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PDBsum entry 1iu4

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Top Page protein Protein-protein interface(s) links
Transferase PDB id
1iu4
Jmol
Contents
Protein chains
331 a.a.
Waters ×550
HEADER    TRANSFERASE                             27-FEB-02   1IU4
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE MICROBIAL TRANSGLUTAMINASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MICROBIAL TRANSGLUTAMINASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: RESIDUES 1-331;
COMPND   5 EC: 2.3.2.13;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES MOBARAENSIS;
SOURCE   3 ORGANISM_TAXID: 35621;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ALPHA-BETA, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.KASHIWAGI,K.YOKOYAMA,K.ISHIKAWA,K.ONO,D.EJIMA,H.MATSUI,
AUTHOR   2 E.SUZUKI
REVDAT   3   24-FEB-09 1IU4    1       VERSN
REVDAT   2   04-MAR-03 1IU4    1       JRNL
REVDAT   1   27-AUG-02 1IU4    0
JRNL        AUTH   T.KASHIWAGI,K.YOKOYAMA,K.ISHIKAWA,K.ONO,D.EJIMA,
JRNL        AUTH 2 H.MATSUI,E.SUZUKI
JRNL        TITL   CRYSTAL STRUCTURE OF MICROBIAL TRANSGLUTAMINASE
JRNL        TITL 2 FROM STREPTOVERTICILLIUM MOBARAENSE
JRNL        REF    J.BIOL.CHEM.                  V. 277 44252 2002
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   12221081
JRNL        DOI    10.1074/JBC.M203933200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.5
REMARK   3   NUMBER OF REFLECTIONS             : 54496
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.266
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2752
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            : 10712
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 550
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.25
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  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) : 0.020
REMARK   3   BOND ANGLES            (DEGREES) : 3.65
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  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 1IU4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-FEB-02.
REMARK 100 THE RCSB ID CODE IS RCSB005277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-99
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 5.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : SI(111) (JOHAM TYPE)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55351
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 1.0
REMARK 200  DATA REDUNDANCY                : 3.380
REMARK 200  R MERGE                    (I) : 0.04000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.0000
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) : 2.44
REMARK 200  COMPLETENESS FOR SHELL     (%) : 0.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.13000
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: MIR
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG1000, CALCIUM CHLORIDE,
REMARK 280  CACODYLATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  293K
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       58.56000
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, 3, 4
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 300 REMARK: THE PROTEIN ACTS AS A MONOMER.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS A  64   CB    CYS A  64   SG      0.110
REMARK 500    HIS A 289   CG    HIS A 289   CD2     0.066
REMARK 500    ARG B  45   NE    ARG B  45   CZ      0.085
REMARK 500    CYS B  64   CB    CYS B  64   SG      0.121
REMARK 500    CYS C  64   CB    CYS C  64   SG      0.184
REMARK 500    HIS C 201   CG    HIS C 201   CD2     0.058
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    ASP A   1   CA  -  CB  -  CG  ANGL. DEV. = -13.4 DEGREES
REMARK 500    TYR A  20   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    TYR A  24   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    VAL A  30   CG1 -  CB  -  CG2 ANGL. DEV. =  13.1 DEGREES
REMARK 500    VAL A  31   CB  -  CA  -  C   ANGL. DEV. = -15.6 DEGREES
REMARK 500    VAL A  31   CG1 -  CB  -  CG2 ANGL. DEV. =  12.5 DEGREES
REMARK 500    TYR A  34   CB  -  CG  -  CD1 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A  45   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ALA A 106   CB  -  CA  -  C   ANGL. DEV. = -11.1 DEGREES
REMARK 500    GLU A 115   CB  -  CA  -  C   ANGL. DEV. = -12.9 DEGREES
REMARK 500    ARG A 125   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A 127   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 DEGREES
REMARK 500    ARG A 127   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A 127   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A 135   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    TYR A 146   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP A 189   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    LYS A 200   CB  -  CA  -  C   ANGL. DEV. = -13.1 DEGREES
REMARK 500    ARG A 215   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500    ARG A 224   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 236   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    TYR A 256   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    LYS A 269   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES
REMARK 500    THR A 270   N   -  CA  -  CB  ANGL. DEV. = -12.9 DEGREES
REMARK 500    THR A 270   CA  -  CB  -  CG2 ANGL. DEV. =   9.2 DEGREES
REMARK 500    TYR A 302   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ASP B   3   CA  -  CB  -  CG  ANGL. DEV. = -14.1 DEGREES
REMARK 500    ARG B  15   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG B  21   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    TYR B  24   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    VAL B  31   CG1 -  CB  -  CG2 ANGL. DEV. =  12.1 DEGREES
REMARK 500    ARG B  36   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG B  36   NE  -  CZ  -  NH2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG B  45   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG B  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    TYR B  62   CB  -  CG  -  CD1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    CYS B  64   CA  -  CB  -  SG  ANGL. DEV. =   7.0 DEGREES
REMARK 500    LYS B  95   C   -  N   -  CA  ANGL. DEV. = -17.6 DEGREES
REMARK 500    ARG B 111   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG B 111   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    LEU B 137   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES
REMARK 500    GLU B 153   CA  -  CB  -  CG  ANGL. DEV. =  13.5 DEGREES
REMARK 500    ARG B 162   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG B 175   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG B 208   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG B 224   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG B 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TYR B 256   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     109 ANGLE DEVIATIONS.
