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PDBsum entry 2ahs

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2ahs
Jmol
Contents
Protein chain
281 a.a.
Ligands
EDO ×8
Metals
_CL ×9
_NA
Waters ×479
HEADER    HYDROLASE                               28-JUL-05   2AHS
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN TYROSINE RECEPTOR
TITLE    2 PHOSPHATASE BETA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE BETA;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: PTPR-BETA;
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE BETA, R-PTP-BETA;
COMPND   6 EC: 3.1.3.48;
COMPND   7 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: PTPRB, PTPB;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)-R3;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P2
KEYWDS    TYROSINE RECEPTOR PHOSPHATASE, BETA, HUMAN, STRUCTURAL GENOMICS,
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.UGOCHUKWU,J.ESWARAN,A.BARR,O.GILEADI,F.SOBOTT,N.BURGESS,L.BALL,
AUTHOR   2 J.BRAY,F.VON DELFT,J.DEBRECZENI,G.BUNKOCZI,A.TURNBULL,S.DAS,
AUTHOR   3 J.WEIGELT,A.EDWARDS,C.ARROWSMITH,M.SUNDSTROM,S.KNAPP,STRUCTURAL
AUTHOR   4 GENOMICS CONSORTIUM (SGC)
REVDAT   8   28-MAR-12 2AHS    1       JRNL   VERSN
REVDAT   7   11-MAY-11 2AHS    1       REMARK
REVDAT   6   05-MAY-10 2AHS    1       AUTHOR
REVDAT   5   09-JUN-09 2AHS    1       REVDAT
REVDAT   4   24-FEB-09 2AHS    1       VERSN
REVDAT   3   27-JAN-09 2AHS    1       JRNL
REVDAT   2   16-AUG-05 2AHS    1       REMARK
REVDAT   1   09-AUG-05 2AHS    0
JRNL        AUTH   A.J.BARR,E.UGOCHUKWU,W.H.LEE,O.N.KING,P.FILIPPAKOPOULOS,
JRNL        AUTH 2 I.ALFANO,P.SAVITSKY,N.A.BURGESS-BROWN,S.MULLER,S.KNAPP
JRNL        TITL   LARGE-SCALE STRUCTURAL ANALYSIS OF THE CLASSICAL HUMAN
JRNL        TITL 2 PROTEIN TYROSINE PHOSPHATOME.
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 136   352 2009
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   19167335
JRNL        DOI    10.1016/J.CELL.2008.11.038
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.40
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 44882
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 + TEST SET) : 0.155
REMARK   3   R VALUE            (WORKING SET) : 0.152
REMARK   3   FREE R VALUE                     : 0.206
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2394
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3024
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.61
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1830
REMARK   3   BIN FREE R VALUE SET COUNT          : 173
REMARK   3   BIN FREE R VALUE                    : 0.2900
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4444
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 42
REMARK   3   SOLVENT ATOMS            : 479
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.19000
REMARK   3    B22 (A**2) : -0.19000
REMARK   3    B33 (A**2) : 0.28000
REMARK   3    B12 (A**2) : -0.09000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.147
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.148
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.573
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4643 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  4128 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6311 ; 1.337 ; 1.939
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9554 ; 0.895 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   570 ; 6.312 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   241 ;31.211 ;23.444
