spacer
spacer

PDBsum entry 1xm2

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
1xm2
Jmol
Contents
Protein chains
(+ 0 more) 149 a.a.
Ligands
SO4 ×6
Waters ×92
HEADER    HYDROLASE                               01-OCT-04   1XM2
TITLE     CRYSTAL STRUCTURE OF HUMAN PRL-1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE PHOSPHATASE;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 SYNONYM: PRL-1;
COMPND   5 EC: 3.1.3.48;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.G.JEONG,S.J.KIM,J.H.KIM,J.H.SON,S.E.RYU
REVDAT   2   24-FEB-09 1XM2    1       VERSN
REVDAT   1   25-JAN-05 1XM2    0
JRNL        AUTH   D.G.JEONG,S.J.KIM,J.H.KIM,J.H.SON,M.R.PARK,S.M.LIM,
JRNL        AUTH 2 T.S.YOON,S.E.RYU
JRNL        TITL   TRIMERIC STRUCTURE OF PRL-1 PHOSPHATASE REVEALS AN
JRNL        TITL 2 ACTIVE ENZYME CONFORMATION AND REGULATION
JRNL        TITL 3 MECHANISMS
JRNL        REF    J.MOL.BIOL.                   V. 345   401 2005
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   15571731
JRNL        DOI    10.1016/J.JMB.2004.10.061
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.9
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
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)   (%) : 94.5
REMARK   3   NUMBER OF REFLECTIONS             : 31124
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.237
REMARK   3   FREE R VALUE                     : 0.296
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1546
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            : 7080
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 30
REMARK   3   SOLVENT ATOMS            : 92
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  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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.37
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.17
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.93
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 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 1XM2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PAL/PLS
REMARK 200  BEAMLINE                       : 6B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979, 0.9792, 0.9794, 0.9716
REMARK 200  MONOCHROMATOR                  : MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31124
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5
REMARK 200  DATA REDUNDANCY                : 4.300
REMARK 200  R MERGE                    (I) : 0.07900
REMARK 200  R SYM                      (I) : 0.07900
REMARK 200   FOR THE DATA SET  : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.26000
REMARK 200  R SYM FOR SHELL            (I) : 0.26000
REMARK 200   FOR SHELL         : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4K, SODIUM ACETATE, AMS, PH
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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       42.38000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER. TWO TRIMERS EXIST
REMARK 300 IN THE ASYMMETRIC UNIT.
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 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 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 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     MSE A     1
REMARK 465     ALA A     2
REMARK 465     ARG A     3
REMARK 465     MSE A     4
REMARK 465     ASN A     5
REMARK 465     ARG A     6
REMARK 465     PRO A     7
REMARK 465     ARG A   157
REMARK 465     LEU A   158
REMARK 465     ARG A   159
REMARK 465     PHE A   160
REMARK 465     LYS A   161
REMARK 465     ASP A   162
REMARK 465     SER A   163
