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PDBsum entry 2v5y

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Hydrolase PDB id
2v5y
Jmol
Contents
Protein chain
564 a.a.
Ligands
NAG ×7
Metals
_NA ×2
HEADER    HYDROLASE                               11-JUL-07   2V5Y
TITLE     CRYSTAL STRUCTURE OF THE RECEPTOR PROTEIN TYROSINE
TITLE    2 PHOSPHATASE MU ECTODOMAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE MU;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR REGION, RESIDUES 21-742;
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE MU, R-PTP-MU;
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 ORGAN: LUNG;
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK-293S GNTI-;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: EPISOMAL PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS    MEMBRANE, RECEPTOR, HYDROLASE, GLYCOPROTEIN, RECEPTOR PROTEIN
KEYWDS   2 TYROSINE PHOSPHATASE, CELL ADHESION, TRANSMEMBRANE, PROTEIN
KEYWDS   3 PHOSPHATASE, EXTRACELLULAR REGION, IMMUNOGLOBULIN DOMAIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.R.ARICESCU,C.SIEBOLD,K.CHOUDHURI,V.T.CHANG,W.LU,S.J.DAVIS,
AUTHOR   2 P.A.VAN DER MERWE,E.Y.JONES
REVDAT   3   13-JUL-11 2V5Y    1       VERSN
REVDAT   2   24-FEB-09 2V5Y    1       VERSN
REVDAT   1   11-SEP-07 2V5Y    0
JRNL        AUTH   A.R.ARICESCU,C.SIEBOLD,K.CHOUDHURI,V.T.CHANG,W.LU,S.J.DAVIS,
JRNL        AUTH 2 P.A.VAN DER MERWE,E.Y.JONES
JRNL        TITL   STRUCTURE OF A TYROSINE PHOSPHATASE ADHESIVE INTERACTION
JRNL        TITL 2 REVEALS A SPACER-CLAMP MECHANISM.
JRNL        REF    SCIENCE                       V. 317  1217 2007
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   17761881
JRNL        DOI    10.1126/SCIENCE.1144646
REMARK   2
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 3.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 17792
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) : 0.246
REMARK   3   R VALUE            (WORKING SET) : 0.242
REMARK   3   FREE R VALUE                     : 0.320
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 969
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) : 3.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1294
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990
REMARK   3   BIN FREE R VALUE SET COUNT          : 67
REMARK   3   BIN FREE R VALUE                    : 0.3390
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4423
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 100
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -5.03000
REMARK   3    B22 (A**2) : 5.12000
REMARK   3    B33 (A**2) : -1.63000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -1.94000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.509
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.409
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.964
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.887
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.810
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4649 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  3137 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6350 ; 1.243 ; 1.971
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7590 ; 0.836 ; 3.002
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   562 ; 7.602 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   211 ;34.455 ;23.981
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   713 ;19.584 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;16.173 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   703 ; 0.074 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5208 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   926 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   947 ; 0.187 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3198 ; 0.187 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2206 ; 0.181 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2678 ; 0.087 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    97 ; 0.154 ; 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):    18 ; 0.175 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.223 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.134 ; 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):  2811 ; 0.481 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1134 ; 0.041 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4576 ; 0.858 ; 3.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1913 ; 0.378 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1774 ; 0.752 ; 3.000