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   759 ;13.223 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;13.063 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   684 ; 0.121 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5215 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   984 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   853 ; 0.202 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4201 ; 0.186 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2226 ; 0.173 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2585 ; 0.081 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   344 ; 0.219 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.295 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    57 ; 0.288 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    33 ; 0.467 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2785 ; 5.038 ; 5.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1127 ; 2.003 ; 5.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4525 ; 6.752 ; 7.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1936 ; 9.518 ; 9.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1776 ;11.135 ;11.000
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 9
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A   1705       A    1745      5
REMARK   3           1     B   1705       B    1745      5
REMARK   3           2     A   1756       A    1803      5
REMARK   3           2     B   1756       B    1803      5
REMARK   3           3     A   1804       A    1810      6
REMARK   3           3     B   1804       B    1810      6
REMARK   3           4     A   1811       A    1816      5
REMARK   3           4     B   1811       B    1816      5
REMARK   3           5     A   1817       A    1822      6
REMARK   3           5     B   1817       B    1822      6
REMARK   3           6     A   1823       A    1851      5
REMARK   3           6     B   1823       B    1851      5
REMARK   3           7     A   1855       A    1869      5
REMARK   3           7     B   1855       B    1869      5
REMARK   3           8     A   1871       A    1927      5
REMARK   3           8     B   1871       B    1927      5
REMARK   3           9     A   1930       A    1962      5
REMARK   3           9     B   1930       B    1962      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1340 ;  0.18 ;  0.50
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2271 ;  0.54 ;  5.00
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1340 ;  1.35 ;  2.00
REMARK   3   LOOSE THERMAL      1    A (A**2):   2271 ;  3.30 ; 10.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    11        A   291
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6829  68.3722   6.6808
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0885 T22:  -0.0046
REMARK   3      T33:  -0.1080 T12:  -0.0393
REMARK   3      T13:  -0.0015 T23:  -0.0400
REMARK   3    L TENSOR
REMARK   3      L11:   1.2860 L22:   1.0774
REMARK   3      L33:   0.9823 L12:   0.3136
REMARK   3      L13:  -0.2653 L23:  -0.0778
REMARK   3    S TENSOR
REMARK   3      S11:   0.1592 S12:  -0.2335 S13:  -0.0483
REMARK   3      S21:   0.2038 S22:  -0.1440 S23:   0.0710
REMARK   3      S31:  -0.0519 S32:   0.0698 S33:  -0.0152
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    17        B   290
REMARK   3    ORIGIN FOR THE GROUP (A):   6.2525  35.4469   1.3754
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0722 T22:  -0.0167
REMARK   3      T33:  -0.0580 T12:  -0.0088
REMARK   3      T13:  -0.0216 T23:   0.0408
REMARK   3    L TENSOR
REMARK   3      L11:   1.7062 L22:   1.0150
REMARK   3      L33:   1.4274 L12:   0.2407
REMARK   3      L13:  -0.3890 L23:   0.2347
REMARK   3    S TENSOR
REMARK   3      S11:   0.0105 S12:  -0.2621 S13:  -0.2249
REMARK   3      S21:   0.1605 S22:   0.0220 S23:  -0.0635
REMARK   3      S31:   0.2288 S32:   0.0189 S33:  -0.0325
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2AHS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-05.
REMARK 100 THE RCSB ID CODE IS RCSB033910.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-05
