
SITE     1 BC2  4 PHE E  46  ARG E  47  ASN J  52  ARG J  55
SITE     1 BC3  1 ASN J  83
SITE     1 BC4  5 LYS K   4  ASN K   6  THR K   8  TYR K  22
SITE     2 BC4  5 ILE K  94
SITE     1 BC5  3 ASN K  52  SER K  54  ARG K  55
SITE     1 BC6  2 ASN K  83  SER K  85
SITE     1 BC7  5 LYS L   4  ASN L   6  THR L   8  TYR L  22
SITE     2 BC7  5 ILE L  94
SITE     1 BC8  3 ASN L  52  SER L  54  ARG L  55
SITE     1 BC9  2 TYR F 233  ASN L  83
CRYST1  101.656  170.295  122.002  90.00  92.04  90.00 P 1 21 1     12
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      0.009837  0.000000  0.000350        0.00000
SCALE2      0.000000  0.005872  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008202        0.00000
      
PROCHECK
Go to PROCHECK summary
 References