REMARK 465     ASN A   164
REMARK 465     GLY A   165
REMARK 465     HIS A   166
REMARK 465     ARG A   167
REMARK 465     ASN A   168
REMARK 465     ASN A   169
REMARK 465     CYS A   170
REMARK 465     CYS A   171
REMARK 465     ILE A   172
REMARK 465     GLN A   173
REMARK 465     MSE B     1
REMARK 465     ALA B     2
REMARK 465     ARG B     3
REMARK 465     MSE B     4
REMARK 465     ASN B     5
REMARK 465     ARG B     6
REMARK 465     PRO B     7
REMARK 465     ARG B   157
REMARK 465     LEU B   158
REMARK 465     ARG B   159
REMARK 465     PHE B   160
REMARK 465     LYS B   161
REMARK 465     ASP B   162
REMARK 465     SER B   163
REMARK 465     ASN B   164
REMARK 465     GLY B   165
REMARK 465     HIS B   166
REMARK 465     ARG B   167
REMARK 465     ASN B   168
REMARK 465     ASN B   169
REMARK 465     CYS B   170
REMARK 465     CYS B   171
REMARK 465     ILE B   172
REMARK 465     GLN B   173
REMARK 465     MSE C     1
REMARK 465     ALA C     2
REMARK 465     ARG C     3
REMARK 465     MSE C     4
REMARK 465     ASN C     5
REMARK 465     ARG C     6
REMARK 465     PRO C     7
REMARK 465     ARG C   157
REMARK 465     LEU C   158
REMARK 465     ARG C   159
REMARK 465     PHE C   160
REMARK 465     LYS C   161
REMARK 465     ASP C   162
REMARK 465     SER C   163
REMARK 465     ASN C   164
REMARK 465     GLY C   165
REMARK 465     HIS C   166
REMARK 465     ARG C   167
REMARK 465     ASN C   168
REMARK 465     ASN C   169
REMARK 465     CYS C   170
REMARK 465     CYS C   171
REMARK 465     ILE C   172
REMARK 465     GLN C   173
REMARK 465     MSE D     1
REMARK 465     ALA D     2
REMARK 465     ARG D     3
REMARK 465     MSE D     4
REMARK 465     ASN D     5
REMARK 465     ARG D     6
REMARK 465     PRO D     7
REMARK 465     THR D    26
REMARK 465     ASN D    27
REMARK 465     ALA D    51
REMARK 465     THR D    52
REMARK 465     TYR D    53
REMARK 465     ARG D   157
REMARK 465     LEU D   158
REMARK 465     ARG D   159
REMARK 465     PHE D   160
REMARK 465     LYS D   161
REMARK 465     ASP D   162
REMARK 465     SER D   163
REMARK 465     ASN D   164
REMARK 465     GLY D   165
REMARK 465     HIS D   166
REMARK 465     ARG D   167
REMARK 465     ASN D   168
REMARK 465     ASN D   169
REMARK 465     CYS D   170
REMARK 465     CYS D   171
REMARK 465     ILE D   172
REMARK 465     GLN D   173
REMARK 465     MSE E     1
REMARK 465     ALA E     2
REMARK 465     ARG E     3
REMARK 465     MSE E     4
REMARK 465     ASN E     5
REMARK 465     ARG E     6
REMARK 465     PRO E     7
REMARK 465     ARG E   157
REMARK 465     LEU E   158
REMARK 465     ARG E   159
REMARK 465     PHE E   160
REMARK 465     LYS E   161
REMARK 465     ASP E   162
REMARK 465     SER E   163
REMARK 465     ASN E   164
REMARK 465     GLY E   165
REMARK 465     HIS E   166
REMARK 465     ARG E   167
REMARK 465     ASN E   168
REMARK 465     ASN E   169
REMARK 465     CYS E   170
REMARK 465     CYS E   171
REMARK 465     ILE E   172
REMARK 465     GLN E   173
REMARK 465     MSE F     1
REMARK 465     ALA F     2
REMARK 465     ARG F     3
REMARK 465     MSE F     4
REMARK 465     ASN F     5
REMARK 465     ARG F     6
REMARK 465     PRO F     7
REMARK 465     THR F    26
REMARK 465     ASN F    27
REMARK 465     ARG F   157
REMARK 465     LEU F   158
REMARK 465     ARG F   159
REMARK 465     PHE F   160
REMARK 465     LYS F   161
REMARK 465     ASP F   162
REMARK 465     SER F   163
REMARK 465     ASN F   164
REMARK 465     GLY F   165
REMARK 465     HIS F   166
REMARK 465     ARG F   167
REMARK 465     ASN F   168
REMARK 465     ASN F   169
