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PDBsum entry 1zc0

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Hydrolase PDB id
1zc0
Jmol
Contents
Protein chain
286 a.a.
Ligands
PO4
Waters ×286
HEADER    HYDROLASE                               09-APR-05   1ZC0
TITLE     CRYSTAL STRUCTURE OF HUMAN HEMATOPOIETIC TYROSINE PHOSPHATASE (HEPTP)
TITLE    2 CATALYTIC DOMAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE, NON-RECEPTOR TYPE 7;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CATALYTIC PHOSPHATASE DOMAIN;
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE LC-PTP, HEMATOPOIETIC PROTEIN-
COMPND   6 TYROSINE PHOSPHATASE, HEPTP;
COMPND   7 EC: 3.1.3.48;
COMPND   8 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: PTPN7;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    HEPTP, HUMAN TYROSINE PHOSPHATASE CATALYTIC DOMAIN, LC-PTP, PTPN7,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.PAGE,T.MUSTELIN
REVDAT   3   13-JUL-11 1ZC0    1       VERSN
REVDAT   2   24-FEB-09 1ZC0    1       VERSN
REVDAT   1   06-DEC-05 1ZC0    0
JRNL        AUTH   T.MUSTELIN,L.TAUTZ,R.PAGE
JRNL        TITL   STRUCTURE OF THE HEMATOPOIETIC TYROSINE PHOSPHATASE (HEPTP)
JRNL        TITL 2 CATALYTIC DOMAIN: STRUCTURE OF A KIM PHOSPHATASE WITH
JRNL        TITL 3 PHOSPHATE BOUND AT THE ACTIVE SITE.
JRNL        REF    J.MOL.BIOL.                   V. 354   150 2005
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16226275
JRNL        DOI    10.1016/J.JMB.2005.09.049
REMARK   2
REMARK   2 RESOLUTION.    1.85 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) : 1.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 44913
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) : 0.163
REMARK   3   R VALUE            (WORKING SET) : 0.161
REMARK   3   FREE R VALUE                     : 0.186
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2398
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) : 1.85
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3214
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.33
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660
REMARK   3   BIN FREE R VALUE SET COUNT          : 196
REMARK   3   BIN FREE R VALUE                    : 0.3380
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2217
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 286
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) : 34.03
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.38000
REMARK   3    B22 (A**2) : -0.38000
REMARK   3    B33 (A**2) : 0.58000
REMARK   3    B12 (A**2) : -0.19000
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): 0.082
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.056
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.940
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2318 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3157 ; 1.329 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   284 ; 5.583 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   102 ;32.978 ;23.431
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   378 ;12.726 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;15.860 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   348 ; 0.089 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1768 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1097 ; 0.207 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1578 ; 0.311 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   259 ; 0.132 ; 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):    27 ; 0.218 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.186 ; 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):  1474 ; 1.849 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2328 ; 2.852 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   966 ; 4.216 ; 8.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   829 ; 6.336 ;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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
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    45        A   304
REMARK   3    ORIGIN FOR THE GROUP (A):  43.5730  44.1410   9.9030
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0380 T22:  -0.0060
REMARK   3      T33:  -0.0684 T12:   0.0358
REMARK   3      T13:   0.0293 T23:   0.0324
REMARK   3    L TENSOR
REMARK   3      L11:   1.6473 L22:   0.9277