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47341
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.400
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
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) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1
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: 1RPM.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, ETHYLENE GLYCOL, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K, PH 7.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
REMARK 290       7555   Y,X,-Z+1/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+2/3
REMARK 290      10555   -Y,-X,-Z+5/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+1/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.85633
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      119.71267
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       89.78450
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      149.64083
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.92817
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       59.85633
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      119.71267
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      149.64083
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       89.78450
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       29.92817
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: 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 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     GLY A  1677
REMARK 465     PRO A  1678
REMARK 465     LEU A  1679
REMARK 465     GLY A  1680
REMARK 465     SER A  1681
REMARK 465     PRO A  1682
REMARK 465     GLY A  1683
REMARK 465     ILE A  1684
REMARK 465     PRO A  1685
REMARK 465     ASN A  1686
REMARK 465     LYS A  1968
REMARK 465     LEU A  1969
REMARK 465     ARG A  1970
REMARK 465     SER A  1971
REMARK 465     GLY B  1677
REMARK 465     PRO B  1678
REMARK 465     LEU B  1679
REMARK 465     GLY B  1680
REMARK 465     SER B  1681
REMARK 465     PRO B  1682
REMARK 465     GLY B  1683
REMARK 465     ILE B  1684
REMARK 465     PRO B  1685
REMARK 465     ASN B  1686
REMARK 465     GLN B  1687
REMARK 465     PHE B  1688
REMARK 465     GLU B  1689
REMARK 465     GLY B  1690
REMARK 465     HIS B  1691
REMARK 465     PHE B  1692
REMARK 465     ASP B  1928
REMARK 465     SER B  1929
REMARK 465     ARG B  1967
REMARK 465     LYS B  1968
REMARK 465     LEU B  1969
REMARK 465     ARG B  1970
REMARK 465     SER B  1971
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     MET A1693    CE
REMARK 470     LYS A1694    NZ
REMARK 470     ASP A1750    CG   OD1  OD2
REMARK 470     ASP A1751    CG   OD1  OD2
REMARK 470     ARG A1809    CZ   NH1  NH2
REMARK 470     GLU A1852    CG   CD   OE1  OE2
REMARK 470     GLN A1853    CD   OE1  NE2
REMARK 470     LYS A1927    CE   NZ
REMARK 470     ASP A1928    CG   OD1  OD2
REMARK 470     SER A1929    OG
REMARK 470     LYS B1694    CG   CD   CE   NZ
REMARK 470     LEU B1695    CG   CD1  CD2
REMARK 470     GLN B1696    CG   CD   OE1  NE2
REMARK 470     SER B1699    OG
REMARK 470     LEU B1702    CG   CD1  CD2
REMARK 470     LYS B1705    CG   CD   CE   NZ
REMARK 470     GLU B1708    CD   OE1  OE2
REMARK 470     LYS B1711    CD   CE   NZ
REMARK 470     LYS B1807    CG   CD   CE   NZ
REMARK 470     HIS B1871    CG   ND1  CD2  CE1  NE2
REMARK 470     GLU B1875    CD   OE1  OE2
REMARK 470     ARG B1961    CD   NE   CZ   NH1  NH2
REMARK 470     ARG B1965    CD   NE   CZ   NH1  NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH B   161     O    HOH B   643              1.80
REMARK 500   O    HOH A   632     O    HOH A   646              2.00
REMARK 500   O    HOH B    61     O    HOH B   510              2.09
REMARK 500   O    HOH A   160     O    HOH A   518              2.09