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    THR A  53      151.19    -48.69
REMARK 500    SER A  61       -4.38    -59.97
REMARK 500    SER A 101       98.29     -1.27
REMARK 500    ASP A 165      159.11    -25.26
REMARK 500    THR A 245      -76.75    -92.79
REMARK 500    ALA A 261       39.88   -158.14
REMARK 500    GLU A 264       99.83    -25.99
REMARK 500    ASP A 268      -38.15    -31.98
REMARK 500    HIS A 277     -179.80   -173.56
REMARK 500    ALA A 280       67.69   -119.25
REMARK 500    ASP A 304      -34.11    -32.63
REMARK 500    CYS B  64      -67.30    -22.69
REMARK 500    PRO B  76       97.34    -24.71
REMARK 500    THR B  77      -66.36    -21.78
REMARK 500    ASN B  78       25.38     42.72
REMARK 500    ASN B  96      -40.30    173.34
REMARK 500    ASN B 139       -6.51     60.58
REMARK 500    ASN B 158       65.26     38.02
REMARK 500    SER B 191        3.97    -67.38
REMARK 500    PRO B 227     -133.96     29.63
REMARK 500    ASN B 239       40.14     37.19
REMARK 500    THR B 245      -72.20    -89.97
REMARK 500    PRO B 247       73.57    -65.21
REMARK 500    GLU B 249       86.82    -39.31
REMARK 500    ALA B 261       40.57   -176.26
REMARK 500    GLU B 264      116.75    -39.25
REMARK 500    ASN B 282      -43.65    -22.93
REMARK 500    ASP C   4      139.50    -36.39
REMARK 500    PRO C  12      141.94    -39.70
REMARK 500    ASP C  46       63.96   -117.41
REMARK 500    PRO C  76      108.78    -52.96
REMARK 500    SER C 101     -131.59     67.74
REMARK 500    SER C 168      152.64    -46.16
REMARK 500    THR C 177      106.44    -46.42
REMARK 500    HIS C 188      -10.07     74.84
REMARK 500    ARG C 208       12.66     49.77
REMARK 500    ARG C 238       -9.40     61.62
REMARK 500    THR C 245      -79.58    -86.39
REMARK 500    ALA C 261       60.15   -170.67
REMARK 500    GLU C 264      126.33    -36.39
REMARK 500    VAL D  30      150.92    -48.06
REMARK 500    ARG D  36      -69.66    -23.55
REMARK 500    HIS D  44       92.02    -41.97
REMARK 500    ASP D  46     -148.70     42.61
REMARK 500    CYS D  64      -58.91    -24.12
REMARK 500    PRO D  76      109.47    -32.88
REMARK 500    LYS D  95       -4.01     60.79
REMARK 500    PRO D  99      106.25    -34.55
REMARK 500    ARG D 100     -103.26    -54.43
REMARK 500    SER D 101      -79.38    -74.15
REMARK 500    ASN D 139      -31.20     66.38
REMARK 500    ALA D 160      -27.31    -37.14
REMARK 500    ASP D 165      155.90    -39.99
REMARK 500    SER D 179      -22.69    -39.25
REMARK 500    ASN D 184      -53.62    -25.95
REMARK 500    HIS D 188        9.65     59.94
REMARK 500    ASP D 207      103.59    -58.00
REMARK 500    SER D 210     -144.06    -71.72
REMARK 500    PHE D 223       27.74     42.90
REMARK 500    SER D 235      -55.64    -27.01
REMARK 500    ALA D 261       55.67   -164.48
REMARK 500    ARG D 296      -60.39    -20.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ALA A  166     ARG A  167                  146.15
REMARK 500 ASN A  282     GLY A  283                 -146.34
REMARK 500 GLU A  300     GLY A  301                 -111.39
REMARK 500 PRO B   76     THR B   77                  143.35