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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 6
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     2        A    61
REMARK   3    ORIGIN FOR THE GROUP (A): 222.0240  71.0690  12.4170
REMARK   3    T TENSOR
REMARK   3      T11:   0.0498 T22:   0.1982
REMARK   3      T33:   0.2330 T12:  -0.0950
REMARK   3      T13:  -0.1414 T23:   0.1101
REMARK   3    L TENSOR
REMARK   3      L11:   1.5380 L22:   6.3608
REMARK   3      L33:   6.8369 L12:   0.4844
REMARK   3      L13:   0.1161 L23:  -2.1212
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0947 S12:  -0.1164 S13:   0.3168
REMARK   3      S21:   0.5441 S22:  -0.3318 S23:  -0.9645
REMARK   3      S31:  -0.4331 S32:   0.4351 S33:   0.4265
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 :   A    62        A   169
REMARK   3    ORIGIN FOR THE GROUP (A): 209.8420  66.2950   7.8270
REMARK   3    T TENSOR
REMARK   3      T11:   0.0866 T22:   0.2105
REMARK   3      T33:   0.1371 T12:  -0.0025
REMARK   3      T13:   0.0195 T23:   0.0046
REMARK   3    L TENSOR
REMARK   3      L11:   2.2139 L22:   2.4385
REMARK   3      L33:   1.8778 L12:   0.4260
REMARK   3      L13:   1.1707 L23:   0.3036
REMARK   3    S TENSOR
REMARK   3      S11:   0.0411 S12:  -0.0340 S13:   0.0608
REMARK   3      S21:   0.1594 S22:  -0.0954 S23:  -0.1960
REMARK   3      S31:   0.0228 S32:   0.1182 S33:   0.0543
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   170        A   277
REMARK   3    ORIGIN FOR THE GROUP (A): 183.6450  63.5490   8.1200
REMARK   3    T TENSOR
REMARK   3      T11:   0.1236 T22:   0.2322
REMARK   3      T33:   0.1355 T12:  -0.0424
REMARK   3      T13:   0.0966 T23:   0.0453
REMARK   3    L TENSOR
REMARK   3      L11:   5.0095 L22:   0.2239
REMARK   3      L33:   0.2753 L12:  -0.5496
REMARK   3      L13:  -0.4291 L23:   0.2446
REMARK   3    S TENSOR
REMARK   3      S11:   0.0413 S12:  -0.2069 S13:   0.0504
REMARK   3      S21:   0.0423 S22:   0.0538 S23:  -0.0393
REMARK   3      S31:   0.1479 S32:  -0.0160 S33:  -0.0951
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   278        A   351
REMARK   3    ORIGIN FOR THE GROUP (A): 152.3730  69.6730  13.6350
REMARK   3    T TENSOR
REMARK   3      T11:   0.0686 T22:   0.2047
REMARK   3      T33:  -0.0114 T12:  -0.0339
REMARK   3      T13:   0.0827 T23:  -0.0786
REMARK   3    L TENSOR
REMARK   3      L11:  12.6624 L22:   1.0087
REMARK   3      L33:   1.3632 L12:   0.3467
REMARK   3      L13:  -2.0053 L23:   0.9673
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0692 S12:  -0.2569 S13:  -0.1633
REMARK   3      S21:  -0.1912 S22:   0.0529 S23:  -0.1352
REMARK   3      S31:   0.2070 S32:   0.1061 S33:   0.0163
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   352        A   460
REMARK   3    ORIGIN FOR THE GROUP (A): 111.3160  59.4700  23.7950
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0497 T22:   0.2663
REMARK   3      T33:   0.0447 T12:  -0.1054
REMARK   3      T13:   0.0906 T23:  -0.1387
REMARK   3    L TENSOR
REMARK   3      L11:  13.2302 L22:   2.4209
REMARK   3      L33:   1.3778 L12:   4.5408
REMARK   3      L13:  -1.9648 L23:  -0.4949
REMARK   3    S TENSOR
REMARK   3      S11:   0.1667 S12:  -0.6786 S13:  -0.0326
REMARK   3      S21:  -0.0347 S22:  -0.3129 S23:   0.1826
REMARK   3      S31:   0.0244 S32:  -0.0771 S33:   0.1461
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   461        A   568
REMARK   3    ORIGIN FOR THE GROUP (A):  65.4420  49.8100  33.8920
REMARK   3    T TENSOR
REMARK   3      T11:   0.1178 T22:   0.1930
REMARK   3      T33:   0.0272 T12:  -0.0025
REMARK   3      T13:   0.0579 T23:  -0.0306
REMARK   3    L TENSOR
REMARK   3      L11:   9.4969 L22:   1.8446
REMARK   3      L33:   3.8995 L12:  -0.5533
REMARK   3      L13:  -2.6458 L23:   0.1055
REMARK   3    S TENSOR
REMARK   3      S11:   0.0536 S12:  -0.2293 S13:   0.0213
REMARK   3      S21:  -0.1184 S22:   0.1266 S23:   0.0727
REMARK   3      S31:  -0.0840 S32:   0.2741 S33:  -0.1801
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2V5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-07.