REMARK 500   O    HOH B    24     O    HOH B   478              2.13
REMARK 500   O    HOH A   361     O    HOH A   655              2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   171     O    HOH A   624    12565     1.56
REMARK 500   O    HOH A   624     O    HOH A   624    12565     1.75
REMARK 500   O    HOH A   616     O    HOH B   114     8665     1.83
REMARK 500   O    HOH A   616     O    HOH B   204     8665     2.02
REMARK 500   O    HOH A   191     O    HOH B    40     8665     2.02
REMARK 500   O    HOH A   195     O    HOH B   643    10664     2.16
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    ASP A1751      -11.62     85.84
REMARK 500    ARG A1770       66.57   -117.97
REMARK 500    VAL A1801       50.17   -111.81
REMARK 500    GLN A1853       75.73   -161.31
REMARK 500    SER A1894       56.64   -119.26
REMARK 500    CYS A1904     -123.33   -131.09
REMARK 500    VAL A1908      -49.80   -133.44
REMARK 500    VAL A1947       86.17     60.38
REMARK 500    ARG B1770       51.17   -116.36
REMARK 500    ASP B1819     -141.17   -118.37
REMARK 500    CYS B1904     -127.94   -131.13
REMARK 500    VAL B1908      -61.41   -132.19
REMARK 500    VAL B1947       87.14     67.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    LYS A1927         1.7      L          L   EXPECTING SP3
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 A 616        DISTANCE =  6.06 ANGSTROMS
REMARK 525    HOH A 617        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH A 618        DISTANCE =  7.79 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 722
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 725
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 726
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 728
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 729
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 734
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 737
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 741
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RPM   RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF DOMAIN 1 OF RECEPTOR PROTEIN-
REMARK 900 TYROSINE PHOSPHATASE MU
DBREF  2AHS A 1686  1971  UNP    P23467   PTPRB_HUMAN   1686   1971
DBREF  2AHS B 1686  1971  UNP    P23467   PTPRB_HUMAN   1686   1971
SEQADV 2AHS GLY A 1677  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS PRO A 1678  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS LEU A 1679  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS GLY A 1680  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS SER A 1681  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS PRO A 1682  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS GLY A 1683  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS ILE A 1684  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS PRO A 1685  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS GLY B 1677  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS PRO B 1678  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS LEU B 1679  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS GLY B 1680  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS SER B 1681  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS PRO B 1682  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS GLY B 1683  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS ILE B 1684  UNP  P23467              CLONING ARTIFACT
SEQADV 2AHS PRO B 1685  UNP  P23467              CLONING ARTIFACT
SEQRES   1 A  295  GLY PRO LEU GLY SER PRO GLY ILE PRO ASN GLN PHE GLU
SEQRES   2 A  295  GLY HIS PHE MET LYS LEU GLN ALA ASP SER ASN TYR LEU
SEQRES   3 A  295  LEU SER LYS GLU TYR GLU GLU LEU LYS ASP VAL GLY ARG
SEQRES   4 A  295  ASN GLN SER CYS ASP ILE ALA LEU LEU PRO GLU ASN ARG
SEQRES   5 A  295  GLY LYS ASN ARG TYR ASN ASN ILE LEU PRO TYR ASP ALA