REMARK 465     CYS F   170
REMARK 465     CYS F   171
REMARK 465     ILE F   172
REMARK 465     GLN F   173
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    LYS C  15   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    TYR A  14      120.14    161.54
REMARK 500    PRO A  25     -168.41    -61.08
REMARK 500    TRP A  68       57.86   -118.29
REMARK 500    SER A 104     -139.36   -117.12
REMARK 500    ARG A 138      -81.90    -23.12
REMARK 500    TYR B  14      117.59    150.31
REMARK 500    THR B  29        3.89   -153.58
REMARK 500    CYS B  49     -165.24   -120.44
REMARK 500    TRP B  68       79.77   -117.36
REMARK 500    SER B  77      170.09    -59.00
REMARK 500    SER B 104     -158.53   -128.98
REMARK 500    ARG B 138      -76.18    -19.51
REMARK 500    TYR C  14      118.36    156.01
REMARK 500    HIS C  23     -148.68    -93.58
REMARK 500    PRO C  25      102.22    -37.78
REMARK 500    THR C  26      173.59    -49.15
REMARK 500    ASN C  27       50.02     13.79
REMARK 500    ALA C  28      -17.13     54.55
REMARK 500    CYS C  49     -151.57   -113.47
REMARK 500    GLU C  50       87.88   -156.67
REMARK 500    TYR C  53      100.87    172.35
REMARK 500    ASP C  54       76.05    -62.36
REMARK 500    SER C  77      174.43    -59.43
REMARK 500    SER C 104     -167.86   -127.90
REMARK 500    ARG C 138      -76.09    -25.10
REMARK 500    TYR D  14      119.69    163.76
REMARK 500    HIS D  23     -152.54    -85.63
REMARK 500    CYS D  49     -165.62   -108.49
REMARK 500    THR D  55       -9.52    -54.45
REMARK 500    TRP D  68       71.47   -118.78
REMARK 500    ASP D  71      144.08    -37.07
REMARK 500    GLU D  95       70.68   -115.92
REMARK 500    SER D 104     -156.85   -123.60
REMARK 500    PRO E   9       24.83    -68.94
REMARK 500    VAL E  10      106.90    -52.31
REMARK 500    TYR E  14      123.44    146.54
REMARK 500    THR E  52        0.74   -154.79
REMARK 500    SER E 104     -152.18   -130.95
REMARK 500    ARG E 138      -94.62    -25.77
REMARK 500    PRO F   9       43.89    -86.72
REMARK 500    TYR F  14      114.85    157.39
REMARK 500    HIS F  23     -169.87    -79.83
REMARK 500    THR F  29       48.28   -107.18
REMARK 500    CYS F  49     -160.69   -114.82
REMARK 500    TRP F  68       72.04   -115.98
REMARK 500    SER F 104     -151.76   -132.77
REMARK 500    ARG F 138      -74.02    -28.59
REMARK 500    SER F 143      -70.62    -41.88
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 SO4 A 181
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 182
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 183
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 184
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 185
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 186
DBREF  1XM2 A    1   173  UNP    Q93096   TP4A1_HUMAN      1    173
DBREF  1XM2 B    1   173  UNP    Q93096   TP4A1_HUMAN      1    173
DBREF  1XM2 C    1   173  UNP    Q93096   TP4A1_HUMAN      1    173
DBREF  1XM2 D    1   173  UNP    Q93096   TP4A1_HUMAN      1    173
DBREF  1XM2 E    1   173  UNP    Q93096   TP4A1_HUMAN      1    173
DBREF  1XM2 F    1   173  UNP    Q93096   TP4A1_HUMAN      1    173
SEQADV 1XM2 MSE A    1  UNP  Q93096    MET     1 MODIFIED RESIDUE
SEQADV 1XM2 MSE A    4  UNP  Q93096    MET     4 MODIFIED RESIDUE
SEQADV 1XM2 MSE A   17  UNP  Q93096    MET    17 MODIFIED RESIDUE
SEQADV 1XM2 SER A  104  UNP  Q93096    CYS   104 ENGINEERED
SEQADV 1XM2 MSE A  124  UNP  Q93096    MET   124 MODIFIED RESIDUE
SEQADV 1XM2 MSE A  156  UNP  Q93096    MET   156 MODIFIED RESIDUE
