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PDBsum entry 3s4s

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Top Page protein ligands Protein-protein interface(s) links
Immune system PDB id
3s4s
Jmol
Contents
Protein chains
178 a.a.
186 a.a.
13 a.a.
176 a.a.
Ligands
GOL ×3
Waters ×68
HEADER    IMMUNE SYSTEM                           20-MAY-11   3S4S
TITLE     CRYSTAL STRUCTURE OF CD4 MUTANT BOUND TO HLA-DR1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND   3 CHAIN: A, D;
COMPND   4 FRAGMENT: UNP RESIDUES 26-207;
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND   9 CHAIN: B, E;
COMPND  10 FRAGMENT: UNP RESIDUES 30-221;
COMPND  11 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: HEMAGGLUTININ PEPTIDE;
COMPND  15 CHAIN: C, F;
COMPND  16 FRAGMENT: UNP RESIDUES 306-318;
COMPND  17 ENGINEERED: YES;
COMPND  18 MOL_ID: 4;
COMPND  19 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;
COMPND  20 CHAIN: G, H;
COMPND  21 FRAGMENT: UNP RESIDUES 26-203;
COMPND  22 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3;
COMPND  23 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DRA, HLA-DRA1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET26;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 GENE: HLA-DRB1;
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET26B;
SOURCE  21 MOL_ID: 3;
SOURCE  22 MOL_ID: 4;
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  24 ORGANISM_COMMON: HUMAN;
SOURCE  25 ORGANISM_TAXID: 9606;
SOURCE  26 GENE: CD4;
SOURCE  27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  28 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  30 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  31 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  32 EXPRESSION_SYSTEM_PLASMID: PACGP67-B
KEYWDS    PROTEIN-PROTEIN COMPLEX, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.LI
REVDAT   3   16-NOV-11 3S4S    1       JRNL
REVDAT   2   02-NOV-11 3S4S    1
REVDAT   1   21-SEP-11 3S4S    0
JRNL        AUTH   X.X.WANG,Y.LI,Y.YIN,M.MO,Q.WANG,W.GAO,L.WANG,R.A.MARIUZZA
JRNL        TITL   AFFINITY MATURATION OF HUMAN CD4 BY YEAST SURFACE DISPLAY
JRNL        TITL 2 AND CRYSTAL STRUCTURE OF A CD4-HLA-DR1 COMPLEX.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108 15960 2011
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   21900604
JRNL        DOI    10.1073/PNAS.1109438108
REMARK   2
REMARK   2 RESOLUTION.    2.40 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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 59805
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.251
REMARK   3   FREE R VALUE                     : 0.286
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3011
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8838
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 18
REMARK   3   SOLVENT ATOMS            : 68
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 17.86200
REMARK   3    B22 (A**2) : -16.46500
REMARK   3    B33 (A**2) : -1.39700
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -8.20900
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) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 46.25
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  : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER.PARAM
REMARK   3  PARAMETER FILE  3  : GOL.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3S4S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB065760.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X29A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.502
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60345
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
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     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 5.800
REMARK 200  R MERGE                    (I) : 0.11000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.59900