REMARK 500 ALA B  226     PRO B  227                  146.13
REMARK 500 PRO B  281     ASN B  282                  149.55
REMARK 500 TYR C   20     ARG C   21                 -146.90
REMARK 500 ARG C  100     SER C  101                  127.79
REMARK 500 GLN C  206     ASP C  207                 -144.67
REMARK 500 ARG C  208     SER C  209                  113.45
REMARK 500 TYR D   20     ARG D   21                 -142.61
REMARK 500 ARG D   45     ASP D   46                 -146.27
REMARK 500 LYS D   95     ASN D   96                  133.21
REMARK 500 ARG D  100     SER D  101                 -148.30
REMARK 500 GLY D  102     GLU D  103                 -134.59
REMARK 500 ASN D  156     GLY D  157                  149.11
REMARK 500 GLY D  218     ASP D  219                  148.62
REMARK 500 HIS D  274     GLY D  275                 -142.88
REMARK 500 ASN D  282     GLY D  283                   62.13
REMARK 500 ASP D  324     LYS D  325                  147.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A  26         0.09    SIDE_CHAIN
REMARK 500    ARG A  36         0.17    SIDE_CHAIN
REMARK 500    TYR A  42         0.08    SIDE_CHAIN
REMARK 500    ARG A  45         0.15    SIDE_CHAIN
REMARK 500    TYR A  62         0.12    SIDE_CHAIN
REMARK 500    ARG A 105         0.10    SIDE_CHAIN
REMARK 500    ARG A 183         0.12    SIDE_CHAIN
REMARK 500    PHE A 202         0.09    SIDE_CHAIN
REMARK 500    ARG A 224         0.12    SIDE_CHAIN
REMARK 500    ARG A 238         0.19    SIDE_CHAIN
REMARK 500    TYR A 278         0.09    SIDE_CHAIN
REMARK 500    ARG B   5         0.14    SIDE_CHAIN
REMARK 500    TYR B  34         0.07    SIDE_CHAIN
REMARK 500    ARG B  36         0.13    SIDE_CHAIN
REMARK 500    TYR B  62         0.09    SIDE_CHAIN
REMARK 500    ARG B  89         0.08    SIDE_CHAIN
REMARK 500    ARG B 105         0.13    SIDE_CHAIN
REMARK 500    ARG B 175         0.12    SIDE_CHAIN
REMARK 500    TYR B 198         0.07    SIDE_CHAIN
REMARK 500    ARG B 208         0.08    SIDE_CHAIN
REMARK 500    TYR B 217         0.09    SIDE_CHAIN
REMARK 500    PHE B 254         0.08    SIDE_CHAIN
REMARK 500    TYR B 256         0.08    SIDE_CHAIN
REMARK 500    ARG B 296         0.08    SIDE_CHAIN
REMARK 500    ARG B 307         0.12    SIDE_CHAIN
REMARK 500    ARG C  21         0.09    SIDE_CHAIN
REMARK 500    TYR C  24         0.09    SIDE_CHAIN
REMARK 500    ARG C  48         0.08    SIDE_CHAIN
REMARK 500    TYR C  75         0.11    SIDE_CHAIN
REMARK 500    ARG C 105         0.12    SIDE_CHAIN
REMARK 500    ARG C 162         0.21    SIDE_CHAIN
REMARK 500    ARG C 175         0.09    SIDE_CHAIN
REMARK 500    ARG C 192         0.20    SIDE_CHAIN
REMARK 500    TYR C 217         0.07    SIDE_CHAIN
REMARK 500    ARG C 242         0.12    SIDE_CHAIN
REMARK 500    TYR C 291         0.11    SIDE_CHAIN
REMARK 500    TYR C 302         0.08    SIDE_CHAIN
REMARK 500    ARG C 307         0.10    SIDE_CHAIN
REMARK 500    ARG D  21         0.09    SIDE_CHAIN
REMARK 500    ARG D  57         0.13    SIDE_CHAIN
REMARK 500    ARG D  98         0.34    SIDE_CHAIN
REMARK 500    ARG D 111         0.16    SIDE_CHAIN