SEQADV 1XM2 MSE B    1  UNP  Q93096    MET     1 MODIFIED RESIDUE
SEQADV 1XM2 MSE B    4  UNP  Q93096    MET     4 MODIFIED RESIDUE
SEQADV 1XM2 MSE B   17  UNP  Q93096    MET    17 MODIFIED RESIDUE
SEQADV 1XM2 SER B  104  UNP  Q93096    CYS   104 ENGINEERED
SEQADV 1XM2 MSE B  124  UNP  Q93096    MET   124 MODIFIED RESIDUE
SEQADV 1XM2 MSE B  156  UNP  Q93096    MET   156 MODIFIED RESIDUE
SEQADV 1XM2 MSE C    1  UNP  Q93096    MET     1 MODIFIED RESIDUE
SEQADV 1XM2 MSE C    4  UNP  Q93096    MET     4 MODIFIED RESIDUE
SEQADV 1XM2 MSE C   17  UNP  Q93096    MET    17 MODIFIED RESIDUE
SEQADV 1XM2 SER C  104  UNP  Q93096    CYS   104 ENGINEERED
SEQADV 1XM2 MSE C  124  UNP  Q93096    MET   124 MODIFIED RESIDUE
SEQADV 1XM2 MSE C  156  UNP  Q93096    MET   156 MODIFIED RESIDUE
SEQADV 1XM2 MSE D    1  UNP  Q93096    MET     1 MODIFIED RESIDUE
SEQADV 1XM2 MSE D    4  UNP  Q93096    MET     4 MODIFIED RESIDUE
SEQADV 1XM2 MSE D   17  UNP  Q93096    MET    17 MODIFIED RESIDUE
SEQADV 1XM2 SER D  104  UNP  Q93096    CYS   104 ENGINEERED
SEQADV 1XM2 MSE D  124  UNP  Q93096    MET   124 MODIFIED RESIDUE
SEQADV 1XM2 MSE D  156  UNP  Q93096    MET   156 MODIFIED RESIDUE
SEQADV 1XM2 MSE E    1  UNP  Q93096    MET     1 MODIFIED RESIDUE
SEQADV 1XM2 MSE E    4  UNP  Q93096    MET     4 MODIFIED RESIDUE
SEQADV 1XM2 MSE E   17  UNP  Q93096    MET    17 MODIFIED RESIDUE
SEQADV 1XM2 SER E  104  UNP  Q93096    CYS   104 ENGINEERED
SEQADV 1XM2 MSE E  124  UNP  Q93096    MET   124 MODIFIED RESIDUE
SEQADV 1XM2 MSE E  156  UNP  Q93096    MET   156 MODIFIED RESIDUE
SEQADV 1XM2 MSE F    1  UNP  Q93096    MET     1 MODIFIED RESIDUE
SEQADV 1XM2 MSE F    4  UNP  Q93096    MET     4 MODIFIED RESIDUE
SEQADV 1XM2 MSE F   17  UNP  Q93096    MET    17 MODIFIED RESIDUE
SEQADV 1XM2 SER F  104  UNP  Q93096    CYS   104 ENGINEERED
SEQADV 1XM2 MSE F  124  UNP  Q93096    MET   124 MODIFIED RESIDUE
SEQADV 1XM2 MSE F  156  UNP  Q93096    MET   156 MODIFIED RESIDUE
SEQRES   1 A  173  MSE ALA ARG MSE ASN ARG PRO ALA PRO VAL GLU VAL THR
SEQRES   2 A  173  TYR LYS ASN MSE ARG PHE LEU ILE THR HIS ASN PRO THR
SEQRES   3 A  173  ASN ALA THR LEU ASN LYS PHE ILE GLU GLU LEU LYS LYS
SEQRES   4 A  173  TYR GLY VAL THR THR ILE VAL ARG VAL CYS GLU ALA THR
SEQRES   5 A  173  TYR ASP THR THR LEU VAL GLU LYS GLU GLY ILE HIS VAL
SEQRES   6 A  173  LEU ASP TRP PRO PHE ASP ASP GLY ALA PRO PRO SER ASN
SEQRES   7 A  173  GLN ILE VAL ASP ASP TRP LEU SER LEU VAL LYS ILE LYS
SEQRES   8 A  173  PHE ARG GLU GLU PRO GLY CYS CYS ILE ALA VAL HIS SER
SEQRES   9 A  173  VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU VAL ALA LEU
SEQRES  10 A  173  ALA LEU ILE GLU GLY GLY MSE LYS TYR GLU ASP ALA VAL
SEQRES  11 A  173  GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA PHE ASN SER
SEQRES  12 A  173  LYS GLN LEU LEU TYR LEU GLU LYS TYR ARG PRO LYS MSE
SEQRES  13 A  173  ARG LEU ARG PHE LYS ASP SER ASN GLY HIS ARG ASN ASN
SEQRES  14 A  173  CYS CYS ILE GLN
SEQRES   1 B  173  MSE ALA ARG MSE ASN ARG PRO ALA PRO VAL GLU VAL THR
SEQRES   2 B  173  TYR LYS ASN MSE ARG PHE LEU ILE THR HIS ASN PRO THR
SEQRES   3 B  173  ASN ALA THR LEU ASN LYS PHE ILE GLU GLU LEU LYS LYS
SEQRES   4 B  173  TYR GLY VAL THR THR ILE VAL ARG VAL CYS GLU ALA THR
SEQRES   5 B  173  TYR ASP THR THR LEU VAL GLU LYS GLU GLY ILE HIS VAL
SEQRES   6 B  173  LEU ASP TRP PRO PHE ASP ASP GLY ALA PRO PRO SER ASN
SEQRES   7 B  173  GLN ILE VAL ASP ASP TRP LEU SER LEU VAL LYS ILE LYS
SEQRES   8 B  173  PHE ARG GLU GLU PRO GLY CYS CYS ILE ALA VAL HIS SER
SEQRES   9 B  173  VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU VAL ALA LEU