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, (NH4)SO4, PH 6.5, VAPOR
REMARK 280  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       68.64500
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G
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 APPLY THE FOLLOWING TO CHAINS: D, E, F, 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 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     ILE A     1
REMARK 465     LYS A     2
REMARK 465     ASP A   181
REMARK 465     ALA A   182
REMARK 465     LYS B   105
REMARK 465     THR B   106
REMARK 465     GLN B   107
REMARK 465     PRO B   108
REMARK 465     LEU B   109
REMARK 465     ARG B   191
REMARK 465     SER B   192
REMARK 465     ASP G    -3
REMARK 465     LEU G    -2
REMARK 465     GLY G    -1
REMARK 465     SER G     0
REMARK 465     ASP G   105
REMARK 465     THR G   106
REMARK 465     ALA G   179
REMARK 465     ALA G   180
REMARK 465     ALA G   181
REMARK 465     HIS G   182
REMARK 465     HIS G   183
REMARK 465     HIS G   184
REMARK 465     HIS G   185
REMARK 465     HIS G   186
REMARK 465     HIS G   187
REMARK 465     ASP D   181
REMARK 465     ALA D   182
REMARK 465     THR E   106
REMARK 465     GLN E   107
REMARK 465     PRO E   108
REMARK 465     LEU E   109
REMARK 465     GLN E   110
REMARK 465     HIS E   111
REMARK 465     ARG E   191
REMARK 465     SER E   192
REMARK 465     ASP H    -3
REMARK 465     LEU H    -2
REMARK 465     GLY H    -1
REMARK 465     SER H     0
REMARK 465     ASN H   103
REMARK 465     SER H   104
REMARK 465     ASP H   105
REMARK 465     ALA H   179
REMARK 465     ALA H   180
REMARK 465     ALA H   181
REMARK 465     HIS H   182
REMARK 465     HIS H   183
REMARK 465     HIS H   184
REMARK 465     HIS H   185
REMARK 465     HIS H   186
REMARK 465     HIS H   187
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     GLN B 110    CB   CG   CD   OE1  NE2
REMARK 470     HIS B 111    CB   CG   ND1  CD2  CE1  NE2
REMARK 470     HIS B 112    CB   CG   ND1  CD2  CE1  NE2
REMARK 470     ASN G 103    CG   OD1  ND2
REMARK 470     SER G 104    OG
REMARK 470     HIS G 107    CG   ND1  CD2  CE1  NE2
REMARK 470     LEU G 108    CG   CD1  CD2
REMARK 470     LEU G 109    CG   CD1  CD2
REMARK 470     LYS G 136    CG   CD   CE   NZ
REMARK 470     GLU G 150    CB   CG   CD   OE1  OE2
REMARK 470     ILE D   1    CB   CG1  CG2  CD1
REMARK 470     LYS D   2    CB   CG   CD   CE   NZ
REMARK 470     LYS E 105    CG   CD   CE   NZ
REMARK 470     HIS E 112    CG   ND1  CD2  CE1  NE2
REMARK 470     THR F  15    OG1  CG2
REMARK 470     THR H 101    OG1  CG2
REMARK 470     THR H 106    CB   OG1  CG2
REMARK 470     HIS H 107    CB   CG   ND1  CD2  CE1  NE2
REMARK 470     LEU H 108    CB   CG   CD1  CD2
REMARK 470     LYS H 136    CG   CD   CE   NZ
REMARK 470     LYS H 142    CG   CD   CE   NZ
REMARK 470     SER H 147    CB   OG
REMARK 470     GLN H 148    CB   CG   CD   OE1  NE2
REMARK 470     LEU H 149    CB   CG   CD1  CD2
REMARK 470     GLU H 150    CB   CG   CD   OE1  OE2
REMARK 470     LEU H 151    CB   CG   CD1  CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  78       40.72     70.97
REMARK 500    LEU A  99      132.74    -35.32
REMARK 500    PRO A 102      123.02    -36.24
REMARK 500    LYS A 111       71.67     35.20
REMARK 500    THR A 129       -3.19   -151.39
REMARK 500    ASP B   2       76.42     57.60
REMARK 500    ASN B  19       72.07     57.09
REMARK 500    ASN B  33     -103.77     60.83
REMARK 500    ASP B  76      -66.00   -104.72
REMARK 500    TYR B  78      -71.02   -109.36
REMARK 500    CYS B  79      -79.99    -56.37
REMARK 500    THR B  90      -79.69   -131.90
REMARK 500    HIS B 111      -83.66     76.29
REMARK 500    ASP G  10     -168.86    -78.44
REMARK 500    SER G  19      -77.29    -66.57
REMARK 500    ASN G  52     -128.25     34.30