REMARK 100 THE PDBE ID CODE IS EBI-33160.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19030
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.10
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : 5.3
REMARK 200  R MERGE                    (I) : 0.16
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.6
REMARK 200  R MERGE FOR SHELL          (I) : 0.61
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2C9A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS-PROPANE, PH 6.5
REMARK 280  22.5% (W/V) PEG-SMEAR, 200MM K-THIOCYANATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       83.66800
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.66250
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       83.66800
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.66250
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.9 KCAL/MOL
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   BIOMT1   2 -1.000000  0.000000  0.000000      334.67200
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     GLU A     1
REMARK 465     PRO A   508
REMARK 465     GLU A   509
REMARK 465     ILE A   510
REMARK 465     PRO A   569
REMARK 465     ALA A   570
REMARK 465     TYR A   571
REMARK 465     GLU A   572
REMARK 465     LEU A   573
REMARK 465     GLU A   574
REMARK 465     THR A   575
REMARK 465     PRO A   576
REMARK 465     LEU A   577
REMARK 465     ASN A   578
REMARK 465     GLN A   579
REMARK 465     THR A   580
REMARK 465     ASP A   581
REMARK 465     ASN A   582
REMARK 465     THR A   583
REMARK 465     VAL A   584
REMARK 465     THR A   585
REMARK 465     VAL A   586
REMARK 465     MET A   587
REMARK 465     LEU A   588
REMARK 465     LYS A   589
REMARK 465     PRO A   590
REMARK 465     ALA A   591
REMARK 465     HIS A   592
REMARK 465     SER A   593
REMARK 465     ARG A   594
REMARK 465     GLY A   595
REMARK 465     ALA A   596
REMARK 465     PRO A   597
REMARK 465     VAL A   598
REMARK 465     SER A   599
REMARK 465     VAL A   600
REMARK 465     TYR A   601
REMARK 465     GLN A   602
REMARK 465     ILE A   603
REMARK 465     VAL A   604
REMARK 465     VAL A   605
REMARK 465     GLU A   606
REMARK 465     GLU A   607
REMARK 465     GLU A   608
REMARK 465     ARG A   609
REMARK 465     PRO A   610
REMARK 465     ARG A   611
REMARK 465     ARG A   612
REMARK 465     THR A   613
REMARK 465     LYS A   614
REMARK 465     LYS A   615
REMARK 465     THR A   616
REMARK 465     THR A   617
REMARK 465     GLU A   618
REMARK 465     ILE A   619
REMARK 465     LEU A   620
REMARK 465     LYS A   621
REMARK 465     CYS A   622
REMARK 465     TYR A   623
REMARK 465     PRO A   624
REMARK 465     VAL A   625
REMARK 465     PRO A   626
REMARK 465     ILE A   627
REMARK 465     HIS A   628
REMARK 465     PHE A   629
REMARK 465     GLN A   630
REMARK 465     ASN A   631
REMARK 465     ALA A   632
REMARK 465     SER A   633
REMARK 465     LEU A   634
REMARK 465     LEU A   635
REMARK 465     ASN A   636
REMARK 465     SER A   637
REMARK 465     GLN A   638