SEQRES  10 B  173  ALA LEU ILE GLU GLY GLY MSE LYS TYR GLU ASP ALA VAL
SEQRES  11 B  173  GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA PHE ASN SER
SEQRES  12 B  173  LYS GLN LEU LEU TYR LEU GLU LYS TYR ARG PRO LYS MSE
SEQRES  13 B  173  ARG LEU ARG PHE LYS ASP SER ASN GLY HIS ARG ASN ASN
SEQRES  14 B  173  CYS CYS ILE GLN
SEQRES   1 C  173  MSE ALA ARG MSE ASN ARG PRO ALA PRO VAL GLU VAL THR
SEQRES   2 C  173  TYR LYS ASN MSE ARG PHE LEU ILE THR HIS ASN PRO THR
SEQRES   3 C  173  ASN ALA THR LEU ASN LYS PHE ILE GLU GLU LEU LYS LYS
SEQRES   4 C  173  TYR GLY VAL THR THR ILE VAL ARG VAL CYS GLU ALA THR
SEQRES   5 C  173  TYR ASP THR THR LEU VAL GLU LYS GLU GLY ILE HIS VAL
SEQRES   6 C  173  LEU ASP TRP PRO PHE ASP ASP GLY ALA PRO PRO SER ASN
SEQRES   7 C  173  GLN ILE VAL ASP ASP TRP LEU SER LEU VAL LYS ILE LYS
SEQRES   8 C  173  PHE ARG GLU GLU PRO GLY CYS CYS ILE ALA VAL HIS SER
SEQRES   9 C  173  VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU VAL ALA LEU
SEQRES  10 C  173  ALA LEU ILE GLU GLY GLY MSE LYS TYR GLU ASP ALA VAL
SEQRES  11 C  173  GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA PHE ASN SER
SEQRES  12 C  173  LYS GLN LEU LEU TYR LEU GLU LYS TYR ARG PRO LYS MSE
SEQRES  13 C  173  ARG LEU ARG PHE LYS ASP SER ASN GLY HIS ARG ASN ASN
SEQRES  14 C  173  CYS CYS ILE GLN
SEQRES   1 D  173  MSE ALA ARG MSE ASN ARG PRO ALA PRO VAL GLU VAL THR
SEQRES   2 D  173  TYR LYS ASN MSE ARG PHE LEU ILE THR HIS ASN PRO THR
SEQRES   3 D  173  ASN ALA THR LEU ASN LYS PHE ILE GLU GLU LEU LYS LYS
SEQRES   4 D  173  TYR GLY VAL THR THR ILE VAL ARG VAL CYS GLU ALA THR
SEQRES   5 D  173  TYR ASP THR THR LEU VAL GLU LYS GLU GLY ILE HIS VAL
SEQRES   6 D  173  LEU ASP TRP PRO PHE ASP ASP GLY ALA PRO PRO SER ASN
SEQRES   7 D  173  GLN ILE VAL ASP ASP TRP LEU SER LEU VAL LYS ILE LYS
SEQRES   8 D  173  PHE ARG GLU GLU PRO GLY CYS CYS ILE ALA VAL HIS SER
SEQRES   9 D  173  VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU VAL ALA LEU
SEQRES  10 D  173  ALA LEU ILE GLU GLY GLY MSE LYS TYR GLU ASP ALA VAL
SEQRES  11 D  173  GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA PHE ASN SER
SEQRES  12 D  173  LYS GLN LEU LEU TYR LEU GLU LYS TYR ARG PRO LYS MSE
SEQRES  13 D  173  ARG LEU ARG PHE LYS ASP SER ASN GLY HIS ARG ASN ASN
SEQRES  14 D  173  CYS CYS ILE GLN
SEQRES   1 E  173  MSE ALA ARG MSE ASN ARG PRO ALA PRO VAL GLU VAL THR
SEQRES   2 E  173  TYR LYS ASN MSE ARG PHE LEU ILE THR HIS ASN PRO THR
SEQRES   3 E  173  ASN ALA THR LEU ASN LYS PHE ILE GLU GLU LEU LYS LYS
SEQRES   4 E  173  TYR GLY VAL THR THR ILE VAL ARG VAL CYS GLU ALA THR
SEQRES   5 E  173  TYR ASP THR THR LEU VAL GLU LYS GLU GLY ILE HIS VAL
SEQRES   6 E  173  LEU ASP TRP PRO PHE ASP ASP GLY ALA PRO PRO SER ASN
SEQRES   7 E  173  GLN ILE VAL ASP ASP TRP LEU SER LEU VAL LYS ILE LYS
SEQRES   8 E  173  PHE ARG GLU GLU PRO GLY CYS CYS ILE ALA VAL HIS SER
SEQRES   9 E  173  VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU VAL ALA LEU
SEQRES  10 E  173  ALA LEU ILE GLU GLY GLY MSE LYS TYR GLU ASP ALA VAL
SEQRES  11 E  173  GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA PHE ASN SER
SEQRES  12 E  173  LYS GLN LEU LEU TYR LEU GLU LYS TYR ARG PRO LYS MSE
SEQRES  13 E  173  ARG LEU ARG PHE LYS ASP SER ASN GLY HIS ARG ASN ASN
SEQRES  14 E  173  CYS CYS ILE GLN
SEQRES   1 F  173  MSE ALA ARG MSE ASN ARG PRO ALA PRO VAL GLU VAL THR
SEQRES   2 F  173  TYR LYS ASN MSE ARG PHE LEU ILE THR HIS ASN PRO THR
SEQRES   3 F  173  ASN ALA THR LEU ASN LYS PHE ILE GLU GLU LEU LYS LYS
SEQRES   4 F  173  TYR GLY VAL THR THR ILE VAL ARG VAL CYS GLU ALA THR
