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PDBsum entry 1g7f

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Hydrolase PDB id
1g7f
Jmol
Contents
Protein chain
297 a.a. *
Ligands
INZ
Waters ×462
* Residue conservation analysis
HEADER    HYDROLASE                               10-NOV-00   1G7F
TITLE     HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH PNU177496
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE
COMPND   3 1;
COMPND   4 CHAIN: A;
COMPND   5 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 1-298);
COMPND   6 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1B;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    HYDROLASE (PHOSPHORYLATION), TYROSINE PHOSPHATASE,
KEYWDS   2 INHIBITOR, COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.E.BLEASDALE,D.OGG,S.D.LARSEN
REVDAT   3   24-FEB-09 1G7F    1       VERSN
REVDAT   2   01-APR-03 1G7F    1       JRNL
REVDAT   1   06-JUN-01 1G7F    0
JRNL        AUTH   J.E.BLEASDALE,D.OGG,B.J.PALAZUK,C.S.JACOB,
JRNL        AUTH 2 M.L.SWANSON,X.Y.WANG,D.P.THOMPSON,R.A.CONRADI,
JRNL        AUTH 3 W.R.MATHEWS,A.L.LABORDE,C.W.STUCHLY,A.HEIJBEL,
JRNL        AUTH 4 K.BERGDAHL,C.A.BANNOW,C.W.SMITH,C.SVENSSON,
JRNL        AUTH 5 C.LILJEBRIS,H.J.SCHOSTAREZ,P.D.MAY,F.C.STEVENS,
JRNL        AUTH 6 S.D.LARSEN
JRNL        TITL   SMALL MOLECULE PEPTIDOMIMETICS CONTAINING A NOVEL
JRNL        TITL 2 PHOSPHOTYROSINE BIOISOSTERE INHIBIT PROTEIN
JRNL        TITL 3 TYROSINE PHOSPHATASE 1B AND AUGMENT INSULIN ACTION.
JRNL        REF    BIOCHEMISTRY                  V.  40  5642 2001
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11341829
JRNL        DOI    10.1021/BI002865V
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 32023
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1824
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2426
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 39
REMARK   3   SOLVENT ATOMS            : 462
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 11.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.011 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 0.024 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.901 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.695 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1G7F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-00.
REMARK 100 THE RCSB ID CODE IS RCSB012327.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-97
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SMART
REMARK 200  DATA SCALING SOFTWARE          : SAINT
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36586
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 5.790
REMARK 200  R MERGE                    (I) : 0.06700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.74
REMARK 200  R MERGE FOR SHELL          (I) : 0.34800
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: MERLOT
REMARK 200 STARTING MODEL: 1PTV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, MAGNESIUM ACETATE, HEPES,
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       26.19996
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.44840
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.80089
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.44840
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.19996
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.80089
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: 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     1
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   597     O    HOH A   789     2554     1.97
REMARK 500   O    HOH A   597     O    HOH A   673     2554     2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS A  32   CB    CYS A  32   SG      0.127
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 240   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES
REMARK 500    ASP A 252   N   -  CA  -  CB  ANGL. DEV. =  13.3 DEGREES
REMARK 500    ASP A 252   OD1 -  CG  -  OD2 ANGL. DEV. = -13.2 DEGREES
REMARK 500    ASP A 252   CB  -  CG  -  OD1 ANGL. DEV. =  15.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    HIS A  60       57.12    -91.00
REMARK 500    CYS A 215     -128.67   -137.80
REMARK 500    ILE A 219      -36.08   -134.02
REMARK 500    ILE A 261      100.05     78.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INZ A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G7G   RELATED DB: PDB