REMARK 465     TYR A   639
REMARK 465     TYR A   640
REMARK 465     PHE A   641
REMARK 465     ALA A   642
REMARK 465     ALA A   643
REMARK 465     GLU A   644
REMARK 465     PHE A   645
REMARK 465     PRO A   646
REMARK 465     ALA A   647
REMARK 465     ASP A   648
REMARK 465     SER A   649
REMARK 465     LEU A   650
REMARK 465     GLN A   651
REMARK 465     ALA A   652
REMARK 465     ALA A   653
REMARK 465     GLN A   654
REMARK 465     PRO A   655
REMARK 465     PHE A   656
REMARK 465     THR A   657
REMARK 465     ILE A   658
REMARK 465     GLY A   659
REMARK 465     ASP A   660
REMARK 465     ASN A   661
REMARK 465     LYS A   662
REMARK 465     THR A   663
REMARK 465     TYR A   664
REMARK 465     ASN A   665
REMARK 465     GLY A   666
REMARK 465     TYR A   667
REMARK 465     TRP A   668
REMARK 465     ASN A   669
REMARK 465     THR A   670
REMARK 465     PRO A   671
REMARK 465     LEU A   672
REMARK 465     LEU A   673
REMARK 465     PRO A   674
REMARK 465     TYR A   675
REMARK 465     LYS A   676
REMARK 465     SER A   677
REMARK 465     TYR A   678
REMARK 465     ARG A   679
REMARK 465     ILE A   680
REMARK 465     TYR A   681
REMARK 465     PHE A   682
REMARK 465     GLN A   683
REMARK 465     ALA A   684
REMARK 465     ALA A   685
REMARK 465     SER A   686
REMARK 465     ARG A   687
REMARK 465     ALA A   688
REMARK 465     ASN A   689
REMARK 465     GLY A   690
REMARK 465     GLU A   691
REMARK 465     THR A   692
REMARK 465     LYS A   693
REMARK 465     ILE A   694
REMARK 465     ASP A   695
REMARK 465     CYS A   696
REMARK 465     VAL A   697
REMARK 465     GLN A   698
REMARK 465     VAL A   699
REMARK 465     ALA A   700
REMARK 465     THR A   701
REMARK 465     LYS A   702
REMARK 465     GLY A   703
REMARK 465     ALA A   704
REMARK 465     ALA A   705
REMARK 465     THR A   706
REMARK 465     PRO A   707
REMARK 465     LYS A   708
REMARK 465     PRO A   709
REMARK 465     VAL A   710
REMARK 465     PRO A   711
REMARK 465     GLU A   712
REMARK 465     PRO A   713
REMARK 465     GLU A   714
REMARK 465     LYS A   715
REMARK 465     GLN A   716
REMARK 465     THR A   717
REMARK 465     ASP A   718
REMARK 465     HIS A   719
REMARK 465     THR A   720
REMARK 465     VAL A   721
REMARK 465     LYS A   722
REMARK 465     GLY A   723
REMARK 465     THR A   724
REMARK 465     LYS A   725
REMARK 465     HIS A   726
REMARK 465     HIS A   727
REMARK 465     HIS A   728
REMARK 465     HIS A   729
REMARK 465     HIS A   730
REMARK 465     HIS A   731
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     THR A   2    OG1  CG2
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    PHE A   3       50.14   -111.76
REMARK 500    ASP A  24     -152.02   -108.67
REMARK 500    THR A  35      -49.92   -130.11
REMARK 500    LYS A  70       57.52   -150.34
REMARK 500    LYS A  86     -105.79     96.44
REMARK 500    SER A  87     -119.88    -67.08
REMARK 500    ASN A  88       28.93   -149.53
REMARK 500    ASN A 111      142.67   -173.83
REMARK 500    THR A 117       -0.16   -150.85
