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PDBsum entry 4i5b

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Immune system PDB id
4i5b
Jmol
Contents
Protein chains
180 a.a.
192 a.a.
12 a.a.
11 a.a.
Waters ×190
HEADER    IMMUNE SYSTEM                           28-NOV-12   4I5B
TITLE     STRUCTURE OF HUMAN MHC CLASS II PROTEIN HLA-DR1 CARRYING AN INFLUENZA
TITLE    2 HEMAGGLUTININ PEPTIDE PARTIALLY FILLING THE BINDING GROOVE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND   3 CHAIN: A, D;
COMPND   4 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND   8 CHAIN: B, E;
COMPND   9 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND  10 ENGINEERED: YES;
COMPND  11 MOL_ID: 3;
COMPND  12 MOLECULE: TRUNCATED HEMAGGLUTININ PEPTIDE;
COMPND  13 CHAIN: C, F;
COMPND  14 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DRA, HLA-DRA1;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 MOL_ID: 2;
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  10 ORGANISM_COMMON: HUMAN;
SOURCE  11 ORGANISM_TAXID: 9606;
SOURCE  12 GENE: HLA-DRB1;
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  15 MOL_ID: 3;
SOURCE  16 SYNTHETIC: YES
KEYWDS    IMMUNOGLOBULIN FOLD, ANTIGEN PRESENTATION, PEPTIDE-MHC COMPLEX,
KEYWDS   2 MEMBRANE, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.-S.E.D.SCHULZE
REVDAT   1   04-DEC-13 4I5B    0
JRNL        AUTH   M.-S.E.D.SCHULZE
JRNL        TITL   STRUCTURAL CONSERVATION OF MHC CLASS II PEPTIDE-BINDING
JRNL        TITL 2 GROOVE IN ABSENCE OF PEPTIDE RESIDUES N-TERMINAL TO P1
JRNL        TITL 3 POCKET
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.28
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.4
REMARK   3   NUMBER OF REFLECTIONS             : 58717
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050
REMARK   3   FREE R VALUE TEST SET COUNT      : 2967
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 49.2908 -  5.8510    0.98     3010   177  0.1905 0.1994
REMARK   3     2  5.8510 -  4.6452    0.98     2934   134  0.1683 0.1818
REMARK   3     3  4.6452 -  4.0583    0.96     2839   146  0.1639 0.1847
REMARK   3     4  4.0583 -  3.6874    0.96     2799   150  0.1939 0.2259
REMARK   3     5  3.6874 -  3.4232    0.95     2792   153  0.1967 0.2385
REMARK   3     6  3.4232 -  3.2214    0.95     2750   157  0.2089 0.2380
REMARK   3     7  3.2214 -  3.0601    0.95     2741   143  0.2228 0.2676
REMARK   3     8  3.0601 -  2.9269    0.95     2760   143  0.2255 0.2714
REMARK   3     9  2.9269 -  2.8142    0.95     2752   138  0.2134 0.2914
REMARK   3    10  2.8142 -  2.7171    0.94     2730   125  0.2041 0.2350
REMARK   3    11  2.7171 -  2.6322    0.94     2711   151  0.2114 0.2567
REMARK   3    12  2.6322 -  2.5570    0.94     2705   146  0.2146 0.2583
REMARK   3    13  2.5570 -  2.4896    0.93     2708   131  0.2063 0.2450
REMARK   3    14  2.4896 -  2.4289    0.93     2670   136  0.2110 0.2723
REMARK   3    15  2.4289 -  2.3737    0.91     2591   156  0.2033 0.2491
REMARK   3    16  2.3737 -  2.3232    0.90     2607   140  0.2063 0.2652
REMARK   3    17  2.3232 -  2.2767    0.88     2513   138  0.2027 0.2660
REMARK   3    18  2.2767 -  2.2337    0.87     2458   144  0.2059 0.2773
REMARK   3    19  2.2337 -  2.1938    0.82     2374   148  0.2087 0.2616
REMARK   3    20  2.1938 -  2.1567    0.79     2256   121  0.2205 0.2674
REMARK   3    21  2.1567 -  2.1200    0.70     2050    90  0.2363 0.3091
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.990
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           6507
REMARK   3   ANGLE     :  1.144           8837
REMARK   3   CHIRALITY :  0.076            951
REMARK   3   PLANARITY :  0.006           1156
REMARK   3   DIHEDRAL  : 14.119           2392
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4I5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-12.