SEQRES   6 A  295  THR ARG VAL LYS LEU SER ASN VAL ASP ASP ASP PRO CYS
SEQRES   7 A  295  SER ASP TYR ILE ASN ALA SER TYR ILE PRO GLY ASN ASN
SEQRES   8 A  295  PHE ARG ARG GLU TYR ILE VAL THR GLN GLY PRO LEU PRO
SEQRES   9 A  295  GLY THR LYS ASP ASP PHE TRP LYS MET VAL TRP GLU GLN
SEQRES  10 A  295  ASN VAL HIS ASN ILE VAL MET VAL THR GLN CYS VAL GLU
SEQRES  11 A  295  LYS GLY ARG VAL LYS CYS ASP HIS TYR TRP PRO ALA ASP
SEQRES  12 A  295  GLN ASP SER LEU TYR TYR GLY ASP LEU ILE LEU GLN MET
SEQRES  13 A  295  LEU SER GLU SER VAL LEU PRO GLU TRP THR ILE ARG GLU
SEQRES  14 A  295  PHE LYS ILE CYS GLY GLU GLU GLN LEU ASP ALA HIS ARG
SEQRES  15 A  295  LEU ILE ARG HIS PHE HIS TYR THR VAL TRP PRO ASP HIS
SEQRES  16 A  295  GLY VAL PRO GLU THR THR GLN SER LEU ILE GLN PHE VAL
SEQRES  17 A  295  ARG THR VAL ARG ASP TYR ILE ASN ARG SER PRO GLY ALA
SEQRES  18 A  295  GLY PRO THR VAL VAL HIS CYS SER ALA GLY VAL GLY ARG
SEQRES  19 A  295  THR GLY THR PHE ILE ALA LEU ASP ARG ILE LEU GLN GLN
SEQRES  20 A  295  LEU ASP SER LYS ASP SER VAL ASP ILE TYR GLY ALA VAL
SEQRES  21 A  295  HIS ASP LEU ARG LEU HIS ARG VAL HIS MET VAL GLN THR
SEQRES  22 A  295  GLU CYS GLN TYR VAL TYR LEU HIS GLN CYS VAL ARG ASP
SEQRES  23 A  295  VAL LEU ARG ALA ARG LYS LEU ARG SER
SEQRES   1 B  295  GLY PRO LEU GLY SER PRO GLY ILE PRO ASN GLN PHE GLU
SEQRES   2 B  295  GLY HIS PHE MET LYS LEU GLN ALA ASP SER ASN TYR LEU
SEQRES   3 B  295  LEU SER LYS GLU TYR GLU GLU LEU LYS ASP VAL GLY ARG
SEQRES   4 B  295  ASN GLN SER CYS ASP ILE ALA LEU LEU PRO GLU ASN ARG
SEQRES   5 B  295  GLY LYS ASN ARG TYR ASN ASN ILE LEU PRO TYR ASP ALA
SEQRES   6 B  295  THR ARG VAL LYS LEU SER ASN VAL ASP ASP ASP PRO CYS
SEQRES   7 B  295  SER ASP TYR ILE ASN ALA SER TYR ILE PRO GLY ASN ASN
SEQRES   8 B  295  PHE ARG ARG GLU TYR ILE VAL THR GLN GLY PRO LEU PRO
SEQRES   9 B  295  GLY THR LYS ASP ASP PHE TRP LYS MET VAL TRP GLU GLN
SEQRES  10 B  295  ASN VAL HIS ASN ILE VAL MET VAL THR GLN CYS VAL GLU
SEQRES  11 B  295  LYS GLY ARG VAL LYS CYS ASP HIS TYR TRP PRO ALA ASP
SEQRES  12 B  295  GLN ASP SER LEU TYR TYR GLY ASP LEU ILE LEU GLN MET
SEQRES  13 B  295  LEU SER GLU SER VAL LEU PRO GLU TRP THR ILE ARG GLU
SEQRES  14 B  295  PHE LYS ILE CYS GLY GLU GLU GLN LEU ASP ALA HIS ARG
SEQRES  15 B  295  LEU ILE ARG HIS PHE HIS TYR THR VAL TRP PRO ASP HIS
SEQRES  16 B  295  GLY VAL PRO GLU THR THR GLN SER LEU ILE GLN PHE VAL
SEQRES  17 B  295  ARG THR VAL ARG ASP TYR ILE ASN ARG SER PRO GLY ALA
SEQRES  18 B  295  GLY PRO THR VAL VAL HIS CYS SER ALA GLY VAL GLY ARG
SEQRES  19 B  295  THR GLY THR PHE ILE ALA LEU ASP ARG ILE LEU GLN GLN
SEQRES  20 B  295  LEU ASP SER LYS ASP SER VAL ASP ILE TYR GLY ALA VAL
SEQRES  21 B  295  HIS ASP LEU ARG LEU HIS ARG VAL HIS MET VAL GLN THR
SEQRES  22 B  295  GLU CYS GLN TYR VAL TYR LEU HIS GLN CYS VAL ARG ASP
SEQRES  23 B  295  VAL LEU ARG ALA ARG LYS LEU ARG SER
HET     CL  B 801       1
HET     CL  A 802       1
HET     CL  A 803       1
HET     CL  B 804       1
HET     CL  B 805       1
HET     CL  A 807       1
HET     CL  B 808       1
HET     CL  B 809       1
HET     CL  B 810       1
HET     NA  A 811       1
HET    EDO  A 722       4
HET    EDO  A 725       4
HET    EDO  A 726       4
HET    EDO  B 728       4
HET    EDO  A 729       4
HET    EDO  B 734       4
HET    EDO  B 737       4
HET    EDO  B 741       4
HETNAM      CL CHLORIDE ION
HETNAM      NA SODIUM ION
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3   CL    9(CL 1-)
FORMUL  12   NA    NA 1+
FORMUL  13  EDO    8(C2 H6 O2)
FORMUL  21  HOH   *479(H2 O)
HELIX    1   1 GLN A 1687  LEU A 1710  1                                  24
HELIX    2   2 CYS A 1719  LEU A 1724  1                                   6
HELIX    3   3 PRO A 1725  ASN A 1731  5                                   7
HELIX    4   4 ASP A 1752  SER A 1755  5                                   4