SEQRES   5 F  173  TYR ASP THR THR LEU VAL GLU LYS GLU GLY ILE HIS VAL
SEQRES   6 F  173  LEU ASP TRP PRO PHE ASP ASP GLY ALA PRO PRO SER ASN
SEQRES   7 F  173  GLN ILE VAL ASP ASP TRP LEU SER LEU VAL LYS ILE LYS
SEQRES   8 F  173  PHE ARG GLU GLU PRO GLY CYS CYS ILE ALA VAL HIS SER
SEQRES   9 F  173  VAL ALA GLY LEU GLY ARG ALA PRO VAL LEU VAL ALA LEU
SEQRES  10 F  173  ALA LEU ILE GLU GLY GLY MSE LYS TYR GLU ASP ALA VAL
SEQRES  11 F  173  GLN PHE ILE ARG GLN LYS ARG ARG GLY ALA PHE ASN SER
SEQRES  12 F  173  LYS GLN LEU LEU TYR LEU GLU LYS TYR ARG PRO LYS MSE
SEQRES  13 F  173  ARG LEU ARG PHE LYS ASP SER ASN GLY HIS ARG ASN ASN
SEQRES  14 F  173  CYS CYS ILE GLN
MODRES 1XM2 MSE A   17  MET  SELENOMETHIONINE
MODRES 1XM2 MSE A  124  MET  SELENOMETHIONINE
MODRES 1XM2 MSE A  156  MET  SELENOMETHIONINE
MODRES 1XM2 MSE B   17  MET  SELENOMETHIONINE
MODRES 1XM2 MSE B  124  MET  SELENOMETHIONINE
MODRES 1XM2 MSE B  156  MET  SELENOMETHIONINE
MODRES 1XM2 MSE C   17  MET  SELENOMETHIONINE
MODRES 1XM2 MSE C  124  MET  SELENOMETHIONINE
MODRES 1XM2 MSE C  156  MET  SELENOMETHIONINE
MODRES 1XM2 MSE D   17  MET  SELENOMETHIONINE
MODRES 1XM2 MSE D  124  MET  SELENOMETHIONINE
MODRES 1XM2 MSE D  156  MET  SELENOMETHIONINE
MODRES 1XM2 MSE E   17  MET  SELENOMETHIONINE
MODRES 1XM2 MSE E  124  MET  SELENOMETHIONINE
MODRES 1XM2 MSE E  156  MET  SELENOMETHIONINE
MODRES 1XM2 MSE F   17  MET  SELENOMETHIONINE
MODRES 1XM2 MSE F  124  MET  SELENOMETHIONINE
MODRES 1XM2 MSE F  156  MET  SELENOMETHIONINE
HET    MSE  A  17       8
HET    MSE  A 124       8
HET    MSE  A 156       8
HET    MSE  B  17       8
HET    MSE  B 124       8
HET    MSE  B 156       8
HET    MSE  C  17       8
HET    MSE  C 124       8
HET    MSE  C 156       8
HET    MSE  D  17       8
HET    MSE  D 124       8
HET    MSE  D 156       8
HET    MSE  E  17       8
HET    MSE  E 124       8
HET    MSE  E 156       8
HET    MSE  F  17       8
HET    MSE  F 124       8
HET    MSE  F 156       8
HET    SO4  A 181       5
HET    SO4  B 182       5
HET    SO4  C 183       5
HET    SO4  D 184       5
HET    SO4  E 185       5
HET    SO4  F 186       5
HETNAM     MSE SELENOMETHIONINE
HETNAM     SO4 SULFATE ION
FORMUL   1  MSE    18(C5 H11 N O2 SE)
FORMUL   7  SO4    6(O4 S 2-)
FORMUL  13  HOH   *92(H2 O)
HELIX    1   1 THR A   29  TYR A   40  1                                  12
HELIX    2   2 THR A   55  GLU A   61  1                                   7
HELIX    3   3 SER A   77  GLU A   95  1                                  19
HELIX    4   4 GLY A  109  GLY A  122  1                                  14
HELIX    5   5 LYS A  125  GLN A  135  1                                  11
HELIX    6   6 ASN A  142  TYR A  152  1                                  11
HELIX    7   7 THR B   29  TYR B   40  1                                  12
HELIX    8   8 ASP B   54  GLU B   61  1                                   8
HELIX    9   9 SER B   77  GLU B   95  1                                  19
HELIX   10  10 GLY B  109  GLY B  122  1                                  14
HELIX   11  11 LYS B  125  GLN B  135  1                                  11
HELIX   12  12 ASN B  142  TYR B  152  1                                  11
HELIX   13  13 THR C   29  TYR C   40  1                                  12
HELIX   14  14 ASP C   54  GLU C   61  1                                   8
HELIX   15  15 SER C   77  GLU C   95  1                                  19
HELIX   16  16 GLY C  109  GLY C  122  1                                  14
HELIX   17  17 LYS C  125  GLN C  135  1                                  11