REMARK 100 THE RCSB ID CODE IS RCSB076322.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58717
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 9% PEG 10000,
REMARK 280  PH 4.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.77200
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      105.77200
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       47.90550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.69050
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.90550
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.69050
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      105.77200
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.90550
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.69050
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      105.77200
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.90550
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.69050
REMARK 290   SMTRY3   8  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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH E 207  LIES ON A SPECIAL POSITION.
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     ALA A   182
REMARK 465     PRO A   183
REMARK 465     SER A   184
REMARK 465     PRO A   185
REMARK 465     LEU A   186
REMARK 465     PRO A   187
REMARK 465     GLU A   188
REMARK 465     SER E   192
REMARK 465     GLU E   193
REMARK 465     LYS F   319
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 B  33     -103.67     57.91
REMARK 500    THR B  90      -77.51   -121.86
REMARK 500    GLN B 110       -1.41     73.11
REMARK 500    ASN E  33     -103.34     56.70
REMARK 500    THR E  90      -74.71   -119.72
REMARK 500    GLN E 110       -3.04     76.91
REMARK 500
REMARK 500 REMARK: NULL
DBREF  4I5B A    2   188  UNP    P01903   DRA_HUMAN       27    213
DBREF  4I5B B    2   193  UNP    P04229   2B11_HUMAN      31    222
DBREF  4I5B D    2   188  UNP    P01903   DRA_HUMAN       27    213
DBREF  4I5B E    2   193  UNP    P04229   2B11_HUMAN      31    222
DBREF  4I5B C  308   319  PDB    4I5B     4I5B           308    319
DBREF  4I5B F  308   319  PDB    4I5B     4I5B           308    319
SEQADV 4I5B CYS A   65  UNP  P01903    VAL    90 CONFLICT
SEQADV 4I5B SER B   30  UNP  P04229    CYS    59 CONFLICT
SEQADV 4I5B CYS D   65  UNP  P01903    VAL    90 CONFLICT
SEQADV 4I5B SER E   30  UNP  P04229    CYS    59 CONFLICT
SEQRES   1 A  187  LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU
SEQRES   2 A  187  ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP
SEQRES   3 A  187  GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU
SEQRES   4 A  187  THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER
SEQRES   5 A  187  PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA CYS ASP
SEQRES   6 A  187  LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR
SEQRES   7 A  187  THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU
SEQRES   8 A  187  THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU
SEQRES   9 A  187  ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN
SEQRES  10 A  187  VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY
SEQRES  11 A  187  VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU
SEQRES  12 A  187  PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR
SEQRES  13 A  187  GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU
SEQRES  14 A  187  ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA PRO
SEQRES  15 A  187  SER PRO LEU PRO GLU
SEQRES   1 B  192  ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE GLU
SEQRES   2 B  192  CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU LEU
SEQRES   3 B  192  GLU ARG SER ILE TYR ASN GLN GLU GLU SER VAL ARG PHE
SEQRES   4 B  192  ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU
SEQRES   5 B  192  GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP
SEQRES   6 B  192  LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS
SEQRES   7 B  192  ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN
SEQRES   8 B  192  ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER LYS