REMARK 500    SER G  57     -167.37   -118.21
REMARK 500    ASP G  80      179.70    171.00
REMARK 500    GLU G  87       62.19     31.67
REMARK 500    GLN G 110      102.10    -57.42
REMARK 500    SER G 125       54.97   -141.72
REMARK 500    SER G 132      173.96    -45.84
REMARK 500    GLN G 148      112.34     57.13
REMARK 500    VAL G 175       69.42   -110.96
REMARK 500    LYS D   2     -109.71    176.94
REMARK 500    ALA D  37      -77.51    -61.81
REMARK 500    LYS D  38        5.07    -62.81
REMARK 500    LYS D  39       43.75     31.83
REMARK 500    GLU D  46      -73.90    -34.26
REMARK 500    ASN D 124       63.84     64.08
REMARK 500    THR D 129       -5.05   -145.78
REMARK 500    VAL D 136     -164.37    -79.34
REMARK 500    ASN E  33     -114.69     54.49
REMARK 500    TYR E  78      -70.77   -100.05
REMARK 500    CYS E  79      -73.74    -52.38
REMARK 500    THR E  90      -73.88   -127.55
REMARK 500    SER E 104     -141.54   -122.06
REMARK 500    PRO E 124     -175.24    -67.85
REMARK 500    ARG E 166      130.34   -173.13
REMARK 500    SER E 167      134.16    -30.51
REMARK 500    PRO E 178      -17.28    -45.64
REMARK 500    GLN H  33       -3.86     78.21
REMARK 500    ASN H  52     -137.85     39.99
REMARK 500    ASP H  53       44.76   -100.11
REMARK 500    ASP H  80      179.74    177.68
REMARK 500    ASP H  88      -19.82     73.66
REMARK 500    LYS H  90       69.57   -159.44
REMARK 500    HIS H 107       36.45   -165.40
REMARK 500    GLN H 110       90.37    -61.50
REMARK 500    PRO H 133       27.18    -65.64
REMARK 500
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.
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 GOL B 960
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 962
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 961
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S5L   RELATED DB: PDB
DBREF  3S4S A    1   182  UNP    P01903   DRA_HUMAN       26    207
DBREF  3S4S B    1   192  UNP    P04229   2B11_HUMAN      30    221
DBREF  3S4S C    3    15  UNP    Q9YS52   Q9YS52_9INFA   306    318
DBREF  3S4S G    1   178  UNP    P01730   CD4_HUMAN       26    203
DBREF  3S4S D    1   182  UNP    P01903   DRA_HUMAN       26    207
DBREF  3S4S E    1   192  UNP    P04229   2B11_HUMAN      30    221
DBREF  3S4S F    3    15  UNP    Q9YS52   Q9YS52_9INFA   306    318
DBREF  3S4S H    1   178  UNP    P01730   CD4_HUMAN       26    203
SEQADV 3S4S GLN A  177  UNP  P01903    HIS   202 CONFLICT
SEQADV 3S4S MET B    0  UNP  P04229              EXPRESSION TAG
SEQADV 3S4S ASP G   -3  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S LEU G   -2  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S GLY G   -1  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S SER G    0  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S TYR G   40  UNP  P01730    GLN    65 CONFLICT
SEQADV 3S4S TRP G   45  UNP  P01730    THR    70 CONFLICT
SEQADV 3S4S ALA G  179  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S ALA G  180  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S ALA G  181  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS G  182  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS G  183  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS G  184  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS G  185  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS G  186  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS G  187  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S GLN D  177  UNP  P01903    HIS   202 CONFLICT
SEQADV 3S4S MET E    0  UNP  P04229              EXPRESSION TAG
SEQADV 3S4S ASP H   -3  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S LEU H   -2  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S GLY H   -1  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S SER H    0  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S TYR H   40  UNP  P01730    GLN    65 CONFLICT