REMARK 500    ARG D 215         0.12    SIDE_CHAIN
REMARK 500    ARG D 238         0.17    SIDE_CHAIN
REMARK 500    TYR D 278         0.16    SIDE_CHAIN
REMARK 500    ARG D 307         0.17    SIDE_CHAIN
REMARK 500    TYR D 310         0.15    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH C 391        DISTANCE =  6.45 ANGSTROMS
REMARK 525    HOH A 401        DISTANCE =  5.49 ANGSTROMS
REMARK 525    HOH C 416        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH C 420        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH B 428        DISTANCE =  6.10 ANGSTROMS
REMARK 525    HOH C 447        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH B 460        DISTANCE =  5.69 ANGSTROMS
REMARK 525    HOH A 471        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH B 472        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH C 480        DISTANCE =  6.79 ANGSTROMS
DBREF  1IU4 A    1   331  UNP    P81453   TGAS_STRMB      46    376
DBREF  1IU4 B    1   331  UNP    P81453   TGAS_STRMB      46    376
DBREF  1IU4 C    1   331  UNP    P81453   TGAS_STRMB      46    376
DBREF  1IU4 D    1   331  UNP    P81453   TGAS_STRMB      46    376
SEQRES   1 A  331  ASP SER ASP ASP ARG VAL THR PRO PRO ALA GLU PRO LEU
SEQRES   2 A  331  ASP ARG MET PRO ASP PRO TYR ARG PRO SER TYR GLY ARG
SEQRES   3 A  331  ALA GLU THR VAL VAL ASN ASN TYR ILE ARG LYS TRP GLN
SEQRES   4 A  331  GLN VAL TYR SER HIS ARG ASP GLY ARG LYS GLN GLN MET
SEQRES   5 A  331  THR GLU GLU GLN ARG GLU TRP LEU SER TYR GLY CYS VAL
SEQRES   6 A  331  GLY VAL THR TRP VAL ASN SER GLY GLN TYR PRO THR ASN
SEQRES   7 A  331  ARG LEU ALA PHE ALA SER PHE ASP GLU ASP ARG PHE LYS
SEQRES   8 A  331  ASN GLU LEU LYS ASN GLY ARG PRO ARG SER GLY GLU THR
SEQRES   9 A  331  ARG ALA GLU PHE GLU GLY ARG VAL ALA LYS GLU SER PHE
SEQRES  10 A  331  ASP GLU GLU LYS GLY PHE GLN ARG ALA ARG GLU VAL ALA
SEQRES  11 A  331  SER VAL MET ASN ARG ALA LEU GLU ASN ALA HIS ASP GLU
SEQRES  12 A  331  SER ALA TYR LEU ASP ASN LEU LYS LYS GLU LEU ALA ASN
SEQRES  13 A  331  GLY ASN ASP ALA LEU ARG ASN GLU ASP ALA ARG SER PRO
SEQRES  14 A  331  PHE TYR SER ALA LEU ARG ASN THR PRO SER PHE LYS GLU
SEQRES  15 A  331  ARG ASN GLY GLY ASN HIS ASP PRO SER ARG MET LYS ALA
SEQRES  16 A  331  VAL ILE TYR SER LYS HIS PHE TRP SER GLY GLN ASP ARG
SEQRES  17 A  331  SER SER SER ALA ASP LYS ARG LYS TYR GLY ASP PRO ASP
SEQRES  18 A  331  ALA PHE ARG PRO ALA PRO GLY THR GLY LEU VAL ASP MET
SEQRES  19 A  331  SER ARG ASP ARG ASN ILE PRO ARG SER PRO THR SER PRO
SEQRES  20 A  331  GLY GLU GLY PHE VAL ASN PHE ASP TYR GLY TRP PHE GLY
SEQRES  21 A  331  ALA GLN THR GLU ALA ASP ALA ASP LYS THR VAL TRP THR
SEQRES  22 A  331  HIS GLY ASN HIS TYR HIS ALA PRO ASN GLY SER LEU GLY
SEQRES  23 A  331  ALA MET HIS VAL TYR GLU SER LYS PHE ARG ASN TRP SER
SEQRES  24 A  331  GLU GLY TYR SER ASP PHE ASP ARG GLY ALA TYR VAL ILE
SEQRES  25 A  331  THR PHE ILE PRO LYS SER TRP ASN THR ALA PRO ASP LYS
SEQRES  26 A  331  VAL LYS GLN GLY TRP PRO
SEQRES   1 B  331  ASP SER ASP ASP ARG VAL THR PRO PRO ALA GLU PRO LEU
SEQRES   2 B  331  ASP ARG MET PRO ASP PRO TYR ARG PRO SER TYR GLY ARG