SEQRES   9 B  192  THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER
SEQRES  10 B  192  VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP
SEQRES  11 B  192  PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL SER
SEQRES  12 B  192  THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN THR
SEQRES  13 B  192  LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL
SEQRES  14 B  192  TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO
SEQRES  15 B  192  LEU THR VAL GLU TRP ARG ALA ARG SER GLU
SEQRES   1 C   12  VAL VAL LYS GLN ASN CYS LEU LYS LEU ALA THR LYS
SEQRES   1 D  187  LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU
SEQRES   2 D  187  ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE ASP
SEQRES   3 D  187  GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS GLU
SEQRES   4 D  187  THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA SER
SEQRES   5 D  187  PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA CYS ASP
SEQRES   6 D  187  LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN TYR
SEQRES   7 D  187  THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL LEU
SEQRES   8 D  187  THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU
SEQRES   9 D  187  ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL ASN
SEQRES  10 D  187  VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR GLY
SEQRES  11 D  187  VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS LEU
SEQRES  12 D  187  PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR
SEQRES  13 D  187  GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU
SEQRES  14 D  187  ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA PRO
SEQRES  15 D  187  SER PRO LEU PRO GLU
SEQRES   1 E  192  ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE GLU
SEQRES   2 E  192  CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU LEU
SEQRES   3 E  192  GLU ARG SER ILE TYR ASN GLN GLU GLU SER VAL ARG PHE
SEQRES   4 E  192  ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU
SEQRES   5 E  192  GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS ASP
SEQRES   6 E  192  LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR CYS
SEQRES   7 E  192  ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL GLN
SEQRES   8 E  192  ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER LYS
SEQRES   9 E  192  THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS SER
SEQRES  10 E  192  VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG TRP
SEQRES  11 E  192  PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL SER
SEQRES  12 E  192  THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN THR
SEQRES  13 E  192  LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU VAL
SEQRES  14 E  192  TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER PRO
SEQRES  15 E  192  LEU THR VAL GLU TRP ARG ALA ARG SER GLU
SEQRES   1 F   12  VAL VAL LYS GLN ASN CYS LEU LYS LEU ALA THR LYS
FORMUL   7  HOH   *190(H2 O)
HELIX    1   1 LEU A   45  ALA A   52  1                                   8
HELIX    2   2 GLU A   55  SER A   77  1                                  23
HELIX    3   3 THR B   51  LEU B   53  5                                   3
HELIX    4   4 GLY B   54  SER B   63  1                                  10
HELIX    5   5 GLN B   64  TYR B   78  1                                  15
HELIX    6   6 TYR B   78  GLU B   87  1                                  10
HELIX    7   7 SER B   88  THR B   90  5                                   3
HELIX    8   8 GLU D   47  ALA D   52  1                                   6
HELIX    9   9 GLU D   55  SER D   77  1                                  23
HELIX   10  10 THR E   51  LEU E   53  5                                   3
HELIX   11  11 GLY E   54  ASN E   62  1                                   9
HELIX   12  12 GLN E   64  TYR E   78  1                                  15
HELIX   13  13 TYR E   78  GLU E   87  1                                  10
HELIX   14  14 SER E   88  THR E   90  5                                   3
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  ILE A   8   O  ASP A  25