HELIX    5   5 LEU A 1779  GLY A 1781  5                                   3
HELIX    6   6 THR A 1782  GLN A 1793  1                                  12
HELIX    7   7 THR A 1876  ARG A 1893  1                                  18
HELIX    8   8 VAL A 1908  ASP A 1928  1                                  21
HELIX    9   9 ASP A 1931  ARG A 1943  1                                  13
HELIX   10  10 THR A 1949  ALA A 1966  1                                  18
HELIX   11  11 LYS B 1694  LEU B 1710  1                                  17
HELIX   12  12 ASP B 1720  ASN B 1731  5                                  12
HELIX   13  13 THR B 1782  GLN B 1793  1                                  12
HELIX   14  14 THR B 1876  ARG B 1893  1                                  18
HELIX   15  15 VAL B 1908  SER B 1926  1                                  19
HELIX   16  16 ASP B 1931  ARG B 1943  1                                  13
HELIX   17  17 THR B 1949  ARG B 1965  1                                  17
SHEET    1   A 9 ARG A1743  LYS A1745  0
SHEET    2   A 9 TYR A1757  ILE A1763 -1  O  ALA A1760   N  VAL A1744
SHEET    3   A 9 TYR A1772  THR A1775 -1  O  VAL A1774   N  SER A1761
SHEET    4   A 9 THR A1900  HIS A1903  1  O  VAL A1902   N  ILE A1773
SHEET    5   A 9 ASN A1797  MET A1800  1  N  VAL A1799   O  VAL A1901
SHEET    6   A 9 ARG A1858  TYR A1865  1  O  PHE A1863   N  MET A1800
SHEET    7   A 9 TRP A1841  GLY A1850 -1  N  THR A1842   O  HIS A1864
SHEET    8   A 9 LEU A1828  VAL A1837 -1  N  ILE A1829   O  CYS A1849
SHEET    9   A 9 LEU A1823  TYR A1825 -1  N  LEU A1823   O  LEU A1830
SHEET    1   B 2 VAL A1805  GLU A1806  0
SHEET    2   B 2 ARG A1809  VAL A1810 -1  O  ARG A1809   N  GLU A1806
SHEET    1   C 9 ARG B1743  LYS B1745  0
SHEET    2   C 9 TYR B1757  ILE B1763 -1  O  ALA B1760   N  VAL B1744
SHEET    3   C 9 TYR B1772  THR B1775 -1  O  VAL B1774   N  SER B1761
SHEET    4   C 9 THR B1900  HIS B1903  1  O  VAL B1902   N  ILE B1773
SHEET    5   C 9 ASN B1797  MET B1800  1  N  VAL B1799   O  VAL B1901
SHEET    6   C 9 GLN B1853  TYR B1865  1  O  PHE B1863   N  ILE B1798
SHEET    7   C 9 TRP B1841  GLY B1850 -1  N  PHE B1846   O  ILE B1860
SHEET    8   C 9 LEU B1828  VAL B1837 -1  N  ILE B1829   O  CYS B1849
SHEET    9   C 9 LEU B1823  TYR B1825 -1  N  LEU B1823   O  LEU B1830
SHEET    1   D 2 VAL B1805  GLU B1806  0
SHEET    2   D 2 ARG B1809  VAL B1810 -1  O  ARG B1809   N  GLU B1806
LINK         O   ARG A1743                NA    NA A 811     1555   1555  2.77
CISPEP   1 LYS A 1927    ASP A 1928          0       -22.14
SITE     1 AC1  2 GLU B1726  CYS B1754
SITE     1 AC2  1 ARG A1770
SITE     1 AC3  1 GLU B1840
SITE     1 AC4  3 SER B1834  SER B1836  ILE B1843
SITE     1 AC5  3 HOH A 201  ASP A1720  LEU A1723
SITE     1 AC6  3 HOH A  71  ARG B1732  TYR B1733
SITE     1 AC7  2 GLN B1717  LEU B1941
SITE     1 AC8  1 LYS B1788
SITE     1 AC9  2 ALA A1741  ARG A1743
SITE     1 BC1  7 HOH A 344  HOH A 650  CYS A1719  ASN A1735
SITE     2 BC1  7 ILE A1736  LEU A1737  VAL A1944
SITE     1 BC2  4 TYR A1733  ASN A1735  ILE A1736  GLN A1948
SITE     1 BC3  7 HOH A 518  HOH A 595  VAL A1873  PRO A1874
SITE     2 BC3  7 GLU A1875  TYR A1955  GLN A1958
SITE     1 BC4  3 PRO B1839  GLU B1840  TRP B1841
SITE     1 BC5  2 ALA A1856  ARG A1858
SITE     1 BC6  5 CYS B1719  ASN B1735  ILE B1736  LEU B1737
SITE     2 BC6  5 VAL B1944
SITE     1 BC7  3 GLY B1765  PHE B1768  ARG B1769
SITE     1 BC8  4 HOH A 637  HOH B 213  ALA B1741  ARG B1770
CRYST1  123.368  123.368  179.569  90.00  90.00 120.00 P 61 2 2     24
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      0.008106  0.004680  0.000000        0.00000
SCALE2      0.000000  0.009360  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005569        0.00000
      
PROCHECK
Go to PROCHECK summary
 References