REMARK 500    ARG A 118       43.53     33.37
REMARK 500    ALA A 126       78.11   -111.30
REMARK 500    SER A 128       64.25   -101.16
REMARK 500    GLN A 147       63.39   -118.60
REMARK 500    ASP A 153      -33.86   -135.82
REMARK 500    ASN A 229       63.65     36.13
REMARK 500    LEU A 278      101.11   -169.24
REMARK 500    ASN A 283      -72.12    -75.83
REMARK 500    ALA A 284       24.82     32.99
REMARK 500    SER A 306      -63.55    -11.19
REMARK 500    PRO A 325      -92.53    -44.85
REMARK 500    LEU A 366       91.89    -68.24
REMARK 500    PRO A 382      173.40    -59.90
REMARK 500    PHE A 383      -63.52   -142.66
REMARK 500    CYS A 390      130.84   -177.37
REMARK 500    VAL A 403       83.95   -153.15
REMARK 500    HIS A 421       62.73     61.90
REMARK 500    ILE A 470       84.71    -66.59
REMARK 500    GLU A 477       -8.75     74.09
REMARK 500    THR A 487      -35.15    -37.42
REMARK 500    PHE A 506       91.26    -67.82
REMARK 500    GLN A 515       73.32   -158.73
REMARK 500    THR A 526       65.23   -106.50
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 PHE A  530     PHE A  531                 -145.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A1576  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  24   OD1
REMARK 620 2 ASN A  27   OD1 118.1
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1569
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1570
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1571
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1573
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1574
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1575
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1576
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1577
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RPM   RELATED DB: PDB
REMARK 900  HUMAN RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU
REMARK 900  , DOMAIN 1
REMARK 900 RELATED ID: 2C9A   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF
REMARK 900   RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU
DBREF  2V5Y A    1   722  UNP    P28827   PTPRM_HUMAN     21    742
DBREF  2V5Y A  723   731  PDB    2V5Y     2V5Y           723    731
SEQADV 2V5Y PHE A   48  UNP  P28827    LEU    68 CONFLICT
SEQRES   1 A  731  GLU THR PHE SER GLY GLY CYS LEU PHE ASP GLU PRO TYR
SEQRES   2 A  731  SER THR CYS GLY TYR SER GLN SER GLU GLY ASP ASP PHE
SEQRES   3 A  731  ASN TRP GLU GLN VAL ASN THR LEU THR LYS PRO THR SER
SEQRES   4 A  731  ASP PRO TRP MET PRO SER GLY SER PHE MET LEU VAL ASN
SEQRES   5 A  731  ALA SER GLY ARG PRO GLU GLY GLN ARG ALA HIS LEU LEU
SEQRES   6 A  731  LEU PRO GLN LEU LYS GLU ASN ASP THR HIS CYS ILE ASP
SEQRES   7 A  731  PHE HIS TYR PHE VAL SER SER LYS SER ASN SER PRO PRO
SEQRES   8 A  731  GLY LEU LEU ASN VAL TYR VAL LYS VAL ASN ASN GLY PRO
SEQRES   9 A  731  LEU GLY ASN PRO ILE TRP ASN ILE SER GLY ASP PRO THR
SEQRES  10 A  731  ARG THR TRP ASN ARG ALA GLU LEU ALA ILE SER THR PHE