REMARK   3      L33:   0.7164 L12:  -0.4070
REMARK   3      L13:   0.6076 L23:   0.0880
REMARK   3    S TENSOR
REMARK   3      S11:   0.0735 S12:  -0.0305 S13:  -0.1040
REMARK   3      S21:  -0.0585 S22:   0.0212 S23:   0.0500
REMARK   3      S31:  -0.0836 S32:  -0.1299 S33:  -0.0947
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 1ZC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032549.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 31-JUL-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.7
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797, 0.9791, 0.8856
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(111) BENT
REMARK 200                                   MONOCHROMATOR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47311
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : 8.300
REMARK 200  R MERGE                    (I) : 0.08000
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) : 1.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM/POTASSIUM PHOSPHATE, ACETATE,
REMARK 280  PH 6.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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
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       19.95433
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       39.90867
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       29.93150
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       49.88583
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        9.97717
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: 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 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     MET A    31
REMARK 465     GLY A    32
REMARK 465     SER A    33
REMARK 465     ASP A    34
REMARK 465     LYS A    35
REMARK 465     ILE A    36
REMARK 465     HIS A    37
REMARK 465     HIS A    38
REMARK 465     HIS A    39
REMARK 465     HIS A    40
REMARK 465     HIS A    41
REMARK 465     HIS A    42
REMARK 465     MET A    43
REMARK 465     ASN A    44
REMARK 465     GLY A   179
REMARK 465     LYS A   180
REMARK 465     GLU A   181
REMARK 465     LYS A   182
REMARK 465     GLU A   335
REMARK 465     GLU A   336
REMARK 465     PRO A   337
REMARK 465     SER A   338
REMARK 465     PRO A   339
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     ARG A  47    NE   CZ   NH1  NH2
REMARK 470     GLU A  48    CD   OE1  OE2
REMARK 470     GLN A  69    CG   CD   OE1  NE2
REMARK 470     GLU A  91    CD   OE1  OE2
REMARK 470     LYS A 105    CG   CD   CE   NZ
REMARK 470     GLN A 123    CG   CD   OE1  NE2
REMARK 470     GLU A 124    CD   OE1  OE2
REMARK 470     ASP A 125    CG   OD1  OD2
REMARK 470     LEU A 176    CG   CD1  CD2
REMARK 470     ARG A 177    CG   CD   NE   CZ   NH1  NH2
REMARK 470     CYS A 183    SG
REMARK 470     GLU A 190    CD   OE1  OE2
REMARK 470     GLU A 191    OE1  OE2
REMARK 470     GLU A 192    CG   CD   OE1  OE2
REMARK 470     ARG A 200    NE   CZ   NH1  NH2
REMARK 470     GLN A 202    CD   OE1  NE2
REMARK 470     LYS A 205    CE   NZ
REMARK 470     GLU A 206    CD   OE1  OE2
REMARK 470     GLU A 241    CD   OE1  OE2
REMARK 470     GLU A 255    CD   OE1  OE2
REMARK 470     GLU A 258    CG   CD   OE1  OE2
REMARK 470     THR A 259    OG1  CG2
REMARK 470     HIS A 262    CG   ND1  CD2  CE1  NE2
REMARK 470     GLU A 295    OE1  OE2
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 A  94       68.84   -112.55
REMARK 500    ASP A 125       42.22    -97.69
REMARK 500    GLU A 190      -59.99   -128.32
REMARK 500    GLN A 220     -122.69     50.68
REMARK 500    ILE A 274      -39.51   -133.17
REMARK 500    ILE A 313      108.33     68.38
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 650        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH A 682        DISTANCE =  5.16 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 436
DBREF  1ZC0 A   44   339  UNP    P35236   PTN7_HUMAN      65    360
SEQADV 1ZC0 MET A   31  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 GLY A   32  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 SER A   33  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 ASP A   34  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 LYS A   35  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 ILE A   36  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 HIS A   37  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 HIS A   38  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 HIS A   39  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 HIS A   40  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 HIS A   41  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 HIS A   42  UNP  P35236              LEADER SEQUENCE