SEQRES   3 B  331  ALA GLU THR VAL VAL ASN ASN TYR ILE ARG LYS TRP GLN
SEQRES   4 B  331  GLN VAL TYR SER HIS ARG ASP GLY ARG LYS GLN GLN MET
SEQRES   5 B  331  THR GLU GLU GLN ARG GLU TRP LEU SER TYR GLY CYS VAL
SEQRES   6 B  331  GLY VAL THR TRP VAL ASN SER GLY GLN TYR PRO THR ASN
SEQRES   7 B  331  ARG LEU ALA PHE ALA SER PHE ASP GLU ASP ARG PHE LYS
SEQRES   8 B  331  ASN GLU LEU LYS ASN GLY ARG PRO ARG SER GLY GLU THR
SEQRES   9 B  331  ARG ALA GLU PHE GLU GLY ARG VAL ALA LYS GLU SER PHE
SEQRES  10 B  331  ASP GLU GLU LYS GLY PHE GLN ARG ALA ARG GLU VAL ALA
SEQRES  11 B  331  SER VAL MET ASN ARG ALA LEU GLU ASN ALA HIS ASP GLU
SEQRES  12 B  331  SER ALA TYR LEU ASP ASN LEU LYS LYS GLU LEU ALA ASN
SEQRES  13 B  331  GLY ASN ASP ALA LEU ARG ASN GLU ASP ALA ARG SER PRO
SEQRES  14 B  331  PHE TYR SER ALA LEU ARG ASN THR PRO SER PHE LYS GLU
SEQRES  15 B  331  ARG ASN GLY GLY ASN HIS ASP PRO SER ARG MET LYS ALA
SEQRES  16 B  331  VAL ILE TYR SER LYS HIS PHE TRP SER GLY GLN ASP ARG
SEQRES  17 B  331  SER SER SER ALA ASP LYS ARG LYS TYR GLY ASP PRO ASP
SEQRES  18 B  331  ALA PHE ARG PRO ALA PRO GLY THR GLY LEU VAL ASP MET
SEQRES  19 B  331  SER ARG ASP ARG ASN ILE PRO ARG SER PRO THR SER PRO
SEQRES  20 B  331  GLY GLU GLY PHE VAL ASN PHE ASP TYR GLY TRP PHE GLY
SEQRES  21 B  331  ALA GLN THR GLU ALA ASP ALA ASP LYS THR VAL TRP THR
SEQRES  22 B  331  HIS GLY ASN HIS TYR HIS ALA PRO ASN GLY SER LEU GLY
SEQRES  23 B  331  ALA MET HIS VAL TYR GLU SER LYS PHE ARG ASN TRP SER
SEQRES  24 B  331  GLU GLY TYR SER ASP PHE ASP ARG GLY ALA TYR VAL ILE
SEQRES  25 B  331  THR PHE ILE PRO LYS SER TRP ASN THR ALA PRO ASP LYS
SEQRES  26 B  331  VAL LYS GLN GLY TRP PRO
SEQRES   1 C  331  ASP SER ASP ASP ARG VAL THR PRO PRO ALA GLU PRO LEU
SEQRES   2 C  331  ASP ARG MET PRO ASP PRO TYR ARG PRO SER TYR GLY ARG
SEQRES   3 C  331  ALA GLU THR VAL VAL ASN ASN TYR ILE ARG LYS TRP GLN
SEQRES   4 C  331  GLN VAL TYR SER HIS ARG ASP GLY ARG LYS GLN GLN MET
SEQRES   5 C  331  THR GLU GLU GLN ARG GLU TRP LEU SER TYR GLY CYS VAL
SEQRES   6 C  331  GLY VAL THR TRP VAL ASN SER GLY GLN TYR PRO THR ASN
SEQRES   7 C  331  ARG LEU ALA PHE ALA SER PHE ASP GLU ASP ARG PHE LYS
SEQRES   8 C  331  ASN GLU LEU LYS ASN GLY ARG PRO ARG SER GLY GLU THR
SEQRES   9 C  331  ARG ALA GLU PHE GLU GLY ARG VAL ALA LYS GLU SER PHE
SEQRES  10 C  331  ASP GLU GLU LYS GLY PHE GLN ARG ALA ARG GLU VAL ALA
SEQRES  11 C  331  SER VAL MET ASN ARG ALA LEU GLU ASN ALA HIS ASP GLU
SEQRES  12 C  331  SER ALA TYR LEU ASP ASN LEU LYS LYS GLU LEU ALA ASN
SEQRES  13 C  331  GLY ASN ASP ALA LEU ARG ASN GLU ASP ALA ARG SER PRO
SEQRES  14 C  331  PHE TYR SER ALA LEU ARG ASN THR PRO SER PHE LYS GLU
SEQRES  15 C  331  ARG ASN GLY GLY ASN HIS ASP PRO SER ARG MET LYS ALA
SEQRES  16 C  331  VAL ILE TYR SER LYS HIS PHE TRP SER GLY GLN ASP ARG
SEQRES  17 C  331  SER SER SER ALA ASP LYS ARG LYS TYR GLY ASP PRO ASP
SEQRES  18 C  331  ALA PHE ARG PRO ALA PRO GLY THR GLY LEU VAL ASP MET
SEQRES  19 C  331  SER ARG ASP ARG ASN ILE PRO ARG SER PRO THR SER PRO
SEQRES  20 C  331  GLY GLU GLY PHE VAL ASN PHE ASP TYR GLY TRP PHE GLY
SEQRES  21 C  331  ALA GLN THR GLU ALA ASP ALA ASP LYS THR VAL TRP THR