SEQRES  11 A  731  TRP PRO ASN PHE TYR GLN VAL ILE PHE GLU VAL ILE THR
SEQRES  12 A  731  SER GLY HIS GLN GLY TYR LEU ALA ILE ASP GLU VAL LYS
SEQRES  13 A  731  VAL LEU GLY HIS PRO CYS THR ARG THR PRO HIS PHE LEU
SEQRES  14 A  731  ARG ILE GLN ASN VAL GLU VAL ASN ALA GLY GLN PHE ALA
SEQRES  15 A  731  THR PHE GLN CYS SER ALA ILE GLY ARG THR VAL ALA GLY
SEQRES  16 A  731  ASP ARG LEU TRP LEU GLN GLY ILE ASP VAL ARG ASP ALA
SEQRES  17 A  731  PRO LEU LYS GLU ILE LYS VAL THR SER SER ARG ARG PHE
SEQRES  18 A  731  ILE ALA SER PHE ASN VAL VAL ASN THR THR LYS ARG ASP
SEQRES  19 A  731  ALA GLY LYS TYR ARG CYS MET ILE ARG THR GLU GLY GLY
SEQRES  20 A  731  VAL GLY ILE SER ASN TYR ALA GLU LEU VAL VAL LYS GLU
SEQRES  21 A  731  PRO PRO VAL PRO ILE ALA PRO PRO GLN LEU ALA SER VAL
SEQRES  22 A  731  GLY ALA THR TYR LEU TRP ILE GLN LEU ASN ALA ASN SER
SEQRES  23 A  731  ILE ASN GLY ASP GLY PRO ILE VAL ALA ARG GLU VAL GLU
SEQRES  24 A  731  TYR CYS THR ALA SER GLY SER TRP ASN ASP ARG GLN PRO
SEQRES  25 A  731  VAL ASP SER THR SER TYR LYS ILE GLY HIS LEU ASP PRO
SEQRES  26 A  731  ASP THR GLU TYR GLU ILE SER VAL LEU LEU THR ARG PRO
SEQRES  27 A  731  GLY GLU GLY GLY THR GLY SER PRO GLY PRO ALA LEU ARG
SEQRES  28 A  731  THR ARG THR LYS CYS ALA ASP PRO MET ARG GLY PRO ARG
SEQRES  29 A  731  LYS LEU GLU VAL VAL GLU VAL LYS SER ARG GLN ILE THR
SEQRES  30 A  731  ILE ARG TRP GLU PRO PHE GLY TYR ASN VAL THR ARG CYS
SEQRES  31 A  731  HIS SER TYR ASN LEU THR VAL HIS TYR CYS TYR GLN VAL
SEQRES  32 A  731  GLY GLY GLN GLU GLN VAL ARG GLU GLU VAL SER TRP ASP
SEQRES  33 A  731  THR GLU ASN SER HIS PRO GLN HIS THR ILE THR ASN LEU
SEQRES  34 A  731  SER PRO TYR THR ASN VAL SER VAL LYS LEU ILE LEU MET
SEQRES  35 A  731  ASN PRO GLU GLY ARG LYS GLU SER GLN GLU LEU ILE VAL
SEQRES  36 A  731  GLN THR ASP GLU ASP LEU PRO GLY ALA VAL PRO THR GLU
SEQRES  37 A  731  SER ILE GLN GLY SER THR PHE GLU GLU LYS ILE PHE LEU
SEQRES  38 A  731  GLN TRP ARG GLU PRO THR GLN THR TYR GLY VAL ILE THR
SEQRES  39 A  731  LEU TYR GLU ILE THR TYR LYS ALA VAL SER SER PHE ASP
SEQRES  40 A  731  PRO GLU ILE ASP LEU SER ASN GLN SER GLY ARG VAL SER
SEQRES  41 A  731  LYS LEU GLY ASN GLU THR HIS PHE LEU PHE PHE GLY LEU
SEQRES  42 A  731  TYR PRO GLY THR THR TYR SER PHE THR ILE ARG ALA SER
SEQRES  43 A  731  THR ALA LYS GLY PHE GLY PRO PRO ALA THR ASN GLN PHE
SEQRES  44 A  731  THR THR LYS ILE SER ALA PRO SER MET PRO ALA TYR GLU
SEQRES  45 A  731  LEU GLU THR PRO LEU ASN GLN THR ASP ASN THR VAL THR
SEQRES  46 A  731  VAL MET LEU LYS PRO ALA HIS SER ARG GLY ALA PRO VAL
SEQRES  47 A  731  SER VAL TYR GLN ILE VAL VAL GLU GLU GLU ARG PRO ARG
SEQRES  48 A  731  ARG THR LYS LYS THR THR GLU ILE LEU LYS CYS TYR PRO
SEQRES  49 A  731  VAL PRO ILE HIS PHE GLN ASN ALA SER LEU LEU ASN SER
SEQRES  50 A  731  GLN TYR TYR PHE ALA ALA GLU PHE PRO ALA ASP SER LEU
SEQRES  51 A  731  GLN ALA ALA GLN PRO PHE THR ILE GLY ASP ASN LYS THR
SEQRES  52 A  731  TYR ASN GLY TYR TRP ASN THR PRO LEU LEU PRO TYR LYS
SEQRES  53 A  731  SER TYR ARG ILE TYR PHE GLN ALA ALA SER ARG ALA ASN