HELIX   18  18 ASN C  142  TYR C  152  1                                  11
HELIX   19  19 THR D   29  GLY D   41  1                                  13
HELIX   20  20 THR D   55  GLU D   61  1                                   7
HELIX   21  21 SER D   77  GLU D   95  1                                  19
HELIX   22  22 GLY D  109  GLY D  122  1                                  14
HELIX   23  23 LYS D  125  GLN D  135  1                                  11
HELIX   24  24 ASN D  142  TYR D  152  1                                  11
HELIX   25  25 THR E   26  ALA E   28  5                                   3
HELIX   26  26 THR E   29  TYR E   40  1                                  12
HELIX   27  27 THR E   55  GLU E   61  1                                   7
HELIX   28  28 SER E   77  GLU E   95  1                                  19
HELIX   29  29 GLY E  109  GLY E  122  1                                  14
HELIX   30  30 LYS E  125  GLN E  135  1                                  11
HELIX   31  31 ASN E  142  TYR E  152  1                                  11
HELIX   32  32 LEU F   30  TYR F   40  1                                  11
HELIX   33  33 THR F   55  GLU F   61  1                                   7
HELIX   34  34 SER F   77  GLU F   95  1                                  19
HELIX   35  35 GLY F  109  GLY F  122  1                                  14
HELIX   36  36 LYS F  125  GLN F  135  1                                  11
HELIX   37  37 ASN F  142  TYR F  152  1                                  11
SHEET    1   A 5 VAL A  10  THR A  13  0
SHEET    2   A 5 ARG A  18  THR A  22 -1  O  PHE A  19   N  VAL A  12
SHEET    3   A 5 CYS A  99  HIS A 103  1  O  VAL A 102   N  LEU A  20
SHEET    4   A 5 VAL A  42  ARG A  47  1  N  VAL A  46   O  HIS A 103
SHEET    5   A 5 HIS A  64  ASP A  67  1  O  HIS A  64   N  ILE A  45
SHEET    1   B 5 VAL B  10  THR B  13  0
SHEET    2   B 5 ARG B  18  THR B  22 -1  O  PHE B  19   N  VAL B  12
SHEET    3   B 5 CYS B  99  HIS B 103  1  O  VAL B 102   N  LEU B  20
SHEET    4   B 5 VAL B  42  ARG B  47  1  N  VAL B  46   O  ALA B 101
SHEET    5   B 5 HIS B  64  ASP B  67  1  O  HIS B  64   N  ILE B  45
SHEET    1   C 5 VAL C  10  THR C  13  0
SHEET    2   C 5 ARG C  18  THR C  22 -1  O  PHE C  19   N  VAL C  12
SHEET    3   C 5 CYS C  99  HIS C 103  1  O  VAL C 102   N  LEU C  20
SHEET    4   C 5 VAL C  42  ARG C  47  1  N  VAL C  46   O  HIS C 103
SHEET    5   C 5 HIS C  64  ASP C  67  1  O  HIS C  64   N  ILE C  45
SHEET    1   D 5 VAL D  10  THR D  13  0
SHEET    2   D 5 ARG D  18  THR D  22 -1  O  PHE D  19   N  VAL D  12
SHEET    3   D 5 CYS D  99  HIS D 103  1  O  VAL D 102   N  LEU D  20
SHEET    4   D 5 VAL D  42  ARG D  47  1  N  THR D  44   O  ALA D 101
SHEET    5   D 5 HIS D  64  ASP D  67  1  O  LEU D  66   N  ARG D  47
SHEET    1   E 5 GLU E  11  THR E  13  0
SHEET    2   E 5 ARG E  18  THR E  22 -1  O  PHE E  19   N  VAL E  12
SHEET    3   E 5 CYS E  99  HIS E 103  1  O  VAL E 102   N  LEU E  20
SHEET    4   E 5 VAL E  42  ARG E  47  1  N  VAL E  46   O  ALA E 101
SHEET    5   E 5 HIS E  64  ASP E  67  1  O  HIS E  64   N  ILE E  45
SHEET    1   F 5 VAL F  10  THR F  13  0
SHEET    2   F 5 ARG F  18  THR F  22 -1  O  ILE F  21   N  VAL F  10
SHEET    3   F 5 CYS F  99  HIS F 103  1  O  VAL F 102   N  LEU F  20
SHEET    4   F 5 VAL F  42  ARG F  47  1  N  VAL F  46   O  ALA F 101
SHEET    5   F 5 HIS F  64  ASP F  67  1  O  LEU F  66   N  ARG F  47
LINK         C   ASN A  16                 N   MSE A  17     1555   1555  1.33
LINK         C   MSE A  17                 N   ARG A  18     1555   1555  1.33