SEQRES  22 C  331  HIS GLY ASN HIS TYR HIS ALA PRO ASN GLY SER LEU GLY
SEQRES  23 C  331  ALA MET HIS VAL TYR GLU SER LYS PHE ARG ASN TRP SER
SEQRES  24 C  331  GLU GLY TYR SER ASP PHE ASP ARG GLY ALA TYR VAL ILE
SEQRES  25 C  331  THR PHE ILE PRO LYS SER TRP ASN THR ALA PRO ASP LYS
SEQRES  26 C  331  VAL LYS GLN GLY TRP PRO
SEQRES   1 D  331  ASP SER ASP ASP ARG VAL THR PRO PRO ALA GLU PRO LEU
SEQRES   2 D  331  ASP ARG MET PRO ASP PRO TYR ARG PRO SER TYR GLY ARG
SEQRES   3 D  331  ALA GLU THR VAL VAL ASN ASN TYR ILE ARG LYS TRP GLN
SEQRES   4 D  331  GLN VAL TYR SER HIS ARG ASP GLY ARG LYS GLN GLN MET
SEQRES   5 D  331  THR GLU GLU GLN ARG GLU TRP LEU SER TYR GLY CYS VAL
SEQRES   6 D  331  GLY VAL THR TRP VAL ASN SER GLY GLN TYR PRO THR ASN
SEQRES   7 D  331  ARG LEU ALA PHE ALA SER PHE ASP GLU ASP ARG PHE LYS
SEQRES   8 D  331  ASN GLU LEU LYS ASN GLY ARG PRO ARG SER GLY GLU THR
SEQRES   9 D  331  ARG ALA GLU PHE GLU GLY ARG VAL ALA LYS GLU SER PHE
SEQRES  10 D  331  ASP GLU GLU LYS GLY PHE GLN ARG ALA ARG GLU VAL ALA
SEQRES  11 D  331  SER VAL MET ASN ARG ALA LEU GLU ASN ALA HIS ASP GLU
SEQRES  12 D  331  SER ALA TYR LEU ASP ASN LEU LYS LYS GLU LEU ALA ASN
SEQRES  13 D  331  GLY ASN ASP ALA LEU ARG ASN GLU ASP ALA ARG SER PRO
SEQRES  14 D  331  PHE TYR SER ALA LEU ARG ASN THR PRO SER PHE LYS GLU
SEQRES  15 D  331  ARG ASN GLY GLY ASN HIS ASP PRO SER ARG MET LYS ALA
SEQRES  16 D  331  VAL ILE TYR SER LYS HIS PHE TRP SER GLY GLN ASP ARG
SEQRES  17 D  331  SER SER SER ALA ASP LYS ARG LYS TYR GLY ASP PRO ASP
SEQRES  18 D  331  ALA PHE ARG PRO ALA PRO GLY THR GLY LEU VAL ASP MET
SEQRES  19 D  331  SER ARG ASP ARG ASN ILE PRO ARG SER PRO THR SER PRO
SEQRES  20 D  331  GLY GLU GLY PHE VAL ASN PHE ASP TYR GLY TRP PHE GLY
SEQRES  21 D  331  ALA GLN THR GLU ALA ASP ALA ASP LYS THR VAL TRP THR
SEQRES  22 D  331  HIS GLY ASN HIS TYR HIS ALA PRO ASN GLY SER LEU GLY
SEQRES  23 D  331  ALA MET HIS VAL TYR GLU SER LYS PHE ARG ASN TRP SER
SEQRES  24 D  331  GLU GLY TYR SER ASP PHE ASP ARG GLY ALA TYR VAL ILE
SEQRES  25 D  331  THR PHE ILE PRO LYS SER TRP ASN THR ALA PRO ASP LYS
SEQRES  26 D  331  VAL LYS GLN GLY TRP PRO
FORMUL   5  HOH   *550(H2 O)
HELIX    1   1 VAL A   31  TYR A   42  1                                  12
HELIX    2   2 THR A   53  SER A   61  1                                   9
HELIX    3   3 TYR A   62  CYS A   64  5                                   3
HELIX    4   4 VAL A   65  GLY A   73  1                                   9
HELIX    5   5 ASP A   86  GLY A   97  1                                  12
HELIX    6   6 THR A  104  PHE A  117  1                                  14
HELIX    7   7 ASP A  118  ALA A  136  1                                  19
HELIX    8   8 ASP A  142  GLY A  157  1                                  16
HELIX    9   9 ASP A  159  GLU A  164  5                                   6
HELIX   10  10 SER A  172  THR A  177  1                                   6
HELIX   11  11 ASP A  189  SER A  191  5                                   3
HELIX   12  12 SER A  211  GLY A  218  1                                   8
HELIX   13  13 ASP A  266  LYS A  269  5                                   4