SEQADV 1ZC0 MET A   43  UNP  P35236              LEADER SEQUENCE
SEQRES   1 A  309  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES   2 A  309  ASN THR PRO ARG GLU VAL THR LEU HIS PHE LEU ARG THR
SEQRES   3 A  309  ALA GLY HIS PRO LEU THR ARG TRP ALA LEU GLN ARG GLN
SEQRES   4 A  309  PRO PRO SER PRO LYS GLN LEU GLU GLU GLU PHE LEU LYS
SEQRES   5 A  309  ILE PRO SER ASN PHE VAL SER PRO GLU ASP LEU ASP ILE
SEQRES   6 A  309  PRO GLY HIS ALA SER LYS ASP ARG TYR LYS THR ILE LEU
SEQRES   7 A  309  PRO ASN PRO GLN SER ARG VAL CYS LEU GLY ARG ALA GLN
SEQRES   8 A  309  SER GLN GLU ASP GLY ASP TYR ILE ASN ALA ASN TYR ILE
SEQRES   9 A  309  ARG GLY TYR ASP GLY LYS GLU LYS VAL TYR ILE ALA THR
SEQRES  10 A  309  GLN GLY PRO MET PRO ASN THR VAL SER ASP PHE TRP GLU
SEQRES  11 A  309  MET VAL TRP GLN GLU GLU VAL SER LEU ILE VAL MET LEU
SEQRES  12 A  309  THR GLN LEU ARG GLU GLY LYS GLU LYS CYS VAL HIS TYR
SEQRES  13 A  309  TRP PRO THR GLU GLU GLU THR TYR GLY PRO PHE GLN ILE
SEQRES  14 A  309  ARG ILE GLN ASP MET LYS GLU CYS PRO GLU TYR THR VAL
SEQRES  15 A  309  ARG GLN LEU THR ILE GLN TYR GLN GLU GLU ARG ARG SER
SEQRES  16 A  309  VAL LYS HIS ILE LEU PHE SER ALA TRP PRO ASP HIS GLN
SEQRES  17 A  309  THR PRO GLU SER ALA GLY PRO LEU LEU ARG LEU VAL ALA
SEQRES  18 A  309  GLU VAL GLU GLU SER PRO GLU THR ALA ALA HIS PRO GLY
SEQRES  19 A  309  PRO ILE VAL VAL HIS CYS SER ALA GLY ILE GLY ARG THR
SEQRES  20 A  309  GLY CYS PHE ILE ALA THR ARG ILE GLY CYS GLN GLN LEU
SEQRES  21 A  309  LYS ALA ARG GLY GLU VAL ASP ILE LEU GLY ILE VAL CYS
SEQRES  22 A  309  GLN LEU ARG LEU ASP ARG GLY GLY MET ILE GLN THR ALA
SEQRES  23 A  309  GLU GLN TYR GLN PHE LEU HIS HIS THR LEU ALA LEU TYR
SEQRES  24 A  309  ALA GLY GLN LEU PRO GLU GLU PRO SER PRO
HET    PO4  A 436       5
HETNAM     PO4 PHOSPHATE ION
FORMUL   2  PO4    O4 P 3-
FORMUL   3  HOH   *286(H2 O)
HELIX    1   1 THR A   45  ALA A   57  1                                  13
HELIX    2   2 ARG A   63  GLN A   69  1                                   7
HELIX    3   3 SER A   72  ILE A   83  1                                  12
HELIX    4   4 SER A   89  LEU A   93  5                                   5
HELIX    5   5 GLY A   97  ASP A  102  5                                   6
HELIX    6   6 ASN A  110  GLN A  112  5                                   3
HELIX    7   7 GLY A  136  LYS A  140  5                                   5
HELIX    8   8 MET A  151  ASN A  153  5                                   3
HELIX    9   9 THR A  154  GLU A  165  1                                  12
HELIX   10  10 SER A  242  GLU A  255  1                                  14
HELIX   11  11 ILE A  274  GLY A  294  1                                  21
HELIX   12  12 ASP A  297  ARG A  309  1                                  13
HELIX   13  13 THR A  315  LEU A  333  1                                  19
SHEET    1   A 2 LEU A  61  THR A  62  0
SHEET    2   A 2 GLU A 295  VAL A 296 -1  O  VAL A 296   N  LEU A  61
SHEET    1   B 9 ARG A 114  CYS A 116  0
SHEET    2   B 9 TYR A 128  ILE A 134 -1  O  ALA A 131   N  VAL A 115
SHEET    3   B 9 TYR A 144  GLN A 148 -1  O  TYR A 144   N  ILE A 134
SHEET    4   B 9 ILE A 266  CYS A 270  1  O  VAL A 268   N  ILE A 145
SHEET    5   B 9 LEU A 169  LEU A 173  1  N  VAL A 171   O  VAL A 267
SHEET    6   B 9 GLU A 222  PHE A 231  1  O  ILE A 229   N  MET A 172
SHEET    7   B 9 TYR A 210  TYR A 219 -1  N  ARG A 213   O  HIS A 228
SHEET    8   B 9 PHE A 197  GLU A 206 -1  N  GLN A 202   O  GLN A 214
SHEET    9   B 9 GLU A 191  TYR A 194 -1  N  GLU A 192   O  ILE A 199
SITE     1 AC1 10 ASP A 236  CYS A 270  SER A 271  ALA A 272
SITE     2 AC1 10 ILE A 274  GLY A 275  ARG A 276  GLN A 314
SITE     3 AC1 10 HOH A 438  HOH A 578
CRYST1  127.101  127.101   59.863  90.00  90.00 120.00 P 61          6
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      0.007868  0.004542  0.000000        0.00000
SCALE2      0.000000  0.009085  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016705        0.00000
      
PROCHECK
Go to PROCHECK summary
 References