SEQADV 3S4S TRP H   45  UNP  P01730    THR    70 CONFLICT
SEQADV 3S4S ALA H  179  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S ALA H  180  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S ALA H  181  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS H  182  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS H  183  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS H  184  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS H  185  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS H  186  UNP  P01730              EXPRESSION TAG
SEQADV 3S4S HIS H  187  UNP  P01730              EXPRESSION TAG
SEQRES   1 A  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 A  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 A  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 A  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 A  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 A  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 A  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 A  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 A  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 A  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 A  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 A  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 A  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 A  182  LEU ASP GLU PRO LEU LEU LYS GLN TRP GLU PHE ASP ALA
SEQRES   1 B  193  MET GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS
SEQRES   2 B  193  PHE GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG
SEQRES   3 B  193  LEU LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL
SEQRES   4 B  193  ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR
SEQRES   5 B  193  GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN
SEQRES   6 B  193  LYS ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR
SEQRES   7 B  193  TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR
SEQRES   8 B  193  VAL GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO
SEQRES   9 B  193  SER LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL
SEQRES  10 B  193  CYS SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL
SEQRES  11 B  193  ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL
SEQRES  12 B  193  VAL SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE
SEQRES  13 B  193  GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY
SEQRES  14 B  193  GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR
SEQRES  15 B  193  SER PRO LEU THR VAL GLU TRP ARG ALA ARG SER
SEQRES   1 C   13  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES   1 G  191  ASP LEU GLY SER LYS LYS VAL VAL LEU GLY LYS LYS GLY
SEQRES   2 G  191  ASP THR VAL GLU LEU THR CYS THR ALA SER GLN LYS LYS
SEQRES   3 G  191  SER ILE GLN PHE HIS TRP LYS ASN SER ASN GLN ILE LYS
SEQRES   4 G  191  ILE LEU GLY ASN TYR GLY SER PHE LEU TRP LYS GLY PRO
SEQRES   5 G  191  SER LYS LEU ASN ASP ARG ALA ASP SER ARG ARG SER LEU
SEQRES   6 G  191  TRP ASP GLN GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU
SEQRES   7 G  191  LYS ILE GLU ASP SER ASP THR TYR ILE CYS GLU VAL GLU
SEQRES   8 G  191  ASP GLN LYS GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU
SEQRES   9 G  191  THR ALA ASN SER ASP THR HIS LEU LEU GLN GLY GLN SER
SEQRES  10 G  191  LEU THR LEU THR LEU GLU SER PRO PRO GLY SER SER PRO
SEQRES  11 G  191  SER VAL GLN CYS ARG SER PRO ARG GLY LYS ASN ILE GLN
SEQRES  12 G  191  GLY GLY LYS THR LEU SER VAL SER GLN LEU GLU LEU GLN
SEQRES  13 G  191  ASP SER GLY THR TRP THR CYS THR VAL LEU GLN ASN GLN
SEQRES  14 G  191  LYS LYS VAL GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA
SEQRES  15 G  191  ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES   1 D  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 D  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 D  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 D  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 D  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 D  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 D  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 D  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 D  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 D  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 D  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 D  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 D  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 D  182  LEU ASP GLU PRO LEU LEU LYS GLN TRP GLU PHE ASP ALA
SEQRES   1 E  193  MET GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS
SEQRES   2 E  193  PHE GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG
SEQRES   3 E  193  LEU LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL
SEQRES   4 E  193  ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR
SEQRES   5 E  193  GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN
SEQRES   6 E  193  LYS ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR
SEQRES   7 E  193  TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR
SEQRES   8 E  193  VAL GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO
SEQRES   9 E  193  SER LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL
SEQRES  10 E  193  CYS SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL
SEQRES  11 E  193  ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL
SEQRES  12 E  193  VAL SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE
SEQRES  13 E  193  GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY
SEQRES  14 E  193  GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR
SEQRES  15 E  193  SER PRO LEU THR VAL GLU TRP ARG ALA ARG SER
SEQRES   1 F   13  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES   1 H  191  ASP LEU GLY SER LYS LYS VAL VAL LEU GLY LYS LYS GLY
SEQRES   2 H  191  ASP THR VAL GLU LEU THR CYS THR ALA SER GLN LYS LYS
SEQRES   3 H  191  SER ILE GLN PHE HIS TRP LYS ASN SER ASN GLN ILE LYS
SEQRES   4 H  191  ILE LEU GLY ASN TYR GLY SER PHE LEU TRP LYS GLY PRO
SEQRES   5 H  191  SER LYS LEU ASN ASP ARG ALA ASP SER ARG ARG SER LEU
SEQRES   6 H  191  TRP ASP GLN GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU
SEQRES   7 H  191  LYS ILE GLU ASP SER ASP THR TYR ILE CYS GLU VAL GLU
SEQRES   8 H  191  ASP GLN LYS GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU
SEQRES   9 H  191  THR ALA ASN SER ASP THR HIS LEU LEU GLN GLY GLN SER
SEQRES  10 H  191  LEU THR LEU THR LEU GLU SER PRO PRO GLY SER SER PRO
SEQRES  11 H  191  SER VAL GLN CYS ARG SER PRO ARG GLY LYS ASN ILE GLN
SEQRES  12 H  191  GLY GLY LYS THR LEU SER VAL SER GLN LEU GLU LEU GLN
SEQRES  13 H  191  ASP SER GLY THR TRP THR CYS THR VAL LEU GLN ASN GLN
SEQRES  14 H  191  LYS LYS VAL GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA
SEQRES  15 H  191  ALA ALA ALA HIS HIS HIS HIS HIS HIS
HET    GOL  B 960       6
HET    GOL  D 962       6
HET    GOL  E 961       6
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   9  GOL    3(C3 H8 O3)
FORMUL  12  HOH   *68(H2 O)
HELIX    1   1 LEU A   45  PHE A   51  5                                   7
HELIX    2   2 ALA A   56  SER A   77  1                                  22
HELIX    3   3 GLY B   54  SER B   63  1                                  10
HELIX    4   4 GLN B   64  TYR B   78  1                                  15
HELIX    5   5 TYR B   78  GLU B   87  1                                  10
HELIX    6   6 SER B   88  THR B   90  5                                   3
HELIX    7   7 ARG G   58  GLY G   65  5                                   8
HELIX    8   8 LYS G   75  SER G   79  5                                   5