SEQRES  54 A  731  GLY GLU THR LYS ILE ASP CYS VAL GLN VAL ALA THR LYS
SEQRES  55 A  731  GLY ALA ALA THR PRO LYS PRO VAL PRO GLU PRO GLU LYS
SEQRES  56 A  731  GLN THR ASP HIS THR VAL LYS GLY THR LYS HIS HIS HIS
SEQRES  57 A  731  HIS HIS HIS
HET    NAG  A1569      14
HET    NAG  A1570      14
HET    NAG  A1571      14
HET    NAG  A1572      14
HET    NAG  A1573      14
HET    NAG  A1574      14
HET    NAG  A1575      14
HET     NA  A1576       1
HET     NA  A1577       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      NA SODIUM ION
HETSYN     NAG NAG
FORMUL   2   NA    2(NA 1+)
FORMUL   3  NAG    7(C8 H15 N O6)
HELIX    1   1 PRO A   12  GLY A   17  5                                   6
HELIX    2   2 GLY A  384  ARG A  389  1                                   6
SHEET    1  AA 5 SER A  19  GLN A  20  0
SHEET    2  AA 5 ARG A  61  LEU A  69 -1  O  LEU A  65   N  SER A  19
SHEET    3  AA 5 TYR A 135  ILE A 142 -1  O  TYR A 135   N  LEU A  69
SHEET    4  AA 5 LEU A  94  VAL A 100 -1  O  ASN A  95   N  GLU A 140
SHEET    5  AA 5 TRP A 110  ILE A 112 -1  O  TRP A 110   N  VAL A  96
SHEET    1  AB 5 GLU A  29  VAL A  31  0
SHEET    2  AB 5 PHE A  48  VAL A  51 -1  O  PHE A  48   N  VAL A  31
SHEET    3  AB 5 LEU A 150  ILE A 152 -1  O  LEU A 150   N  VAL A  51
SHEET    4  AB 5 CYS A  76  VAL A  83 -1  O  PHE A  82   N  ALA A 151
SHEET    5  AB 5 LYS A 156  LEU A 158 -1  O  LYS A 156   N  ASP A  78
SHEET    1  AC 5 GLU A  29  VAL A  31  0
SHEET    2  AC 5 PHE A  48  VAL A  51 -1  O  PHE A  48   N  VAL A  31
SHEET    3  AC 5 LEU A 150  ILE A 152 -1  O  LEU A 150   N  VAL A  51
SHEET    4  AC 5 CYS A  76  VAL A  83 -1  O  PHE A  82   N  ALA A 151
SHEET    5  AC 5 ASN A 121  LEU A 125 -1  O  ASN A 121   N  TYR A  81
SHEET    1  AD 6 HIS A 167  PHE A 168  0
SHEET    2  AD 6 ALA A 182  ILE A 189 -1  O  ILE A 189   N  HIS A 167
SHEET    3  AD 6 PHE A 221  VAL A 227 -1  O  PHE A 221   N  ALA A 188
SHEET    4  AD 6 ALA A 208  VAL A 215 -1  O  PRO A 209   N  ASN A 226
SHEET    5  AD 6 ARG A 197  GLN A 201 -1  O  LEU A 198   N  LEU A 210
SHEET    6  AD 6 ARG A 239  ARG A 243 -1  O  ARG A 239   N  GLN A 201
SHEET    1  AE 2 VAL A 174  ASN A 177  0
SHEET    2  AE 2 LEU A 256  LYS A 259  1  O  VAL A 257   N  VAL A 176
SHEET    1  AF 3 GLN A 269  SER A 272  0
SHEET    2  AF 3 TYR A 277  GLN A 281 -1  O  TRP A 279   N  SER A 272
SHEET    3  AF 3 SER A 317  HIS A 322 -1  O  TYR A 318   N  ILE A 280
SHEET    1  AG 4 ASN A 308  PRO A 312  0
SHEET    2  AG 4 ALA A 295  THR A 302 -1  O  VAL A 298   N  GLN A 311
SHEET    3  AG 4 GLU A 328  THR A 336 -1  O  GLU A 330   N  CYS A 301
SHEET    4  AG 4 LEU A 350  ARG A 353 -1  O  LEU A 350   N  ILE A 331
SHEET    1  AH 3 ARG A 364  VAL A 371  0
SHEET    2  AH 3 ILE A 376  GLU A 381 -1  O  THR A 377   N  VAL A 369
SHEET    3  AH 3 GLN A 423  ILE A 426 -1  O  HIS A 424   N  ILE A 378
SHEET    1  AI 4 GLU A 407  SER A 414  0
SHEET    2  AI 4 ASN A 394  GLN A 402 -1  O  LEU A 395   N  SER A 414
SHEET    3  AI 4 ASN A 434  MET A 442 -1  O  SER A 436   N  CYS A 400