REMARK 900 1G7G CONTAINS THE SAME PROTEIN
DBREF  1G7F A    1   298  UNP    P18031   PTN1_HUMAN       1    298
SEQADV 1G7F ASP A  252  UNP  P18031    GLU   252 CONFLICT
SEQRES   1 A  298  MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES   2 A  298  GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES   3 A  298  ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES   4 A  298  ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES   5 A  298  ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES   6 A  298  TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES   7 A  298  ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES   8 A  298  CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES   9 A  298  ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES  10 A  298  SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES  11 A  298  LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES  12 A  298  LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES  13 A  298  GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES  14 A  298  GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES  15 A  298  GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES  16 A  298  PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES  17 A  298  GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG
SEQRES  18 A  298  SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES  19 A  298  MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES  20 A  298  LYS VAL LEU LEU ASP MET ARG LYS PHE ARG MET GLY LEU
SEQRES  21 A  298  ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES  22 A  298  VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES  23 A  298  VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP
HET    INZ  A 500      39
HETNAM     INZ 2-{4-[(2S)-2-[({[(1S)-1-CARBOXY-2-
HETNAM   2 INZ  PHENYLETHYL]AMINO}CARBONYL)AMINO]-3-OXO-3-
HETNAM   3 INZ  (PENTYLAMINO)PROPYL]PHENOXY}MALONIC ACID
FORMUL   2  INZ    C27 H33 N3 O9
FORMUL   3  HOH   *462(H2 O)
HELIX    1   1 GLU A    2  GLY A   14  1                                  13
HELIX    2   2 SER A   15  ALA A   27  1                                  13
HELIX    3   3 LEU A   37  ASN A   44  5                                   8
HELIX    4   4 PHE A   52  HIS A   54  5                                   3
HELIX    5   5 LEU A   88  ASN A   90  5                                   3
HELIX    6   6 THR A   91  LYS A  103  1                                  13
HELIX    7   7 PRO A  188  GLY A  202  1                                  15
HELIX    8   8 GLY A  220  LYS A  239  1                                  20
HELIX    9   9 ASP A  240  VAL A  244  5                                   5
HELIX   10  10 ASP A  245  ARG A  254  1                                  10
HELIX   11  11 THR A  263  GLY A  283  1                                  21
HELIX   12  12 SER A  286  SER A  295  1                                  10
SHEET    1   A 9 ARG A  56  LYS A  58  0
SHEET    2   A 9 TYR A  66  MET A  74 -1  N  ILE A  67   O  ILE A  57
SHEET    3   A 9 ARG A  79  THR A  84 -1  O  ARG A  79   N  MET A  74
SHEET    4   A 9 VAL A 211  HIS A 214  1  O  VAL A 211   N  ILE A  82
SHEET    5   A 9 GLY A 106  MET A 109  1  O  GLY A 106   N  VAL A 212
SHEET    6   A 9 GLU A 167  TYR A 176  1  O  LEU A 172   N  VAL A 107
SHEET    7   A 9 TYR A 153  ASN A 162 -1  O  THR A 154   N  HIS A 175
SHEET    8   A 9 LEU A 140  ILE A 149 -1  O  LYS A 141   N  GLU A 161
SHEET    9   A 9 MET A 133  PHE A 135 -1  N  MET A 133   O  LEU A 142
SHEET    1   B 2 MET A 114  GLU A 115  0
SHEET    2   B 2 SER A 118  LEU A 119 -1  O  SER A 118   N  GLU A 115
SITE     1 AC1 22 GLN A   9  ILE A  19  ASP A  22  TYR A  46
SITE     2 AC1 22 ARG A  47  ASP A  48  CYS A 215  SER A 216
SITE     3 AC1 22 ALA A 217  GLY A 220  ARG A 221  GLN A 262
SITE     4 AC1 22 GLN A 266  HOH A 514  HOH A 552  HOH A 556
SITE     5 AC1 22 HOH A 652  HOH A 708  HOH A 746  HOH A 872
SITE     6 AC1 22 HOH A 882  HOH A 921
CRYST1   52.740   83.820   88.660  90.00  90.00  90.00 P 21 21 21    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      0.019084  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011682  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011249        0.00000
      
PROCHECK
Go to PROCHECK summary
 References