HELIX    9   9 GLU G  150  SER G  154  5                                   5
HELIX   10  10 LEU D   45  PHE D   51  5                                   7
HELIX   11  11 GLU D   55  SER D   77  1                                  23
HELIX   12  12 THR E   51  LEU E   53  5                                   3
HELIX   13  13 GLY E   54  SER E   63  1                                  10
HELIX   14  14 GLN E   64  ALA E   73  1                                  10
HELIX   15  15 ALA E   73  TYR E   78  1                                   6
HELIX   16  16 TYR E   78  GLU E   87  1                                  10
HELIX   17  17 ARG H   59  ASP H   63  5                                   5
HELIX   18  18 LYS H   75  SER H   79  5                                   5
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  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  ALA A  10   O  MET A  23
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  CYS B  15   N  ILE A   7
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  LEU B  27   N  GLU B  14
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  SER B  37   N  CYS B  30
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  LEU A 151   N  LEU A 105
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  LEU A 151   N  LEU A 105
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  PRO A 127  0
SHEET    2   D 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126
SHEET    3   D 4 VAL A 160  GLU A 166 -1  O  ASP A 162   N  LEU A 122
SHEET    4   D 4 LEU A 174  GLU A 179 -1  O  LEU A 174   N  VAL A 165
SHEET    1   E 4 LYS B  98  PRO B 103  0
SHEET    2   E 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3   E 4 PHE B 155  THR B 163 -1  O  LEU B 161   N  LEU B 115
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   F 4 LYS B  98  PRO B 103  0
SHEET    2   F 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3   F 4 PHE B 155  THR B 163 -1  O  LEU B 161   N  LEU B 115
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 6 LYS G   2  LYS G   7  0
SHEET    2   H 6 GLN G  89  ALA G 102  1  O  GLN G  94   N  VAL G   4
SHEET    3   H 6 ASP G  80  VAL G  86 -1  N  ASP G  80   O  LEU G  95
SHEET    4   H 6 PHE G  26  ASN G  30 -1  N  LYS G  29   O  ILE G  83
SHEET    5   H 6 LYS G  35  TYR G  40 -1  O  ILE G  36   N  TRP G  28
SHEET    6   H 6 PHE G  43  LYS G  46 -1  O  TRP G  45   N  GLY G  38
SHEET    1   I 4 LYS G   2  LYS G   7  0
SHEET    2   I 4 GLN G  89  ALA G 102  1  O  GLN G  94   N  VAL G   4
SHEET    3   I 4 LEU G 114  GLU G 119 -1  O  GLU G 119   N  GLY G  99
SHEET    4   I 4 THR G 143  VAL G 146 -1  O  VAL G 146   N  LEU G 114
SHEET    1   J 3 VAL G  12  LEU G  14  0
SHEET    2   J 3 LEU G  69  ILE G  71 -1  O  LEU G  69   N  LEU G  14
SHEET    3   J 3 ALA G  55  ASP G  56 -1  N  ASP G  56   O  ILE G  70
SHEET    1   K 3 VAL G 128  GLN G 129  0
SHEET    2   K 3 GLY G 155  GLN G 163 -1  O  THR G 160   N  GLN G 129
SHEET    3   K 3 LYS G 166  ILE G 174 -1  O  ILE G 172   N  TRP G 157
SHEET    1   L 8 GLU D  40  TRP D  43  0
SHEET    2   L 8 ASP D  29  ASP D  35 -1  N  HIS D  33   O  VAL D  42
SHEET    3   L 8 SER D  19  PHE D  26 -1  N  PHE D  26   O  ASP D  29
SHEET    4   L 8 HIS D   5  ASN D  15 -1  N  ALA D  10   O  MET D  23
SHEET    5   L 8 PHE E   7  PHE E  18 -1  O  CYS E  15   N  ILE D   7
SHEET    6   L 8 ARG E  23  TYR E  32 -1  O  LEU E  27   N  GLU E  14
SHEET    7   L 8 GLU E  35  ASP E  41 -1  O  SER E  37   N  CYS E  30
SHEET    8   L 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39
SHEET    1   M 4 GLU D  88  THR D  93  0
SHEET    2   M 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   M 4 PHE D 145  PHE D 153 -1  O  PHE D 153   N  ASN D 103
SHEET    4   M 4 SER D 133  GLU D 134 -1  N  SER D 133   O  TYR D 150
SHEET    1   N 4 GLU D  88  THR D  93  0
SHEET    2   N 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   N 4 PHE D 145  PHE D 153 -1  O  PHE D 153   N  ASN D 103