SHEET    4  AI 4 LEU A 453  GLN A 456 -1  O  LEU A 453   N  VAL A 437
SHEET    1  AJ 3 GLU A 407  SER A 414  0
SHEET    2  AJ 3 ASN A 394  GLN A 402 -1  O  LEU A 395   N  SER A 414
SHEET    3  AJ 3 ASN A 434  MET A 442 -1  O  SER A 436   N  CYS A 400
SHEET    1  AK 3 GLN A 471  PHE A 475  0
SHEET    2  AK 3 LYS A 478  GLN A 482 -1  O  LYS A 478   N  PHE A 475
SHEET    3  AK 3 HIS A 527  PHE A 530 -1  O  PHE A 528   N  LEU A 481
SHEET    1  AL 4 VAL A 519  LYS A 521  0
SHEET    2  AL 4 LEU A 495  SER A 504 -1  O  TYR A 496   N  LYS A 521
SHEET    3  AL 4 THR A 538  SER A 546 -1  O  THR A 538   N  VAL A 503
SHEET    4  AL 4 PRO A 554  THR A 560 -1  O  ALA A 555   N  ILE A 543
SSBOND   1 CYS A    7    CYS A   16                          1555   1555  2.05
SSBOND   2 CYS A   76    CYS A  162                          1555   1555  2.02
SSBOND   3 CYS A  186    CYS A  240                          1555   1555  2.04
SSBOND   4 CYS A  356    CYS A  390                          1555   1555  2.03
LINK         ND2 ASN A  52                 C1  NAG A1572     1555   1555  1.45
LINK         ND2 ASN A  72                 C1  NAG A1570     1555   1555  1.44
LINK         ND2 ASN A 111                 C1  NAG A1571     1555   1555  1.44
LINK         ND2 ASN A 386                 C1  NAG A1569     1555   1555  1.44
LINK         ND2 ASN A 394                 C1  NAG A1574     1555   1555  1.44
LINK         ND2 ASN A 434                 C1  NAG A1573     1555   1555  1.44
LINK         ND2 ASN A 524                 C1  NAG A1575     1555   1555  1.46
LINK        NA    NA A1576                 OD1 ASN A  27     1555   1555  2.45
LINK        NA    NA A1576                 OD1 ASP A  24     1555   1555  2.43
LINK        NA    NA A1577                 OD1 ASP A 153     1555   1555  2.59
CISPEP   1 SER A   85    LYS A   86          0        12.39
CISPEP   2 SER A  113    GLY A  114          0       -14.25
CISPEP   3 TRP A  131    PRO A  132          0         1.74
CISPEP   4 VAL A  403    GLY A  404          0       -24.70
CISPEP   5 ASP A  511    LEU A  512          0         5.92
CISPEP   6 SER A  567    MET A  568          0       -10.78
SITE     1 AC1  2 GLU A  22  ASN A 386
SITE     1 AC2  3 LYS A  70  ASN A  72  TRP A 131
SITE     1 AC3  4 ASN A 111  ILE A 112  SER A 113  ARG A 243
SITE     1 AC4  5 GLU A  29  MET A  43  ASN A  52  SER A  54
SITE     2 AC4  5 TYR A 149
SITE     1 AC5  3 TYR A 432  ASN A 434  GLN A 456
SITE     1 AC6  5 SER A 392  TYR A 393  ASN A 394  ASN A 443
SITE     2 AC6  5 PRO A 444
SITE     1 AC7  5 ASN A 285  SER A 286  LEU A 522  ASN A 524
SITE     2 AC7  5 GLU A 525
SITE     1 AC8  4 SER A  21  ASP A  24  PHE A  26  ASN A  27
SITE     1 AC9  3 LEU A   8  SER A  47  ASP A 153
CRYST1  167.336   69.325   97.487  90.00 113.52  90.00 C 1 2 1       4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.005976  0.000000  0.002601        0.00000
SCALE2      0.000000  0.014425  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011187        0.00000
      
PROCHECK
Go to PROCHECK summary
 References