HELIX   14  14 PHE A  295  SER A  299  1                                   5
HELIX   15  15 VAL B   31  TYR B   42  1                                  12
HELIX   16  16 THR B   53  SER B   61  1                                   9
HELIX   17  17 TYR B   62  CYS B   64  5                                   3
HELIX   18  18 VAL B   65  GLY B   73  1                                   9
HELIX   19  19 ASP B   86  LYS B   95  1                                  10
HELIX   20  20 THR B  104  SER B  116  1                                  13
HELIX   21  21 ASP B  118  GLU B  138  1                                  21
HELIX   22  22 ASP B  142  GLY B  157  1                                  16
HELIX   23  23 ASN B  158  ASN B  158  5                                   1
HELIX   24  24 ASP B  159  GLU B  164  5                                   6
HELIX   25  25 SER B  168  THR B  177  1                                  10
HELIX   26  26 THR B  177  GLU B  182  1                                   6
HELIX   27  27 ASP B  189  SER B  191  5                                   3
HELIX   28  28 SER B  211  GLY B  218  1                                   8
HELIX   29  29 ASP B  266  LYS B  269  5                                   4
HELIX   30  30 PHE B  295  GLY B  301  1                                   7
HELIX   31  31 VAL C   31  TYR C   42  1                                  12
HELIX   32  32 THR C   53  SER C   61  1                                   9
HELIX   33  33 VAL C   65  GLY C   73  1                                   9
HELIX   34  34 ASP C   86  GLY C   97  1                                  12
HELIX   35  35 THR C  104  SER C  116  1                                  13
HELIX   36  36 GLU C  119  GLU C  138  1                                  20
HELIX   37  37 ASP C  142  ASN C  158  1                                  17
HELIX   38  38 ASP C  159  GLU C  164  5                                   6
HELIX   39  39 SER C  168  THR C  177  1                                  10
HELIX   40  40 THR C  177  GLU C  182  1                                   6
HELIX   41  41 ASP C  189  SER C  191  5                                   3
HELIX   42  42 SER C  211  GLY C  218  1                                   8
HELIX   43  43 ASP C  233  ASP C  237  5                                   5
HELIX   44  44 ASP C  266  LYS C  269  5                                   4
HELIX   45  45 PHE C  295  GLY C  301  1                                   7
HELIX   46  46 VAL D   31  TYR D   42  1                                  12
HELIX   47  47 THR D   53  SER D   61  1                                   9
HELIX   48  48 VAL D   65  GLY D   73  1                                   9
HELIX   49  49 ASP D   86  LEU D   94  1                                   9
HELIX   50  50 THR D  104  PHE D  117  1                                  14
HELIX   51  51 ASP D  118  GLU D  138  1                                  21
HELIX   52  52 ASP D  142  GLY D  157  1                                  16
HELIX   53  53 ASP D  159  GLU D  164  5                                   6
HELIX   54  54 SER D  168  THR D  177  1                                  10