LINK         C   GLY A 123                 N   MSE A 124     1555   1555  1.33
LINK         C   MSE A 124                 N   LYS A 125     1555   1555  1.33
LINK         C   LYS A 155                 N   MSE A 156     1555   1555  1.33
LINK         C   ASN B  16                 N   MSE B  17     1555   1555  1.33
LINK         C   MSE B  17                 N   ARG B  18     1555   1555  1.33
LINK         C   GLY B 123                 N   MSE B 124     1555   1555  1.33
LINK         C   MSE B 124                 N   LYS B 125     1555   1555  1.33
LINK         C   LYS B 155                 N   MSE B 156     1555   1555  1.33
LINK         C   ASN C  16                 N   MSE C  17     1555   1555  1.33
LINK         C   MSE C  17                 N   ARG C  18     1555   1555  1.33
LINK         C   GLY C 123                 N   MSE C 124     1555   1555  1.34
LINK         C   MSE C 124                 N   LYS C 125     1555   1555  1.33
LINK         C   LYS C 155                 N   MSE C 156     1555   1555  1.33
LINK         C   ASN D  16                 N   MSE D  17     1555   1555  1.33
LINK         C   MSE D  17                 N   ARG D  18     1555   1555  1.33
LINK         C   GLY D 123                 N   MSE D 124     1555   1555  1.33
LINK         C   MSE D 124                 N   LYS D 125     1555   1555  1.33
LINK         C   LYS D 155                 N   MSE D 156     1555   1555  1.33
LINK         C   ASN E  16                 N   MSE E  17     1555   1555  1.34
LINK         C   MSE E  17                 N   ARG E  18     1555   1555  1.33
LINK         C   GLY E 123                 N   MSE E 124     1555   1555  1.33
LINK         C   MSE E 124                 N   LYS E 125     1555   1555  1.33
LINK         C   LYS E 155                 N   MSE E 156     1555   1555  1.34
LINK         C   ASN F  16                 N   MSE F  17     1555   1555  1.34
LINK         C   MSE F  17                 N   ARG F  18     1555   1555  1.33
LINK         C   GLY F 123                 N   MSE F 124     1555   1555  1.33
LINK         C   MSE F 124                 N   LYS F 125     1555   1555  1.33
LINK         C   LYS F 155                 N   MSE F 156     1555   1555  1.34
CISPEP   1 TYR A   14    LYS A   15          0        -1.25
CISPEP   2 TYR B   14    LYS B   15          0        -1.51
CISPEP   3 TYR C   14    LYS C   15          0        -0.92
CISPEP   4 TYR D   14    LYS D   15          0        -0.71
CISPEP   5 TYR E   14    LYS E   15          0        -1.17
CISPEP   6 TYR F   14    LYS F   15          0        -1.71
SITE     1 AC1  8 SER A 104  VAL A 105  ALA A 106  GLY A 107
SITE     2 AC1  8 LEU A 108  GLY A 109  ARG A 110  HOH A 206
SITE     1 AC2  8 ASP B  72  SER B 104  VAL B 105  ALA B 106
SITE     2 AC2  8 GLY B 107  LEU B 108  GLY B 109  ARG B 110
SITE     1 AC3  7 SER C 104  VAL C 105  ALA C 106  GLY C 107
SITE     2 AC3  7 LEU C 108  GLY C 109  ARG C 110
SITE     1 AC4  6 SER D 104  ALA D 106  GLY D 107  LEU D 108
SITE     2 AC4  6 GLY D 109  ARG D 110
SITE     1 AC5  6 SER E 104  VAL E 105  ALA E 106  LEU E 108
SITE     2 AC5  6 GLY E 109  ARG E 110
SITE     1 AC6  7 SER F 104  VAL F 105  ALA F 106  GLY F 107
SITE     2 AC6  7 LEU F 108  GLY F 109  ARG F 110
CRYST1   59.290   84.760  122.180  90.00  99.79  90.00 P 1 21 1     12
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.016866  0.000000  0.002910        0.00000
SCALE2      0.000000  0.011798  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008306        0.00000
      
PROCHECK
Go to PROCHECK summary
 References