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  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  GLU B  35   N  TYR B  32
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   B 4 GLU A  88  THR A  93  0
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  HIS A 149   N  CYS A 107
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  HIS A 149   N  CYS A 107
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 TYR A 161  GLU A 166 -1  O  ARG A 164   N  THR A 120
SHEET    4   D 4 LEU A 174  TRP A 178 -1  O  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  SER B 118   N  THR B 100
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  SER B 118   N  THR B 100
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  ARG B 133   O  GLN B 136
SHEET    3   G 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175
SHEET    1   H 8 GLU D  40  TRP D  43  0
SHEET    2   H 8 ASP D  29  ASP D  35 -1  N  HIS D  33   O  VAL D  42
SHEET    3   H 8 SER D  19  PHE D  26 -1  N  PHE D  26   O  ASP D  29
SHEET    4   H 8 HIS D   5  ASN D  15 -1  N  ILE D   8   O  ASP D  25
SHEET    5   H 8 PHE E   7  PHE E  18 -1  O  CYS E  15   N  ILE D   7
SHEET    6   H 8 ARG E  23  TYR E  32 -1  O  LEU E  27   N  GLU E  14
SHEET    7   H 8 GLU E  35  ASP E  41 -1  O  GLU E  35   N  TYR E  32
SHEET    8   H 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39
SHEET    1   I 4 GLU D  88  THR D  93  0
SHEET    2   I 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   I 4 PHE D 145  PHE D 153 -1  O  HIS D 149   N  CYS D 107
SHEET    4   I 4 SER D 133  GLU D 134 -1  N  SER D 133   O  TYR D 150
SHEET    1   J 4 GLU D  88  THR D  93  0
SHEET    2   J 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   J 4 PHE D 145  PHE D 153 -1  O  HIS D 149   N  CYS D 107
SHEET    4   J 4 LEU D 138  PRO D 139 -1  N  LEU D 138   O  ARG D 146
SHEET    1   K 4 LYS D 126  VAL D 128  0
SHEET    2   K 4 ASN D 118  ARG D 123 -1  N  ARG D 123   O  LYS D 126
SHEET    3   K 4 VAL D 160  GLU D 166 -1  O  ARG D 164   N  THR D 120
SHEET    4   K 4 LEU D 174  GLU D 179 -1  O  LEU D 174   N  VAL D 165
SHEET    1   L 4 LYS E  98  PRO E 103  0
SHEET    2   L 4 ASN E 113  PHE E 122 -1  O  SER E 120   N  LYS E  98
SHEET    3   L 4 PHE E 155  THR E 163 -1  O  LEU E 161   N  LEU E 115
SHEET    4   L 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160
SHEET    1   M 4 LYS E  98  PRO E 103  0
SHEET    2   M 4 ASN E 113  PHE E 122 -1  O  SER E 120   N  LYS E  98
SHEET    3   M 4 PHE E 155  THR E 163 -1  O  LEU E 161   N  LEU E 115
SHEET    4   M 4 ILE E 148  GLN E 149 -1  N  ILE E 148   O  GLN E 156
SHEET    1   N 4 GLN E 136  GLU E 137  0
SHEET    2   N 4 GLU E 128  ARG E 133 -1  N  ARG E 133   O  GLN E 136
SHEET    3   N 4 VAL E 170  GLU E 176 -1  O  GLN E 174   N  ARG E 130
SHEET    4   N 4 LEU E 184  ARG E 189 -1  O  TRP E 188   N  TYR E 171
SSBOND   1 CYS A   65    CYS C  313                          1555   1555  2.08
SSBOND   2 CYS A  107    CYS A  163                          1555   1555  2.02
SSBOND   3 CYS B   15    CYS B   79                          1555   1555  2.06
SSBOND   4 CYS B  117    CYS B  173                          1555   1555  2.03
SSBOND   5 CYS D   65    CYS F  313                          1555   1555  2.06
SSBOND   6 CYS D  107    CYS D  163                          1555   1555  2.06
SSBOND   7 CYS E   15    CYS E   79                          1555   1555  2.08
SSBOND   8 CYS E  117    CYS E  173                          1555   1555  2.04
CISPEP   1 ASN A   15    PRO A   16          0         2.89
CISPEP   2 THR A  113    PRO A  114          0        -2.22
CISPEP   3 TYR B  123    PRO B  124          0         2.36
CISPEP   4 ASN D   15    PRO D   16          0         3.23
CISPEP   5 THR D  113    PRO D  114          0        -0.95
CISPEP   6 TYR E  123    PRO E  124          0         0.81
CRYST1   95.811  111.381  211.544  90.00  90.00  90.00 C 2 2 21     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.010437  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008978  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004727        0.00000
      
PROCHECK
Go to PROCHECK summary
 References