HELIX   55  55 PRO D  178  GLU D  182  5                                   5
HELIX   56  56 ASP D  189  SER D  191  5                                   3
HELIX   57  57 SER D  211  GLY D  218  1                                   8
HELIX   58  58 ASP D  233  ASP D  237  5                                   5
HELIX   59  59 ASP D  266  LYS D  269  5                                   4
HELIX   60  60 PHE D  295  GLY D  301  1                                   7
SHEET    1   A 3 ARG A  26  VAL A  30  0
SHEET    2   A 3 HIS A 289  LYS A 294 -1  O  VAL A 290   N  THR A  29
SHEET    3   A 3 VAL A 271  GLY A 275 -1  N  TRP A 272   O  SER A 293
SHEET    1   B 5 LEU A 231  VAL A 232  0
SHEET    2   B 5 ALA A  81  PHE A  82 -1  N  ALA A  81   O  VAL A 232
SHEET    3   B 5 ARG A 307  PRO A 316 -1  O  TYR A 310   N  PHE A  82
SHEET    4   B 5 MET A 193  PHE A 202 -1  N  LYS A 200   O  ALA A 309
SHEET    5   B 5 PHE A 254  GLY A 260 -1  O  GLY A 260   N  ILE A 197
SHEET    1   C 3 ARG B  26  VAL B  30  0
SHEET    2   C 3 HIS B 289  LYS B 294 -1  O  VAL B 290   N  THR B  29
SHEET    3   C 3 VAL B 271  GLY B 275 -1  N  HIS B 274   O  TYR B 291
SHEET    1   D 5 LEU B 231  VAL B 232  0
SHEET    2   D 5 ALA B  81  PHE B  82 -1  N  ALA B  81   O  VAL B 232
SHEET    3   D 5 ARG B 307  PRO B 316 -1  O  TYR B 310   N  PHE B  82
SHEET    4   D 5 MET B 193  PHE B 202 -1  N  VAL B 196   O  THR B 313
SHEET    5   D 5 ASP B 255  GLY B 260 -1  O  GLY B 257   N  SER B 199
SHEET    1   E 3 ARG C  26  VAL C  30  0
SHEET    2   E 3 HIS C 289  LYS C 294 -1  O  VAL C 290   N  THR C  29
SHEET    3   E 3 VAL C 271  GLY C 275 -1  N  HIS C 274   O  TYR C 291
SHEET    1   F 4 ALA C  81  PHE C  82  0
SHEET    2   F 4 ARG C 307  PRO C 316 -1  O  TYR C 310   N  PHE C  82
SHEET    3   F 4 MET C 193  PHE C 202 -1  N  VAL C 196   O  THR C 313
SHEET    4   F 4 ASP C 255  GLY C 260 -1  O  GLY C 257   N  SER C 199
SHEET    1   G 2 SER C  84  PHE C  85  0
SHEET    2   G 2 PHE C 117  ASP C 118 -1  O  ASP C 118   N  SER C  84
SHEET    1   H 4 PRO D  22  SER D  23  0
SHEET    2   H 4 ARG D  26  VAL D  30 -1  O  ARG D  26   N  SER D  23
SHEET    3   H 4 HIS D 289  LYS D 294 -1  O  VAL D 290   N  THR D  29
SHEET    4   H 4 VAL D 271  THR D 273 -1  N  TRP D 272   O  SER D 293
SHEET    1   I 5 LEU D 231  VAL D 232  0
SHEET    2   I 5 ALA D  81  PHE D  82 -1  N  ALA D  81   O  VAL D 232
SHEET    3   I 5 ARG D 307  PRO D 316 -1  O  TYR D 310   N  PHE D  82
SHEET    4   I 5 MET D 193  PHE D 202 -1  N  TYR D 198   O  VAL D 311
SHEET    5   I 5 PHE D 254  GLY D 260 -1  O  GLY D 260   N  ILE D 197
CISPEP   1 TRP A  330    PRO A  331          0         1.70
CISPEP   2 TRP B  330    PRO B  331          0         5.09
CISPEP   3 TRP C  330    PRO C  331          0        -4.99
CISPEP   4 TRP D  330    PRO D  331          0         6.76
CRYST1   78.410  117.120   85.740  90.00 112.80  90.00 P 1 21 1      8
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      0.012753  0.000000  0.005361        0.00000
SCALE2      0.000000  0.008538  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012652        0.00000
      
PROCHECK
Go to PROCHECK summary
 References