SHEET    4   N 4 LEU D 138  PRO D 139 -1  N  LEU D 138   O  ARG D 146
SHEET    1   O 4 LYS D 126  VAL D 128  0
SHEET    2   O 4 ASN D 118  ARG D 123 -1  N  ARG D 123   O  LYS D 126
SHEET    3   O 4 VAL D 160  GLU D 166 -1  O  ASP D 162   N  LEU D 122
SHEET    4   O 4 LEU D 174  GLU D 179 -1  O  LEU D 174   N  VAL D 165
SHEET    1   P 4 LYS E  98  PRO E 103  0
SHEET    2   P 4 LEU E 114  PHE E 122 -1  O  VAL E 116   N  TYR E 102
SHEET    3   P 4 PHE E 155  GLU E 162 -1  O  LEU E 161   N  LEU E 115
SHEET    4   P 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160
SHEET    1   Q 4 LYS E  98  PRO E 103  0
SHEET    2   Q 4 LEU E 114  PHE E 122 -1  O  VAL E 116   N  TYR E 102
SHEET    3   Q 4 PHE E 155  GLU E 162 -1  O  LEU E 161   N  LEU E 115
SHEET    4   Q 4 ILE E 148  GLN E 149 -1  N  ILE E 148   O  GLN E 156
SHEET    1   R 4 GLN E 136  GLU E 138  0
SHEET    2   R 4 GLU E 128  ARG E 133 -1  N  TRP E 131   O  GLU E 138
SHEET    3   R 4 VAL E 170  GLU E 176 -1  O  GLN E 174   N  ARG E 130
SHEET    4   R 4 LEU E 184  ARG E 189 -1  O  LEU E 184   N  VAL E 175
SHEET    1   S 6 VAL H   3  LYS H   7  0
SHEET    2   S 6 GLU H  91  LEU H 100  1  O  GLN H  94   N  VAL H   4
SHEET    3   S 6 ASP H  80  VAL H  86 -1  N  ASP H  80   O  LEU H  95
SHEET    4   S 6 PHE H  26  LYS H  29 -1  N  LYS H  29   O  ILE H  83
SHEET    5   S 6 LYS H  35  TYR H  40 -1  O  LEU H  37   N  TRP H  28
SHEET    6   S 6 PHE H  43  LYS H  46 -1  O  TRP H  45   N  GLY H  38
SHEET    1   T 4 VAL H   3  LYS H   7  0
SHEET    2   T 4 GLU H  91  LEU H 100  1  O  GLN H  94   N  VAL H   4
SHEET    3   T 4 SER H 113  GLU H 119 -1  O  GLU H 119   N  GLY H  99
SHEET    4   T 4 THR H 143  SER H 147 -1  O  LEU H 144   N  LEU H 116
SHEET    1   U 3 VAL H  12  LEU H  14  0
SHEET    2   U 3 LEU H  69  ILE H  71 -1  O  LEU H  69   N  LEU H  14
SHEET    3   U 3 ALA H  55  ASP H  56 -1  N  ASP H  56   O  ILE H  70
SHEET    1   V 2 LEU H 108  LEU H 109  0
SHEET    2   V 2 VAL H 176  LEU H 177  1  O  LEU H 177   N  LEU H 108
SHEET    1   W 2 GLN H 129  ARG H 131  0
SHEET    2   W 2 ASN H 137  GLN H 139 -1  O  ILE H 138   N  CYS H 130
SHEET    1   X 2 GLY H 155  GLN H 163  0
SHEET    2   X 2 LYS H 166  ILE H 174 -1  O  ILE H 172   N  TRP H 157
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.04
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.06
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03
SSBOND   4 CYS G   16    CYS G   84                          1555   1555  2.04
SSBOND   5 CYS G  130    CYS G  159                          1555   1555  2.03
SSBOND   6 CYS D  107    CYS D  163                          1555   1555  2.04
SSBOND   7 CYS E   15    CYS E   79                          1555   1555  2.05
SSBOND   8 CYS E  117    CYS E  173                          1555   1555  2.03
SSBOND   9 CYS H   16    CYS H   84                          1555   1555  2.04
SSBOND  10 CYS H  130    CYS H  159                          1555   1555  2.03
CISPEP   1 ASN A   15    PRO A   16          0         0.13
CISPEP   2 THR A  113    PRO A  114          0        -0.08
CISPEP   3 TYR B  123    PRO B  124          0        -0.13
CISPEP   4 ASN D   15    PRO D   16          0        -0.01
CISPEP   5 THR D  113    PRO D  114          0         0.33
CISPEP   6 TYR E  123    PRO E  124          0         0.30
SITE     1 AC1  2 ARG B  25  ARG B  39
SITE     1 AC2  5 ARG D  44  VAL D 104  SER D 133  TYR D 150
SITE     2 AC2  5 ASP E 152
SITE     1 AC3  3 VAL E 129  SER E 144  VAL E 159
CRYST1   67.260  137.290   88.290  90.00 106.64  90.00 P 1 21 1      4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.014868  0.000000  0.004444        0.00000
SCALE2      0.000000  0.007284  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011821        0.00000
      
PROCHECK
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